Patent Application: US-48837995-A

Abstract:
a purified preparation of a peptide consisting essentially of an amino acid sequence identical to that of a segment of a naturally - occurring human protein , said segment being of 10 to 30 residues in length , inclusive , wherein said peptide binds to a human major histocompatibility complex class ii allotype .

Description:
fig1 a - 1f are chromatographic analyses of the peptide pools extracted from papain digested hla - dr1 , dr2 , dr3 , dr4 , dr7 , and dr8 , respectively , illustrating the peptide repertoire of each hla - dr as detected by uv absorbance . the uv absorbance for both 210 nm and 277 nm is shown at a full scale absorbance of 500 mau with a retention window between 16 minutes and 90 minutes ( each mark represents 2 minutes ). fig2 is a representative mass spectrometric analysis of the size distribution of isolated hla - dr1 bound peptides . the determined peptide masses in groups of 100 mass units were plotted against the number of isolated peptides identified by mass spectrometry . peptide length was calculated by dividing the experimental mass by an average amino acid mass of 118 daltons . fig3 a is a representation of a minigene of the invention ( seq id no : 147 ), in which the hla - drα chain leader peptide is linked to the amino terminus of a 15 - residue blocking peptide fragment of human invariant chain ii . fig3 b is a representation of a second minigene of the invention ( seq id no : 148 ), in which the hla - drα chain leader peptide is linked to the amino terminus of a 24 - residue blocking peptide fragment of human invariant chain ii . hla - dr molecules were purified from homozygous , epstein - barr virus - transformed , human b lymphoblastoid lines : dr1 from lg - 2 cells , dr2 from mst cells , dr3 from wt20 cells , dr4 from priess cells , dr7 from mann cells , and dr8 from 23 . 1 cells . all of these cell lines are publicly available . cell growth , harvest conditions and protein purification were as previously described ( gorga , j . et al ., 1991 ). briefly , 200 grams of each cell type was resuspended in 10 mm tris - hcl , 1 mm dithiothreitol ( dtt ), 0 . 1 mm phenylmethylsulfonylflouride ( pmsf ), ph 8 . 0 , and lysed in a thomas homogenizer . the nuclei were removed by centrifugation at 4000 × g for 5 min and the pellets washed and repelleted until the supernatants were clear . all the supernatants were pooled and the membrane fraction harvested by centrifugation at 175 , 000 × g for 40 min . the pellets were then resuspended in 10 mm tris - hcl , 1 mm dtt , 1 mm pmsf , 4 % np - 40 . the unsolubilized membrane material was removed by centrifugation at 175 , 000 × g for 2 hours , and the np - 40 soluble supernatant fraction used in immunoaffinity purification . detergent soluble hla - dr was bound to a lb3 . 1 - protein a sepharose ™ agarose gel column ( pharmacia ; ( gorga et al ., id ) and eluted with 100 mm glycine , ph 11 . 5 . following elution , the sample was immediately neutralized by the addition of tris - hcl and then dialyzed against 10 mm tris - hcl , 0 . 1 % deoxycholic acid ( doc ). the lb3 . 1 monoclonal antibody recognizes a conformational determinant present on the nonpolymorphic hla - drα chain , and thus recognizes all allotypes of hla - dr . the transmembrane domain of the dr molecules was removed by papain digestion , and the resulting water - soluble molecule further purified by gel filtration chromatography on an s - 200 column equilibrated in 10 mm tris - hcl , ph 8 . 0 . the purified dr samples were concentrated by ultrafiltration , yield determined by bca assay , and analyzed by sds polyacrylamide gel electrophoresis . water - soluble , immunoaffinity - purified class ii molecules were further purified by high - performance size exclusion chromatography ( sec ), in 25 mm n - morpholino ethane sulfonic acid ( mes ) ph 6 . 5 and a flowrate of 1 ml / min ., to remove any residual small molecular weight contaminants . next , centricon ™ untrafiltration microconcentrators ( molecular weight cutoff 10 , 000 daltons ) ( amicon corp .) were sequentially washed using sec buffer and 10 % acetic acid prior to spin - concentration of the protein sample ( final volume between 100 - 200 μl ). peptide pools were extracted from chosen class ii alleles by the addition of 1 ml of 10 % acetic acid for 15 minutes at 70 ° c . these conditions are sufficient to free bound peptide from class ii molecules , yet mild enough to avoid peptide degradation . the peptide pool was separated from the class ii molecule after centrifugation through the centricon ™ ultrafiltration microcentrator with the flow - through containing the previously bound peptides . the collected acid - extracted peptide pool was concentrated in a speed - vac ™ vacuum equipped centrifuge ( savant ) to a volume of 50 μl prior to hplc separation . peptides were separated on a microbore c - 18 reversed - phase chromatography ( rpc ) column ( vydac ) utilizing the following non - linear gradient protocol at a constant flowrate of 0 . 15 ml / min . : 0 - 63 min . 5 %- 33 % buffer b ; 63 - 95 min . 33 %- 60 % buffer b ; 95 - 105 min 60 %- 80 % buffer b , where buffer a was 0 . 06 % trifluoroacetic acid / water and buffer b was 0 . 055 % trifluoroacetic acid / acetonitrile . chromatographic analysis was monitored at multiple uv wavelengths ( 210 , 254 , 277 , and 292 nm ) simultaneously , permitting spectrophotometric evaluation prior to mass and sequence analyses . shown in fig1 are chromatograms for each of the six dr peptide pools analyzed . collected fractions were subsequently analyzed by mass spectrometry and edman sequencing . the spectrophotometric evaluation of the peptides during rpc provides valuable information regarding amino acid composition ( contribution of aromatic amino acids ) and is used as a screening method for subsequent characterization . appropriate fractions collected during the rpc separation were next analyzed using a finnegan - mat lasermat ™ matrix - assisted laser - desorption mass spectrometer ( mald - ms ) to determine the individual mass values for the predominant peptides . between 1 %- 4 % of the collected fraction was mixed with matrix ( 1 ρl α - cyano - 4 - hydroxycinnamic acid ) to achieve mass determination of extracted peptides . the result of this analysis for hla - dr1 is shown in fig2 . next , chosen peptide samples were sequenced by automated edman degradation microsequencing using an abi 477a protein sequencer ( applied biosystems ) with carboxy - terminal verification provided by mass spectral analysis using the finnigan - mat tsq 700 triple quadruple mass spectrometer equipped with an electro - spray ion source . this parallel analysis ensures complete identity of peptide composition and sequence . peptide alignment with protein sequences stored in the swiss - prot database was performed using the fasta computer database search program . set forth in tables 1 - 10 are the results of this sequence analysis for each of the dr molecules studied . the hla - dr1 used in this study was papain solubilized to enable the material to be used both for crystallographic and bound peptide analyses . the peptides bound to dr1 were acid extracted and fractionated using rpc ( fig1 ). the absence of any detectable peptidic material following a second extraction / rpc separation verified quantitative peptide extraction . amino acid analysis ( abi 420a / 130a derivatizer / hplc ) of extracted peptide pools demonstrated a 70 - 80 % yield , assuming total occupancy of purified dr1 with a molar equivalent of bound peptides corresponding to the size distribution determined by mass spectrometry ( see fig2 ). the rpc profiles obtained from dr1 extractions of multiple independent preparations were reproducible . furthermore , profiles from either detergent - soluble or papain - solubilized dr1 were equivalent . to confirm that the peptides were in fact identical in detergent - soluble and papain - digested dr1 , mass spectrometry and edman sequencing analyses were performed and revealed identical masses and sequences for analogous fractions from the two preparations . matrix - assisted laser desorption mass spectrometry ( mald - ms ) was used to identify 111 species of unique mass contained within the eluted peptide pool of dr1 with an average size of 18 and a mode of 15 residues ( fig2 ). over 500 additional mass species present within the molecular weight range of 13 - 25 residues were detected ; however , the signal was not sufficient to assign individual masses with confidence . multiple species of varying mass were detected in fractions corresponding to single rpc peaks indicating co - elution of peptides . to characterize these peptides further , samples were analyzed in parallel on a triple quadruple mass spectrometer equipped with an electrospray ion source ( esi - ms ) and by automated edman degradation microsequencing ( lane et al ., j . prot . chem . 10 : 151 - 160 ( 1991 )). combining these two techniques permits crucial verification of both the n - and c - terminal amino acids of peptides contained in single fractions . the sequence and mass data acquired for twenty peptides isolated from dr1 are listed in table 1 . all the identified peptides aligned with complete identity to regions of proteins stored in the swiss - prot database . surprisingly , sixteen of the twenty sequenced dr1 - bound peptides were 100 % identical to regions of the self proteins hla - a2 and class ii - associated invariant chain ( ii ), representing at least 26 % of the total extracted peptide mass . these isolated peptides varied in length and were truncated at both the n - and c - termini , suggesting that : 1 ) antigen processing occurs from both ends after binding to dr1 , or 2 ) class ii molecules bind antigen from a pool of randomly generated peptides . the yields from the peptide microsequencing indicated that hla - a2 ( fig1 ) and ii each represents at least 13 % of the total dr1 - bound peptides . an additional surprising finding concerned a peptide which , although bound to hla - dr and 100 % homologous with hla - a2 peptide , was derived from a cell which does not express hla - a2 protein . evidently this peptide is derived from a protein containing a region homologous with a region of hla - a2 protein . thus , for purposes of this specification , the term &# 34 ; hla - a2 protein &# 34 ; is intended to include hla - a2 protein itself , as well as any naturally occurring protein which contains a ten or greater amino acid long region of & gt ; 80 % homology with an hla - dr - binding peptide derived from hla - a2 . an &# 34 ; hla - a2 peptide &# 34 ; similarly refers to peptides from any hla - a2 protein , as broadly defined herein . the other four peptides identified in the dr1 studies were derived from two self proteins , transferrin receptor and the na + / k + atpase , and one exogenous protein , bovine serum fetuin ( a protein present in the serum used to fortify the medium which bathes the cells ). each of these peptides occupied only 0 . 3 - 0 . 6 % of the total dr1 population , significantly less than either the hla - a2 or the ii peptides . it is known that class ii molecules en route to the cell surface intersect the pathway of incoming endocytic vesicles . both recycling membrane proteins and endocytosed exogenous protein travel this common pathway . hence , the hla - a2 , transferrin receptor , na + / k + atpase and bovine fetuin derived peptides would all encounter dr1 in a similar manner . ii associates with nascent class ii molecules in the endoplasmic reticulum ( er ) ( jones et al ., mol . immunol . 16 : 51 - 60 ( 1978 )), preventing antigen binding until the class ii / ii complex arrives at an endocytic compartment ( roche and cresswell , nature 345 : 615 - 618 ( 1990 )), where ii undergoes proteolysis ( thomas et al ., j . immunol . 140 : 2670 - 2675 ( 1988 ); roche and cresswell , proc . natl . acad . sci . usa 88 : 3150 - 3154 ( 1991 )), thus allowing peptide binding to proceed . presumably , the ii peptides bound to dr1 were generated at this step . synthetic peptides corresponding to five of the peptides reported in table 1 were made and their relative binding affinities to dr1 determined . the influenza a hemagglutinin peptide ( ha ) 307 - 319 ( seq id no : 24 ) has been previously described as a high affinity , hla - dr1 restricted peptide ( roche and cresswell , j . immunol . 144 : 1849 - 1856 ( 1990 ); rothbard et al ., cell 52 : 515 - 523 ( 1988 )), and was thus chosen as the control peptide . &# 34 ; empty &# 34 ; dr1 purified from insect cells expressing recombinant dr1 cdna was used in the binding experiments because of its higher binding capacity and 10 - fold faster association kinetics than dr1 isolated from human cells ( stern and wiley , cell 68 : 465 - 477 ( 1992 )). all the synthetic peptides were found to compete well ( ki & lt ; 100 nm ) against the ha peptide ( table 2 ). at first approximation , the ii 107 - 120 peptide ( seq id no : 156 ) had the highest affinity of all the competitor peptides measured , equivalent to that determined for the control ha peptide . in addition to the ki determinations , these peptides were found to confer resistance to sds - induced α - β chain dissociation of &# 34 ; empty &# 34 ; dr1 when analyzed by sds - page , indicative of stable peptide binding ( sadegh - nasseri and germain , nature 353 : 167 - 170 ( 1991 ); dornmair et al ., cold spring harbor symp . quant . biol . 54 : 409 - 415 ( 1989 ); springer et al ., j . biol . chem . 252 : 6201 - 6207 ( 1977 )). neither of the two control peptides , β 2 m 52 - 64 ( seq id no : 26 ) nor ii 97 - 111 ( seq id no : 25 ), was able to either confer resistance to sds - induced chain dissociation of dr1 or compete with ha 307 - 319 ( seq id no : 24 ) for binding to dr1 ; both of these peptides lack the putative binding motif reported in this study ( see below ). a putative dr1 binding motif based on the sequence alignments of the core epitopes ( the minimum length ) of certain naturally processed peptides is shown in table 3 . the peptides listed in this table include those determined herein for hla - dr1 , as well as a number of peptides identified by others and known to bind dr1 ( reference # 6 in this table being o &# 39 ; sullivan et al ., j . immunol . 145 : 1799 - 1808 , 1990 ; reference # 17 , roche & amp ; cresswell , j . immunol . 144 : 1849 - 1856 , 1990 ; reference # 25 , guttinger et al ., intern . immunol . 3 : 899 - 906 , 1991 ; reference # 27 , guttinger et al . embo j . 7 : 2555 - 2558 , 1988 ; and reference # 28 , harris et al ., j . immunol . 148 : 2169 - 2174 , 1992 ). the key residues proposed in the motif are as follows : a positively charged group is located at the first position , referred to here as the index position for orientation ( i ); a hydrogen bond donor is located at i + 5 ; and a hydrophobic residue is at i + 9 . in addition , a hydrophobic residue is often found at i + 1 and / or i - 1 . every naturally processed peptide sequenced from dr1 conforms to this motif ( with the exception of the hla - a2 peptide 103 - 116 ( seq id no : 3 ) that lacks residue i + 9 ). because the putative motif is not placed in a defined position with respect to the first amino acid and because of the irregular length of bound peptides , it is impossible to deduce a motif from sequencing of peptide pools , as was done for class i molecules ( falk et al ., nature 351 : 290 - 296 ( 1991 )). the ii 97 - 111 peptide ( seq id no : 25 ), a negative control peptide used in binding experiments , has the i and i + 5 motif residues within its sequence , but is missing eight additional amino acids found in ii 106 - 119 ( seq id no : 16 ) ( table 3c ). a sequence comparison of 35 previously described dr1 - binding synthetic peptides ( o &# 39 ; sullivan et al ., j . immunol . 145 : 1799 - 1808 ( 1990 ); guttinger et al ., intern . immunol . 3 : 899 - 906 ( 1991 ); hill et al ., j . immunol . 147 : 189 - 197 ( 1991 ); guttinger et al ., embo j . 7 : 2555 - 2558 ( 1988 ); harris et al ., j . immunol . 148 : 2169 - 2174 ( 1992 )) also supports this motif of the 35 synthetic peptides , 21 ( 60 %) have the precise motif , nine ( 30 %) contain a single shift at either i or i + 9 , and the remaining five ( 10 %) have a single substitution at i ( table 3b and c ). interestingly , in the latter peptides , a positive charge at i is always replaced by a large hydrophobic residue ( table 8c ); a pocket has been described in class i molecules that can accommodate this precise substitution ( latron et al ., proc . natl . acad . sci . usa 88 : 11325 - 11329 ( 1991 )). contributions by the other eight amino acids within the motif or the length of the peptide have not been fully evaluated and may compensate for shifted / missing residues in those peptides exhibiting binding . evaluation of the remaining 117 non - dr1 binding peptides cited in those studies ( which peptides are not included in table 3 ) indicates that 99 ( 85 %) of these peptides do not contain the dr1 motif proposed herein of the remaining 18 peptides ( 15 %) that do not bind to dr1 but which do contain the motif , 6 ( 5 %) are known to bind to other dr allotypes ; the remaining 12 peptides may have unfavorable interactions at other positions which interfere with binding . in contrast to the precise n - terminal cleavages observed in the previous study of six peptides bound to the mouse class ii antigen termed i - a b and five bound to mouse i - e b ( rudensky et al ., nature 3563 : 622 - 627 ( 1991 )), the peptides bound to dr1 are heterogeneous at both the n - and c - termini . in contrast to peptides bound to class i molecules , which are predominantly nonamers ( van bleek and nathenson , nature 348 : 213 - 216 ( 1990 ); rotzschke et al ., nature 348 : 252 - 254 ( 1990 ); jardetzky et al ., nature 353 : 326 - 329 ( 1991 ); hunt et al ., science 255 : 1261 - 1263 ( 1992 )), class ii peptides are larger and display a high degree of heterogeneity both in length and the site of terminal truncation , implying that the mechanisms of processing for class i and class ii peptides are substantially different . furthermore , the present results suggest that class ii processing is a stochastic event and that a dr allotype may bind peptides of different lengths from a complex random mixture . the heterogeneity observed may be solely due to protection of bound peptides from further degradation . thus , class ii molecules would play an active role in antigen processing ( as previously proposed ( donermeyer and allen , j . immunol . 142 : 1063 - 1068 ( 1989 )) by protecting the bound peptides from complete degradation . alternatively , the predominance of 15 mers bound to dr1 ( as detected by both the mald - ms and the yields of sequenced peptides ) could be the result of trimming of bound peptides . in any event , the absence of detectable amounts of peptides shorter than 13 and longer than 25 residues suggests that there are length constraints intrinsic either to the mechanism of peptide binding or to antigen processing . the predominance of peptides bound to dr1 that are derived from endogenously synthesized proteins , and particularly mhc - related proteins , may result from the evolution of a mechanism for presentation of self peptides in connection with the generation of self tolerance . the sequences of naturally processed peptides eluted from each of dr2 , dr3 , dr4 , dr7 and dr8 are shown in tables 4 - 8 , respectively . in addition to those peptides shown in table 4 , it has been found that dr2 binds to long fragments of hla - dr2a β - chain and hla - dr2b β - chain , corresponding to residues 1 - 126 or 127 of each of those proteins . presumably , only a short segment of those long fragments is actually bound within the groove of dr2 , with the remainder of each fragment protruding from one or both ends of the groove . table 9 gives sequences of dr1 from another cell line which does not have wild - type ar , but which has bound a2 - like peptides . table 10 gives sequences of peptides eluted from dr4 and dr11 molecules expressed in cells from a human spleen . these data demonstrate the great prevalence of self peptides bound , compared to exogenous peptides . the data also show that the a2 and ii peptides occur repeatedly . in addition , certain of the tables include peptides that appear to derive from viral proteins , such as epstein - barr virus major capsid protein , which are likely to be present in the cells studied . in order to prepare genetic constructs for in vivo administration of genes encoding immunomodulatory peptides of the invention , the following procedure is carried out . overlapping synthetic oligonucleotides were used to generate the leader peptide / blocking peptide mini - genes illustrated in fig3 by pcr amplification from human hla - drα and invariant chain cdna templates . these mini - genes encode the ii peptide fragments kmrmatpllmqalpm ( or ii 15 ; seq id no : 15 ) and lpkppkpvskmrmatpllmqalpm ( or ii 24 ; seq id no : 7 ). the resulting constructs were cloned into pgem - 2 ( promega corp .) to form the plasmids pgem - 2 - α - ii 15 and pgem - 2 - α - ii 24 , with an upstream t7 promoter for use in the in vitro transcription / translation system described below . for in vivo expression , each mini - gene was subsequently subcloned from the pgem - 2 derivatives into a transfection vector , phβactin - 1 - neo ( gunning et al ., ( 1987 ) proc . natl . acad . sci . u . s . a . 84 : 4831 ), to form the plasmids phβactin - α - ii 15 and phβactin - α - ii 24 . the inserted mini - genes are thus expressed in vivo from the constitutive / strong human β actin promoter . in addition , the mini - genes were subcloned from the pgem - 2 derivatives into the vaccinia virus recombination vector psc11 ( s . chakrabarti et al . ( 1985 ) mol . cell . biol . 5 , 3403 - 3409 ) to form the plasmids psc11 - α - ii 15 and psc11 - α - ii 24 . following recombination into the viral genome the inserted mini - genes are expressed from the strong vaccinia p 7 . 5 promoter . short amino acid sequences can act as signals to target proteins to specific intracellular compartments . for example , hydrophobic signal peptides are found at the amino terminus of proteins destined for the er , while the sequence kferq ( seq id no : 153 ) ( and other closely related sequences ) is known to target intracellular polypeptides to lysosomes , while other sequences target polypeptides to endosomes . in addition , the peptide sequence kdel ( seq id no : 152 ) has been shown to act as a retention signal for the er . each of these signal peptides , or a combination thereof , can be used to traffic the immunomodulating peptides of the invention as desired . for example , a construct encoding a given immunomodulating peptide linked to an er - targeting signal peptide would direct the peptide to the er , where it would bind to the class ii molecule as it is assembled , preventing the binding of intact ii which is essential for trafficking . alternatively , a construct can be made in which an er retention signal on the peptide would help prevent the class ii molecule from ever leaving the er . if instead a peptide of the invention is targeted to the endosomic compartment , this would ensure that large quantities of the peptide are present when invariant chain is replaced by processed peptides , thereby increasing the likelihood that the peptide incorporated into the class ii complex is the high - affinity peptides of the invention rather than naturally - occurring , potentially immunogenic peptides . the likelihood of peptides of the invention being available incorporation into class ii can be increased by linking the peptides to an intact ii polypeptide sequence . since ii is known to traffic class ii molecules to the endosomes , the hybrid ii would carry one or more copies of the peptide of the invention along with the class ii molecule ; once in the endosome , the hybrid ii would be degraded by normal endosomal processes to yield both multiple copies of the peptide of the invention or molecules similar to it , and an open class ii binding cleft . dnas encoding immunomodulatory peptides containing targeting signals will be generated by pcr or other standard genetic engineering or synthetic techniques , and the ability of these peptides to associate with dr molecules will be analyzed in vitro and in vivo , as described below . it is proposed that the invariant chain prevents class ii molecules from binding peptides in the er and may contribute to heterodimer formation . any mechanism that prevents this association would increase the effectiveness of class ii blockade . therefore , a peptide corresponding to the site on ii which binds to the class ii heterodimer , or corresponding to the site on either the α or β subunit of the heterodimer which binds to ii , could be used to prevent this association and thereby disrupt mhc class ii function . cell free extracts are used routinely for expressing eukaryotic proteins ( krieg , p . & amp ; melton , d . ( 1984 ) nucl . acids res . 12 , 7057 ; pelham , h . and jackson , r . ( 1976 ) eur . j . biochem . 67 , 247 ). specific mrnas are transcribed from dna vectors containing viral rna polymerase promoters ( melton , d . et al . ( 1984 ) nucl . acids res . 12 , 7035 ), and added to micrococcal nuclease - treated cell extracts . the addition of 35 s methionine and amino acids initiates translation of the exogenous mrna , resulting in labeled protein . proteins may be subsequently analyzed by sds - page and detected by autoradiography . processing events such as signal peptide cleavage and core glycosylation are initiated by the addition of microsomal vesicles during translation ( walter , p . and blobel , g . ( 1983 ), meth . enzymol ., 96 , 50 ), and these events are monitored by the altered mobility of the proteins in sds - page gels . the ability of peptides containing a signal peptide sequence to be accurately processed and to compete with invariant chain for class ii binding in the er are assayed in the in vitro system described above . specifically , dr1 α - and β - chain and invariant chain peptide constructs described above are transcribed into mrnas , which will be translated in the presence of mammalian microsomal membranes . association of the dr heterodimer with ii is determined by immunoprecipitation with antisera to dr and ii . addition of mrna encoding the peptide of the invention to the translation reaction should result in a decreased level of coimmunoprecipitated ii , and the concomitant appearance of coimmunoprecipitated peptide , as determined by sds - page on tris - tricine gels . these experiments will provide a rapid assay system for determining the potential usefulness of a given blocking peptide as a competitor for ii chain binding in the er . those peptides of the invention which prove to be capable of competing successfully with ii in this cell - free assay can then be tested in intact cells , as described below . human ebv - transformed b cell lines lg - 2 and hom - 2 ( homozygous for hla - dr1 ) and the mouse b cell hybridoma lk35 . 2 are transfected with either 50 μg of linearized phβactin - α - ii 15 or phβactin - α - ii 24 or ( as a control ) phβactin - 1 - neo by electroporation ( 150 mv , 960 μf , 0 . 2 cm cuvette gap ). following electroporation , the cells are cultured in g418 - free medium until total recovery ( approximately 4 days ). each population is then placed under g418 selection until neomycin - expressing resistant populations of transfectants are obtained ( approximately 1 - 2 months ). the resistant populations are subcloned by limiting dilution and the clonality of stable transfectants determined by pcr amplification of blocking peptide mrna expression . stable transfectants of lg - 2 and hom - 2 carrying blocking peptide mini - genes or negative control vectors are grown in large - scale culture conditions until 20 grams of pelleted cell mass is obtained . the hla - dr expressed by each transfectant is purified , and the bound peptide repertoire ( both from within the cell and from the cell surface ) analyzed as described above . successful demonstration of a reduction in the total bound peptide diversity will be conclusive evidence of intracellular delivery of immunomodulatory peptides . a second cell - based assay utilizes stable transfectants of lk35 . 2 cells carrying blocking peptide mini - genes or negative control vectors ; these cells are used as apcs in t cell proliferation assays . each transfectant is cultured for 24 hours in the presence of different dilutions of hen egg lysozyme ( hel ) and hel - specific t cell hybridomas . the relative activation of the t cells present in each assay ( as measured by lymphokine production ) is determined using the publicly available lymphokine dependent cell line ctll2 in a 3 h - thymidine incorporation assay ( vignali et al . ( 1992 ) j . e . m . 175 : 925 - 932 ). successful demonstration of a reduction in the ability of blocking peptide expressing transfectants to present hel to specific t cell hybridomas will be conclusive evidence of intracellular delivery of immuno - modulatory peptides . cells of the human tk - cell line 143 ( atcc ) are infected with vaccinia virus ( strain wr , tk + ) ( atcc ), and two hours postinfection , psc11 - α - ii 15 or psc11 - α - ii 24 or psc11 is introduced into the infected cells by calcium phosphate precipitation . tk - recombinants are selected for with bromodeoxyuridine at 25 μg / ml . recombinant plaques are screened by pcr for the presence of mini - gene dna . recombinant virus is cloned by three rounds of limiting dilution to generate pure clonal viral stocks . in experiments analogous to the transfection experiments described above , recombinant vaccinia viruses encoding mini - genes or vector alone will be used to infect large - scale cultures of the human ebv transformed b cell lines lg - 2 and hom - 2 . following infection , the hla - dr is purified and the bound peptide repertoire analyzed as described above . a reduction of the complexity of the bound peptide population and a significant increase in the relative amount of ii peptides bound are conclusive evidence that vaccinia can deliver blocking peptides to human apcs . the same recombinant vaccinia viruses encoding mini - genes or vector will be used to infect mice experiencing experimentally - induced autoimmunity . a number of such models are known and are referred in kronenberg , cell 65 : 537 - 542 ( 1991 ). liposomes have been successfully used as drug carriers and more recently in safe and potent adjuvant strategies for malaria vaccination in humans ( fries et al . ( 1992 ), proc . natl . acad . sci . usa 89 : 358 ). encapsulated liposomes have been shown to incorporate soluble proteins and deliver these antigens to cells for both in vitro and in vivo cd8 + mediated ctl response ( reddy et al ., j . immunol . 148 : 1585 - 1589 , 1992 ; and collins et al ., j . immunol . 148 : 3336 - 3341 , 1992 ). thus , liposomes may be used as a vehicle for delivering synthetic peptides into apcs . harding et al . ( cell ( 1991 ) 64 , 393 - 401 ) have demonstrated that the targeting of liposome - delivered antigen to either of two intracellular class ii - loading compartments , early endosomes and / or lysosomes , can be accomplished by varying the membrane composition of the liposome : acid - sensitive liposomes were found to target their contents to early endosomes , while acid - resistant liposomes were found to deliver their contents to lysosomes . thus , the peptides of the invention will be incorporated into acid - sensitive liposomes where delivery to endosomes is desired , and into acid - resistant liposomes for delivery to lysosomes . liposomes are prepared by standard detergent dialysis or dehydration - rehydration methods . for acid - sensitive liposomes , dioleoylphosphatidylethanolamine ( dope ) and palmitoylhomocystein ( phc ) are utilized , while dioleoylphospatidylcholine ( dopc ) and dioleoylphosphatidylserine ( dops ) are used for the preparation of acid - resistant liposomes . 10 - 5 mol of total lipid ( dopc / dops or dope / phc at 4 : 1 mol ratios ) are dried , hydrated in 0 . 2 ml of hepes buffered saline ( hbs ) ( 150 mm nacl , 1 mm egta , 10 mm hepes ph 7 . 4 ) and sonicated . the lipid suspensions are solubilized by the addition of 0 . 1 ml of 1m octylglucoside in hbs . the peptides to be entrapped are added to 0 . 2 ml of 0 . 6 mm peptide in 20 % hbs . the mixture is then frozen , lyophilized overnight , and rehydrated . these liposomes will be treated with chymotrypsin to digest any surface - bound peptide . liposome delivery to ebv - transformed cell lines ( as described above ) will be accomplished by 12 - 16 hour incubation at 37 ° c . hla - dr will be purified from the liposome treated cells and bound peptide analyzed as above . alternatively , the liposomes are formulated with the dna mini - gene constructs of the invention , and used to deliver the constructs into apcs either in vitro or in vivo . human immunization will be carried out under the protocol approved by both the johns hopkins university joint committee for clinical investigation and the human subject research review board of the office of the surgeon general of the u . s . army ( fries et al . ( 1992 ), proc . natl . acad . sci . u . s . a . 89 : 358 - 362 ), using dosages described therein , or other dosages described in the literature for liposome - based delivery of therapeutic agents . iscoms are negatively charged cage - like structures of 30 - 40 nm in size formed spontaneously on mixing cholesterol and quil a ( saponin ). protective immunity has been generated in a variety of experimental models of infection , including toxoplasmosis and epstein - barr virus - induced tumors , using iscoms as the delivery vehicle for antigens ( mowat and donachie ) immunology today 12 : 383 - 385 , 1991 . doses of antigen as low as 1 μg encapsulated in iscoms have been found to produce class i mediated ctl responses , where either purified intact hiv - 1 - iiib gp 160 envelope glycoprotein or influenza hemagglutinin is the antigen ( takahashi et al ., nature 344 : 873 - 875 , 1990 ). peptides are delivered into tissue culture cells using iscoms in a manner and dosage similar to that described above for liposomes ; the class ii peptide binding of delivered peptides are then determined by extraction and characterization as described above . iscom - delivered peptides of the invention which are effectively utilized by cultured cells are then tested in animals or humans . in addition to delivery of the therapeutic synthetic peptides , iscoms could be constituted to deliver the mini - gene constructs to apcs , and thus serve as an alternative to the above - outlined vaccinia strategy . in addition to using the above - described intracellular delivery systems to deliver nonimmunogenic self peptides with the specific aim of down - modulating the immune system ( thus alleviating autoimmune conditions ), the delivery systems of the invention may alternatively be used as a novel means of vaccination , in order to stimulate a portion of the immune system of an animal . in the latter context , the delivery system is employed to deliver , into appropriate cells , dna constructs which express immunogenic , pathogen - derived peptides intended to stimulate an immune response against a specific pathogen . because the antigenic peptide is produced inside the target cell itself , the vaccine method of the invention ensures that there is no circulating free antigen available to stimulate antibody formation and thereby induce potentially deleterious or inappropriate immunological reactions . the immune response stimulated by vaccines of the invention is , because the vaccines are targeted solely to apc &# 39 ; s , limited to the t cell mediated response , in contrast to standard vaccine protocols which result in a more generalized immune response . although some of the peptide - presenting apc &# 39 ; s will initially be lysed by host t cells , such lysis will be limited because , inter alia , the virus - based vaccine is non - replicative , i . e ., each carrier virus can infect only one cell . the model antigen that will be used to perfect and test the system of the invention is hen egg lysozyme ( hel ). it is arguably the most well characterized protein for antigen presentation studies , to which there are numerous monoclonal antibodies and class i - and class ii - restricted mouse t cell clones and hybridomas . the primary epitopes that will be studied are the peptide hel 34 - 45 , as both monoclonal antibodies and cd4 + t cell hybridomas are available , and peptide hel 46 - 61 , as both class i and class ii - restricted t cell clones and hybridomas have been raised and are publicly available . these two sequences are thus proven immunogenic epitopes . initially , four constructs encoding different polypeptides are analyzed : ( a ) whole , secreted hel , ( b ) hel 34 - 45 , ( c ) hel 46 - 61 , and ( d ) hel 34 - 61 . the last three include a signal sequence known to be cleaved in these cells , e . g ., iak ( mprsralilgvlalttmlslcgg ; seq id no : 274 , which would result in targeting to the er . all constructs are then subcloned into phβapr - 1 neo . the methodology for making these constructs is similar to that outlined above . the constructs are introduced into appropriate apcs , e . g ., lk35 . 2 cells , by means of a conventional eukaryotic transfection or one of the delivery vehicles discussed above ( e . g ., vaccinia , liposomes , or iscoms ). lk35 . 2 cells , which possess the mouse mhc class ii restriction molecules ia k and ie k , transfected with each of the constructs are tested for their ability to stimulate the appropriate class i and class ii - restricted t cell hybridomas and clones using standard techniques . whether class i stimulation is observed will depend on whether peptide trimming can occur in the er , in order to produce an 8 - 10 - mer suitable for binding to class i molecules . if these constructs are ineffective for class i stimulation , they can be modified in order to produce a more effective peptide for class i binding . if these constructs prove to be less effective for class ii - restricted responses , they can be tagged with endosomal and / or lysosomal targeting sequences as discussed in section v . the effectiveness of targeting signals used to direct immunogenic peptides to particular intracellular organelles would be monitored using electron microscopic analysis of immunogold stained sections of the various transfectants . rabbit anti - peptide antisera would be produced and affinity purified for this application . in addition , monoclonal antibody hf10 , which recognizes hel 34 - 45 , will be used . once a construct is defined that can be effectively presented by transfectants in vitro , its effectiveness in vivo will be determined . this can be tested by injection of the transfectants i . p . and / or s . c . into c3h / balb / c f1 mice , or by injection of the construct incorporated into an appropriate delivery vehicle ( e . g ., liposome , iscoms , retrovirus , vaccinia ). optimal protocols and doses for such immunizing injections can be determined by one of ordinary skill in the art , given the disclosures provided herein . efficiency of immunization can be tested by standard methods such as ( a ) proliferation of class ii - restricted t cells in response to hel pulsed apcs , ( b ) ctl response to 51 cr - labeled targets , and ( c ) serum antibody titre as determined by elisa . once the details of the vaccine delivery system of the invention are optimized , constructs encoding peptides with useful immunizing potential can be incorporated into the system . such peptides can be identified by standard means now used to identify immunogenic epitopes on pathogen - derived proteins . for example , candidate peptides for immunization may be determined from antibody and t cell analysis of animals infected with a particular pathogen . in order to obtain a protective and effective anamnestic response , the peptides used for vaccination should ideally be those which are presented with the highest frequency and efficiency upon infection . this could best be determined by using the procedures outlined in the experimental section above to extract and characterize the peptides bound by mhc class ii molecules from infected cells . given allelic restriction of immunogenic peptides ( in contrast to the observed degenerate binding of self peptides of invention ), a mini - gene encoding several immunogenic peptides will probably be required to provide a vaccine useful for the entire population . vaccine administration and dosage are as currently employed to smallpox vaccination . table 1__________________________________________________________________________lg - 2 / hla - dr1 binding peptides seqprotein source position sequence id no . length fraction mw mass yield__________________________________________________________________________pseudo hla - a2 103 - 120 vgsdwrflrgyhqyaydg 1 18 dr1s - 59 2190 . 4 2190 . 4 39 . 5 103 - 117 vgsdwrflrgyhqya 2 15 dr1s - 58 1855 . 0 1854 . 4 907 . 5 103 - 116 vgsdwrflrgyhqy 3 14 dr1s - 58 1784 . 0 1783 . 6 53 . 3 104 - 117 gsdwrflrgyhqya 4 14 dr1s - 56 1755 . 3 1755 . 2 96 . 5 105 - 117 sdwrflrgyhqya 5 13 dr1s - 56 1698 . 2 1698 . 8 48 . 8invariant chain 98 - 122 lpkppkpvskmrmatpllmqalpmg 6 25 dr1s - 88 2733 . 5 2734 . 5 40 . 5 ( ii ) 98 - 121 lpkppkpvskmrmatpllmqalpm 7 24 dr1s - 88 2676 . 4 2675 . 9 80 . 8 99 - 122 pkppkpvskmrmatpllmqalpmg 8 24 dr1s - 86 2620 . 2 2619 . 7 91 . 5 98 - 120 lpkppkpvskmrmatpllmqalp 9 23 dr1s - 86 2545 . 2 2544 . 5 112 . 2 99 - 121 pkppkpvskmrmatpllmqalpm 10 23 dr1s - 87 2563 . 2 2562 . 3 145 . 0 100 - 121 kppkpvskmrmatpllmqalpm 11 22 dr1s - 87 2466 . 1 2465 . 8 101 . 5 99 - 120 pkppkpvskmrmatpllmqalp 12 22 dr1s - 84 2432 . 0 2431 . 7 72 . 5 100 - 120 kppkpvskmrmatpllmqalp 13 21 dr1s - 84 2334 . 9 2334 . 2 31 . 6 100 - 120 ppxpvskmrmatpllmqalp 14 20 dr1s - 86 2206 - 7 2207 . 4 89 . 8 107 - 121 kmrmatpllmqalpm 15 15 dr1s - 88 1732 . 2 1731 . 9 178 . 5 107 - 120 kmrmatpllmqalp 16 14 dr1s - 86 1601 . 0 1600 . 2 162 . 0na . sup .+ / k . sup .+ atpase 199 - 216 ipadlriisangckvdns 17 18 dr1s - 56 1886 . 6 1885 . 8 48 . 8transferrin recpt . 680 - 696 rveyhflspyvspkesp 18 17 dr1s - 58 2035 . 3 2036 . 8 30 . 3bovine fetuin 56 - 74 ykhtlnqidsvkvwprrpt 19 19 dr1s - 51 2237 . 6 2236 . 5 69 . 0 56 - 73 ykhtlnqidsvkvwprrp 20 18 dr1s - 50 2338 . 7 2338 . 5 32 . 5hla - dr β - chain 43 - 61 dvgeyravtelgrpdaeyw 21 19 dr1s - 51 2226 . 5 ? carboxypeptidase e 101 - 115 epgepefkyignmhg 22 15 dr1s - 48 1704 . 9 1700 . 4 * esi - ms__________________________________________________________________________ table 2__________________________________________________________________________peptide binding to hla - dr1peptide . sup . a seq id no . length ki vs ha 307 - 319 . sup . b nm sds - resistance . sup . c nm__________________________________________________________________________hla - a2 103 - 117 2 15 49 ± 3 + ii 106 - 120 15 15 & lt ; 10 + ii 98 - 121 7 24 33 ± 5 + na . sup .+ / k . sup .+ atpase 17 18 68 ± 9 + 199 - 216transf . recept . 680 - 696 18 17 & lt ; 10 + bavine fetuin 56 - 72 23 19 66 ± 18 + ha 307 - 319 24 14 & lt ; 10 + ii 97 - 111 25 15 & gt ; 10 . sup . 4 - β . sub . 2 m 52 - 64 26 13 & gt ; 10 . sup . 4 - __________________________________________________________________________ . sup . a the first six entries correspond to peptides found associated with hladr1 and the sequences are shown in table 1 . two control peptides were also tested : β . sub . 2 m 52 - 64 , sdlsfskdwsfyl ( seq id no : 26 ), is from human β . sub . 2microglobulin and ii 97 - 111 , lpkppkpvskmrmat ( seq id no 25 ) is a truncated version of the longest invariant chain derived peptide isolated from hladr1 . peptides were synthesized using solidphase fmoc chemistry , deprotected and cleaved using standrd methods , then purified b rpc . purified peptides were analzyed by mass spectrometry and concentrations were determined by quantitative ninhydrin analysis . . sup . b inhibition constants ( ki ) were measured as the concentration of test peptide which inhibited 50 % of the . sup . 125 ilabeled ha 307 - 319 binding to &# 34 ; empty &# 34 ; hladr1 produced in sf9 insect cells ( 20 ). ha 307 - 319 was labeled using na . sup . 125 i and chloraminet and isolated by gel filtration . specific activity , determined by bca assay ( pierce ) and gamma counting , was 26 , 000 cpm / pmol . 10 nm labeled peptide and 10 nm purified hladr1 were mixed with 10 different concentrations ( 10 nm to 10 μm ) of synthetic cold competitor peptide in phosphatebuffered saline , ph 7 . 2 , containing 1 mm edta , 1 mm pmsf , 0 . 1 mm iodoacetamide , and 3 mm nan . sub . 3 and incubated at 37 ° c . for 85 hours . free and bound peptide were separated by native gel electrophoresis ( 33 ) and bound radioactivity was quantitated using a fujix imaging plate analyzer ( bas 2000 ) after four hour exposures on the phosphoimaging plates . percent inhibition was calculated as the ratio of backgroundcorrected radioactivity in the sampl to backgroundcorrected radioactivity in a parallel sample containing no competitor peptide . under these conditions , ki measurements & lt ; 10 nm could not be accurately determined . . sup . c the ability of the synthetic peptides to confer resistance to sdsinduced chain dissociation of hladr1 produced in insect cells was determined as described ( 20 ). briefly , 20 μm hladr1 was incubated with fivefold excess of synthetic peptide at 37 ° c . for 85 hours , in phosphatebuffered saline ( ph 7 . 2 ) with the protease inhibitor mixture described above . after incubation , the samples were analyzed by sds page with and without boiling prior to loading . peptides which prevented sdsinduced chain dissociation are indicated positive (+) and those that did not negative (-). table 3__________________________________________________________________________putative hla - dr1 peptide binding motifa protein source peptide sequence seq id no . length position reference__________________________________________________________________________ hla - a2 sdwrflrgyhqya 5 13 105 - 117 this study invariant chain kmrmatpllmqalp 16 14 106 - 119 na . sup .+ / k . sup .+ atpase ipadlriisangckvdns 17 18 199 - 216 transferrin receptor rveyhflspyvspkesp 18 17 680 - 696 bovine fetuin ykhtlnoidsvkvwprrp 20 18 56 - 73b hel kvfgrcelaaamkrhgld 27 18 1 - 18 6 rnrckgtdvqawirgcrl 28 18 112 - 129 6 β . sub . 2 m hpphieiqmlkngkki 29 16 31 - 46 6 pla . sub . 2 nelgrfkhtdaccrth 30 16 19 - 34 6 skpkvyqwfdlrky 31 14 115 - 128 6 nase atstkklhkepatlikaidg 32 20 1 - 20 6 patlikaidgdtvklmykgq 33 20 11 - 30 6 drvklmykgqpmtfrlllvd 34 20 21 - 40 6 vayvykpnntheqhlrksea 35 20 111 - 130 6 hiv p13 qkqepidkelypltsl 36 16 97 - 112 6 hiv p17 garasvlsggeldkwe 37 16 1 - 16 6 influenza ha rtlyqnvgtyvsvgtstlnk 38 20 187 - 206 6 influenza ha pkyvkqntlklat 24 13 307 - 319 17 p . falcip . p190 lkklvfgyrkpldni 39 15 249 - 263 25 p . falcip . cs khieqylkkikns 40 13 329 - 341 27 chicken ova dvfkelkvhhanenif 41 16 15 - 30 6 dr1 β chain gdtrprflwqlkfechffng 42 20 1 - 20 28 tervrllerciynoeesvrfds 43 22 21 - 42 28 dlleqrraavdtycrhnygvgesft 44 25 66 - 90 28 p cyt c kaeradliaylkqatak 45 17 88 - 104 6 myelin basic prot . grtqdenpvvhffknivtprtppp 46 24 75 - 98 6c influenza matrix plkaeiaorledv 47 13 19 - 31 6 hiv p17 rqilgolqpslqtgse 48 16 57 - 72 6 β . sub . 2 m iqvysrhppengkpni 49 16 7 - 22 6 pla . sub . 2 intkcyklehpvtgcg 50 16 85 - 100 6 p . falcip . p190 yklnfyfdllrakl 51 14 211 - 224 25 idtlkknenikel 52 13 338 - 350 25 dr1 β chain dvgeyravtelgrpdaeywn 53 20 43 - 62 28 hiv p17 erfavnpglletsegc 54 16 41 - 56 6 hel dnyrgyslgnwvcaakfesnftq 55 23 20 - 42 6 nase ealvrqglakvayvykpnnt 56 20 101 - 120 6 hiv p25 pivqnlogqmvhqais 57 16 1 - 16 6 salsegatpqdlntml 58 16 41 - 56 6 β . sub . 2 m sfyilahteftptetd 59 16 61 - 76 6 pla . sub . 2 kmyfnlintkcykleh 60 16 79 - 94 6__________________________________________________________________________ table 4__________________________________________________________________________mst / hla - dr2 binding pepties massprotein source position sequence seq id no . length fraction mw spec__________________________________________________________________________pseudo hla - a2 103 - 120 vgsdwrflrgyhqyaydg 1 18 dr2 - 3 - 57 2190 . 4 2189 . 0 103 - 119 vgsdwrflrgyhqyayad 61 17 dr2 - 3 - 57 2133 . 3 2131 . 8 104 - 119 gsdwrflrgyhqyayd 62 16 dr2 - 3 - 56 2034 . 3 2040 . 4 103 - 117 vgsdwrflrgyhqya 2 15 drz - 3 - 56 1855 . 0 1858 . 5 103 - 116 vgsdwrflrgyhqy 3 14 dr2 - 3 - 56 1784 . 0 1786 . 3 104 - 117 gsdwrflrgyhqya 4 14 dr2 - 3 - 55 1755 . 3 1755 . 0 * 105 - 117 sdwrflrgymqya 5 13 dr2 - 3 - 56 1698 . 2 1702 . 6invariant chain 98 - 121 lpkppkpvskmrmatpllmqalpm 7 24 dr2 - 3 - 70 2676 . 4 2675 . 0 *( ii ) 99 - 121 pkppkpvskmrmatpllmqalpm 10 23 dr2 - 3 - 70 2563 . 2 2562 . 0 * 100 - 121 kppkpvskmrmatpllmqalpm 11 22 dr2 - 3 - 70 2466 . 1 2465 . 0 * 99 - 120 pkppkpvskmrmatpllmqalp 12 22 dr2 - 3 - 66 2432 . 0 2437 . 0 100 - 120 kppkpvskmrmatpllmqalp 13 21 dr2 - 3 - 66 2334 . 9 2340 . 0 101 - 120 ppkpvskmrmatpllmqalp 63 20 dr2 - 3 - 70 2206 . 7 2207 . 0 * 107 - 125 kmrmatpllmqalpmgalp 64 19 dr2 - 3 - 71 2070 . 5 2074 . 3 107 - 121 kmrmatpllmqalpm 15 15 dr2 - 3 - 70 1732 . 2 1732 . 0 * hla - dq α - chain 97 - 119 nivikrsnstaatnevpevtvfs 158 23 dr2 - 3 - 44 2476 . 8 2478 . 1 97 - 112 nivikrsnstaatnev 159 16 dr2 - 3 - 41 1716 . 9 1717 . 0hla - dq β - chain 42 - 59 sdvgvyravtpqgrpdae 160 18 dr2 - 3 - 41 1917 . 1 1920 . 5 43 - 59 dvgvyravtpqgrpdae 161 17 dr2 - 3 - 41 1830 . 0 1833 . 3 43 - 57 dvgvyravtpqgrpd 162 15 dr2 - 3 - 41 1629 . 8 1632 . 9hla - dr α - chain 182 - 194 apsplpettenvv 163 13 dr2 - 3 - 36 1353 . 5 1362 . 0 182 - 198 apsplpettenvvcalg 164 17 dr2 - 3 - 41 1697 . 9 1701 . 0 ( met ) kinase - retate 59 - 81 ehhiflgatnyiyvlheedlqkv 65 23 dr2 - 3 - 65 2746 . 1 2746 . 6transforming proteinguanylate - bind . 434 - 450 qelknkyyqvprkgiqa 66 17 dr2 - 3 - 71 2063 . 4 2074 . 3mannose - bind . prot . 174 - 193 iqnlikeeaflgitdekteg 67 20 dr2 - 3 - 70 2248 . 5 2248 . 0 * apolipoprotein b - 100 1200 - 1220 fpkslhtyanilldrrvpqtd 165 21 dr2 - 3 - 61 2484 . 8 2490 . 9 1200 - 1218 fpkslhtyanilldrrvpq 166 19 dr2 - 3 - 61 2268 . 6 2276 . 7potassium channel prot 173 - 190 gilyyyqsggrlrrpvn 167 18 dr2 - 3 - 61 2127 . 4 2132 . 6 173 - 189 dgilyyyqsggrlrrpv 168 17 dr2 - 3 - 61 2013 . 3 2018 . 1fibronectin receptor 586 - 616 lspihialnfsldpqapvdshglrpalhyq 169 30 dr2 - 3 - 61 3307 . 7 3313 . 1factor viii 1175 - 1790 lwdygmsssphvlrnr 170 16 dr2 - 3 - 44 1918 . 2 1921 . 7hla - dr2b β - chain 94 - 111 rvqpkvtvypsktqplqh 72 18 dr2 - 3 - 39 2106 . 5 2114 . 94 - 108 rvqpkvtvypsktqp 73 15 dr2 - 3 - 39 1728 . 3 1730 . 6 esi - ms * mald - ms__________________________________________________________________________ table 5__________________________________________________________________________wt - 20 / hla - dr3 naturally processed peptidesprotein source position sequence seq id no . length fraction nw mass__________________________________________________________________________ spec . pseudo hla - a2 103 - 117 vgsdwrflrgyhqya 2 15 dr3 - 2 - 63 1855 . 0 1863 . 9hla - a30 28 -? vddtqfvrfdsdaasq . . . 171 ? dr3 - 2 - 55 ? ? hla - dr α - chain 111 - 129 ppevtvltnspvelrepnv 172 19 dr3 - 2 - 55 2090 . 4 2093 . 3 111 - 128 ppevtvltnspvelrepn 173 18 dr3 - 2 - 55 1991 . 2 1989 . 8hla - dr β - chain 1 -? gdtrprfleystsechff 79 18 dr3 - 2 - 73 ? ? acetylcholine recept . 289 - 304 vflllladkvpetsls 174 16 dr3 - 2 - 65 1745 . 1 1750 . 1glucose - transport 459 - 474 tfdejasgfrqggasq 175 16 dr3 - 2 - 55 1670 . 8 1672 . 6sodium channel prot . 384 - 397 ygytsydtfswafl 176 14 dr3 - 2 - 41 1720 . 8 1720 . 5invariant chain 98 - 120 lpkppkpvskmrmatpllmqalp 9 23 dr3 - 2 - 73 2545 . 2 2554 . 0 ( ii ) 99 - 120 pkppkpvskmrmatpllmqalp 12 22 dr3 - 2 - 73 2432 . 0 2441 . 4 100 - 120 kppkpvskmrmatpllmqalp 13 21 dr3 - 2 - 73 2334 2345 . 3 132 - 150 atkygnmtedhvmhllqna 177 19 dr3 - 2 - 69 2173 . 4 2179 . 3cd45 1071 - 1084 gqvkknnhqedkie 178 14 dr3 - 2 - 41 1666 . 8 1667 . 0icam - 2 64 - 76 lnkilldeqaqwk 179 13 dr3 - 2 - 51 / 52 1598 . 9 1602 . 4interferon γ - receptor 28 - 147 gppkldirkeekqimidifh 180 21 dr3 - 2 - 77 2505 . 0 2510 . 3 128 - 148 gppkldirkeekqimidifhp 181 20 dr3 - 2 - 77 2407 . 8 2412 . 4ip - 30 38 - 59 splqaldffgngppvhyktgnl 182 22 dr3 - 2 - 77 2505 . 0 2510 . 3 38 - 57 splqaldffgngppvnyktg 183 20 dr3 - 2 - 77 2122 . 4 2124 . 2cytochrome - b5 reduc . 155 - 172 gkfairpdkksnpiirtv 184 18 dr3 - 2 - 51 / 52 2040 . 4 2043 . 2ebv membrane antigen 592 - 606 tghgartstepttdy 185 15 dr3 - 2 - 41 1593 . 6 1592 . 7gp220ebv tegument protein 1395 - 1407 kelkrqyekklrq 186 13 dr3 - 2 - 51 / 52 1747 . 1 1749 . 8membrane p140apolipoprotein 1276 - 1295 nflksdgrikytlnknslk 74 20 dr3 - 2 - 63 2352 . 9 2360 . 0b - 100 ( human ) 1273 - 1292 ipdnlflksdgrikytlnkn 191 20 dr3 - 2 - 65 2349 . 7 2354 . 6 1273 - 1291 ipdnlflksdgrikytlnk 75 19 dr3 - 2 - 63 2235 . 5 2245 . 1 1273 - 1290 ipdnlflksdgrikytln 192 18 dr3 - 2 - 65 2107 . 4 2096 . 6 1273 - 1289 ipdnlflksdgrikytl 193 17 dr3 - 2 - 65 1993 . 3 2000 . 8 1276 - 1291 nlflksdgrikytlnk 76 16 dr3 - 2 - 60 1910 . 2 1911 . 4 1276 - 1290 nlflksdgrikytln 77 15 dr3 - 2 - 60 1782 . 1 1785 . 9 1207 - 1224 yanilldrrvpqtdmtf 78 17 dr3 - 2 - 63 2053 . 3 2059 . 1 1794 - 1810 vttlnsdlkynaldltn 194 17 dr3 - 2 - 69 1895 . 1 1896 . 5 mald - ms__________________________________________________________________________ table 6__________________________________________________________________________priess / hla - dr4 naturally processed peptidesprotein source position sequence seq id no . length fraction mw mass__________________________________________________________________________ specig kappa chain 188 - 208 khkvyacevihqglsspvtks 80 21 dr4 - 2 - 45 2299 . 6 2304 . 0c region ( human 188 - 207 khkvyacevthqglsspvtk 81 20 dr4 - 2 - 47 2212 . 5 2213 . 0 189 - 206 hkvyacevthqglsspvt 82 18 dr4 - 2 - 43 1955 . 5 1952 . 1 188 - 204 khkvyacevthqglssp 83 17 dr4 - 2 - 45 1883 . 1 1882 . 8 187 - 203 ekhkvyacevthqglss 84 17 dr4 - 2 - 45 1915 . 1 1922 . 5 188 - 203 khkvyacevthqglss 85 16 dr4 - 2 - 54 1787 . 0 1787 . 0 189 - 204 hkvyacevthqglssp 86 16 dr4 - 2 - 47 1755 . 0 1767 . 8 187 - 202 ekhkvyacevthqgls 87 16 dr4 - 2 - 43 1828 . 0 1822 . 8 188 - 202 khkvyacevthqgls 88 15 dr4 - 2 - 51 1699 . 9 1708 . 3 189 - 203 hkvyacevthqglss 89 15 dr4 - 2 - 45 1657 . 8 1667 . 0 187 - 200 ekhkvyacevthqg 90 14 dr4 - 2 - 51 1628 . 8 1632 . 6hla - dr α - chain 182 - 198 apsplpettenvvcalg 91 17 dr4 - 2 - 43 1697 . 9 1700hla - a2 28 - 50 vddtqfvrfdsdaasqrmeprap 195 23 dr4 - 2 - 58 2638 . 6 2641 . 5 28 - 48 vddtqfvrfdsdaasqrmepr 92 21 dr4 - 2 - 56 2470 . 6 2472 . 9 28 - 47 vddtqfvrfdsdaasqrmep 93 20 dr4 - 2 - 59 2314 . 5 2319 . 3 28 - 46 vddtqfvrfdsdaasqrme 94 19 dr4 - 2 - 54 2217 . 2 2218 . 7 30 - 48 dtqfvrfdsdaasqrmepr 95 19 dr4 - 2 - 55 2256 . 4 2263 . 2 31 - 49 tqfvrfdsdaasqrmepra 96 19 dr4 - 2 - 56 2212 . 4 2211 . 5 28 - 44 vddtqfvrfdsdaasqr 97 17 dr4 - 2 - 55 1957 . 0 1963 . 1 31 - 47 tqfvrfdsdaasqrmep 98 17 dr4 - 2 - 56 1985 . 1 1987 . 5 31 - 45 tqfvrfdsdaasqrm 99 15 dr4 - 2 - 54 1758 . 9 1761 . 0 31 - 42 tqfvrfdsdaas 100 12 dr4 - 2 - 54 1343 . 4 1343 . 3hla - c 28 - 50 vddtqfvrfdsdmsprgeprap 101 23 dr4 - 2 - 56 2533 . 7 2536 . 7 31 - 52 tqfvrfdsdaasprgeprapwv 102 22 dr4 - 2 - 54 2489 . 7 2491 . 5 28 - 48 vddtqfvrfdsdaasprgepr 103 21 dr4 - 2 - 54 2365 . 5 2368 . 1 28 - 47 vddtqfvrfdsdaasprgep 104 20 dr4 - 2 - 56 2209 . 3 2211 . 5 28 - 46 vddtqfvrfdsdaasprge 105 19 dr4 - 2 - 56 2112 . 2 2113 . 9hla - cw9 28 - 45 vddtqfvrfdsdaasprg 106 18 dr4 - 2 - 56 1983 . 1 1987 . 5 31 - 48 tqfvrfdsdaasprgepr 107 18 dr4 - 2 - 52 2036 . 2 2041 . 5 28 - 44 vddtqfvrfdsdaaspr 108 17 dr4 - 2 - 55 1926 . 0 1931 . 7 30 - 46 dtqfvrfdsdaasprge 109 17 dr4 - 2 - 52 1897 . 9 1901 . 6 31 - 44 tqfvrfdsdaaspr 110 14 dr4 - 2 - 52 1596 . 7 1603 . 7 31 - 42 tqfvrfdsdaas 111 12 dr4 - 2 - 54 1343 . 4 1343 . 3hla - c 130 - 150 lrswtaadtaaqitqrkweaa 112 21 dr4 - 2 - 56 2374 . 6 2376 . 4 129 - 147 dlrswtaadtaaqitqrkw 197 19 dr4 - 2 - 58 2218 . 4 2220 . 1 130 - 147 lrswtaadtaaqitqrkw 198 18 dr4 - 2 - 58 2103 . 3 2105 . 0 129 - 145 dlrswtaadtaaqitqr 113 17 dr4 - 2 - 59 1904 . 5 1908 . 7 129 - 144 dlrswtaadtaaqitq 114 16 dr4 - 2 - 59 1747 . 9 1752 . 3 129 - 143 dlrswtaadtaaqit 115 15 dr4 - 2 - 59 1619 . 7 1622 . 2hla - bw62 129 - 150 dlsswtaadtaaqitqrkweaa 199 22 dr4 - 2 - 65 2420 . 6 2422 . 7 129 - 145 dlsswtaadtaaqitqr 116 17 dr4 - 2 - 60 1834 . 9 1838 . 1 129 - 146 dlsswtaadtaaqitqrk 200 18 dr4 - 2 - 65 1963 . 1 1966 . 3 129 - 148 dlsswtaadtaaqitqrkwe 117 20 dr4 - 2 - 66 2278 . 4 2284 . 6vla - 4 229 - 248 gslfvynittnkykafldkq 201 20 dr4 - 2 - 65 2350 . 7 2352 . 6 229 - 244 gslfvynittnkykaf 202 16 dr4 - 2 - 65 1866 . 1 1868 . 2pai - 1 261 - 281 aapyekevplsaltnilsaql 203 21 dr4 - 2 - 65 2228 . 5 2229 . 5 261 - 278 aapyekevplsaltnils 204 18 dr4 - 2 - 65 1916 . 2 1917 . 4cathepsin c 151 - 167 ydhnfvkainadqkswt 118 17 dr4 - 2 - 70 2037 . 2 2039 . 6 ( rat homologue i 119 2035 . 3 151 - 166 ydhnfvkainadqksw 120 16 dr4 - 2 - 70 1936 . 1 1937 . 7 i 121 1934 . 2bovine hemoglobin 26 - 41 aealermflsfpttkt 205 16 dr4 - 2 - 78 1842 . 1 1836 . 1hla - dq3 . 2 β - chain 24 - 38 spedfvyqfkgmcyf 206 15 dr4 - 2 - 78 1861 . 1 1861 . 7hla - dr β - chain 1 -? gdtrprfleqvkhe . . . 122 14 dr4 - 2 - 72 1711 . 9ig heavy chain 121 -? gvyfylqwgrstlvsvs . . . 123 (?) dr4 - 2 - 6 ? ? mald - ms__________________________________________________________________________ table 7__________________________________________________________________________mann / hla - dr7 naturally processed peptides seq frac - massprotein source position sequence id no . length tion mw spec__________________________________________________________________________pseudo hla - a2 105 - 124 sdwrflrgyhqyaydgkdyi 207 20 dr7 - 2 - 61 2553 . 8 2556 . 5 103 - 120 vgsdwrflrgyhqyaydg 1 18 dr7 - 2 - 63 2190 . 4 2194 103 - 117 vgsdwrflrgyhqya 2 15 dr7 - 2 - 63 1855 . 0 1860 104 - 117 gsdwrflrgyhqya 208 14 dr7 - 2 - 61 1755 . 9 1760 . 8 104 - 116 gsdwrflrgyhqy 209 13 dr7 - 2 - 61 1684 . 8 1687 . 6 105 - 117 sdwrflrgyhqya 210 13 dr7 - 2 - 61 1698 . 9 1704 . 1hla - a29 234 - 253 rpagdgtfqkwasvvvpsgq 124 20 dr7 - 2 - 66 2087 . 3 2092 234 - 249 rpagdgtfqkwasvvv 125 16 dr7 - 2 - 63 1717 1718 237 - 258 gdgtfqkwasvvvpsgqeqryt 126 22 dr7 - 2 - 66 2436 2440 237 - 254 gdgtfqkwasvvvpsgqe 127 18 dr7 - 2 - 66 1892 . 3 1892 239 - 252 gtfqkwasvvvpsg 128 14 dr7 - 2 - 66 1462 1465 239 - 253 gtfqkwasvvvpsgq 129 15 dr7 - 2 - 66 1718 1721 239 - 261 gtfqkwasvvvpsgqeqrytchv 130 23 dr7 - 2 - 66 2603 2606hla - 844 83 - 99 retqisktntqtyrenl 211 17 dr7 - 2 - 35 2082 . 3 2086 . 1 83 - 98 retqisktntqtyren 212 16 dr7 - 2 - 35 1969 . 1 1971 . 1 83 - 97 retqisktntqtyre 213 15 dr7 - 2 - 35 1855 . 0 1857 . 3hla - dr α - chain 101 - 126 rsnytpitnppevtvltnspvelrep 214 26 dr7 - 2 - 35 2924 . 2 2926 . 9 58 - 78 galaniavdkanleimtkrsn 131 21 dr7 - 2 - 66 2229 . 5 2221 182 - 200 apsplpettenvvcalgltv 215 20 dr7 - 2 - 42 1912 . 2 1917 . 7hla - dq α - chain 179 -? slqspitvewraqsesaqskmlsgiggfvl 216 ? dr7 - 2 - 35 ? ? 4f2 cell - surface 318 - 338 vtqylnatgnrwcswslsqar 217 21 dr7 - 2 - 71 2441 . 7 2445 . 1antigen heavy chain 318 - 334 vtqylnatgnrwcswsl 218 17 dr7 - 2 - 71 1999 . 2 2001 . 9lif receptor 854 - 866 tsilcyrkrewik 219 13 dr7 - 2 - 35 1696 . 0 1700 . 8ig kappa chain c reg . 188 - 201 khkvyacevthqgl 220 14 dr7 - 2 - 61 1612 . 9 1615 . 6 188 - 200 khkvyacevthqg 221 13 dr7 - 2 - 61 1498 . 7 1501 . 0invariant chain 99 - 120 pkppkpvskmrmatpllmqalp 12 22 dr7 - 2 - 72 2432 . 0 2436 . 6 ( ii ) 100 - 120 kppkpvskmrmatpllmqalp 13 21 dr7 - 2 - 72 2334 . 9 2339 . 7k channel protein 492 - 516 gdmypktwsgmlvgalcalagvlti 222 25 dr7 - 2 - 71 2567 . 1 2567 . 3heat shock cognate 38 - 54 tpsyvaftdterligda 132 17 dr7 - 2 - 69 1856 . 0 1856 . 671 kd protein 17 dr7 - 2 - 72 1856 . 0 1857 . 0 38 - 52 tpsyvaftdterlig 133 15 dr7 - 2 - 69 1669 . 8 1671 . 9complement c9 465 - 483 apvlisqklspiynlvpvk 223 19 dr7 - 2 - 61 2079 . 5 2083 . 9thromboxane - a 406 - 420 pafrftreaaqdcev 224 15 dr7 - 2 - 71 1739 . 9 1743 . 0synthaseebv major capsid prot 1264 - 1282 vpglyspcraffnkeell 225 18 dr7 - 2 - 54 2082 . 4 2081 . 2 1264 - 1277 vpglyspcraffnk 226 14 dr7 - 2 - 54 1597 . 9 1598 . 6apolipoprotein b - 100 1586 - 1608 kvdltfskqhallcsdyqadyes 227 23 dr7 - 2 - 54 2660 . 9 2662 . 5 1586 - 1600 kvdltfskqhallcs 228 15 dr7 - 2 - 54 1689 . 0 1687 . 7 1942 - 1954 fshdyrgstshrl 229 13 dr7 - 2 - 42 1562 . 7 1567 . 5 2077 - 2089 lpkyfekkrntii 230 13 dr7 - 2 - 61 1650 . 0 1653 . 8 mald - ms__________________________________________________________________________ table 8__________________________________________________________________________23 . 1 / hla - dr8 naturally processed peptides seq . protein source position sequence id no . length fraction mw mass__________________________________________________________________________ spechla - dr α - chain 158 - 180 setvflpredhlfrkfhylpflp 231 23 dr8 - 3 - 59 2889 . 3 2889 . 0 182 - 198 apsplpettenvvcalg 232 17 dr8 - 3 - 41 1697 . 9 1704 . 3hla - dr β - chain 1 -? gdtrprfleystgecyffngterv 233 ? dr8 - 3 - 75 -- -- hla - dp β - chain 80 - 92 rhnyeldeavtlq 234 13 dr8 - 3 - 76 1587 . 7 1591 . 3lam blast - 1 with 88 - 108 dpqsgalyiskvqkednstyi 235 21 dr8 - 3 - 54 2543 . 6 2549 . 1n - acetyglucosamine 92 - 108 galyiskvqkednstyi 236 17 dr8 - 3 - 52 2116 . 1 2118 . 0 129 - 146 dpvpkpvikiekiedmdd 237 18 dr8 - 3 - 57 2081 . 4 2085 . 7 129 - 143 dpvpkpvikiekied 238 15 dr8 - 3 - 57 1720 . 0 1724 . 9ig kappa chain 63 - 80 ftftisrlepedfavyyc 239 18 dr8 - 3 - 57 2201 . 5 2203 . 6 63 - 77 ftftisrlepedfav 240 15 dr8 - 3 - 57 1772 . 0 1777 . 0lar protein 1302 - 1316 dpvemrrlnyqtpg 241 14 dr8 - 3 - 76 1675 . 9 1679 . 8lif receptor 709 - 726 yqllrsmigyieelapiv 242 18 dr8 - 3 - 66 2108 . 5 2112 . 0ifn - α receptor 271 - 287 gnhlykwkqipdcenvk 243 17 dr8 - 3 - 66 2072 . 4 2075 . 1interleukin - 8 169 - 188 lpfflfrqayhpnnsspvcy 244 20 dr8 - 3 - 59 2400 . 7 2402 . 5receptormetalloproteinase 187 - 214 qakffacikrsdgscawyrgaappkqef 245 28 dr8 - 2 - 63 3161 . 6 3164 . 9inhibitor 2 187 - 205 qakffacikrsdgscawyr 246 19 dr8 - 3 - 63 2235 . 5 2233 . 6metalloproteinase 101 - 118 nrseefliagklqdgllh 134 18 dr8 - 3 - 66 2040 . 3 2042 . 9inhibitor 1 101 - 117 seefliagklqdgll 135 16 dr8 - 3 - 70 1789 . 0 1799 . 9 103 - 117 seefliagklqdgll 247 15 dr8 - 3 - 72 1632 . 9 1646 . 0 101 - 112 nrseefliagkl 248 12 dr8 - 3 - 66 1376 . 6 1381 . 8cathepsin e 89 - 112 qnftvifdtgssnlwvpsvyctsp 249 24 dr8 - 3 - 59 2662 . 9 2664 . 4cathepsin s 189 - 205 tafqyiidnkgidsdas 68 17 dr8 - 3 - 63 1857 . 9 1857 . 1cystatin sn 41 - 58 deyyrrllrvlrareqiv 250 18 dr8 - 3 - 63 2348 . 7 2348 . 0tubulin α - 1 chain 207 - 223 eaiydicrrnldierpt 251 17 dr8 - 3 - 63 2077 . 3 2078 . 3 207 - 219 eaiydicrrnldi 252 13 dr8 - 3 - 63 1593 . 8 1595 . 1myosin β - heavy chain 1027 - 1047 helekikkqveqekceiqaal 253 21 dr8 - 3 - 59 2493 . 9 2494 . 0ca release channel 2614 - 2623 rpsmlqhllr 254 10 dr8 - 3 - 68 1250 . 5 1254 . 8cd35 359 - 380 ddfmgqllngrvlfpvnlqlga 255 22 dr8 - 3 - 72 2417 . 8 2421 . 3cd75 106 - 122 iprlqkiwknylsmnky 256 17 dr8 - 3 - 66 2195 . 6 2202 . 1c - myc transfor . prot . 371 - 385 krsffalrdqipdl 257 14 dr8 - 3 - 68 1706 . 0 1709 . 6k - ras trasnfor . prot . 164 - 180 rqyrlkkiskeektpgc 258 17 dr8 - 3 - 54 2064 . 4 2066 . 5calcitonin 38 - 53 epflyilgksrvleaq 69 16 dr8 - 3 - 78 1863 . 2 1848 . 4receptor ( hum ? ) α - enolase (?) 23 -? aevyhdvaaseff . . . 259 ? dr8 - 3 - 54 -- -- plasminogen activator 378 - 396 drpflfvvrhnptgtvlfm 260 19 dr8 - 3 - 59 2246 . 7 2247 . 1inhibitor - 1 133 - 148 mphffrlfrstvkqvd 261 16 dr8 - 3 - 70 2008 . 4 2116 . 4apolipoprotein b - 100 1724 - 1743 knifhfkvnqeglklsndmm 262 20 dr8 - 3 - 62 2393 . 8 2399 . 4 1724 - 1739 knifhfkvnqeglkls 263 16 dr8 - 3 - 57 1902 . 2 1903 . 7 1780 - 1799 ykqtvsldiqpyslvttlns 264 20 dr8 - 3 - 54 2271 . 5 2273 . 7 2646 - 2662 stpeftilntlhipsft 265 17 dr8 - 3 - 80 1918 . 2 1929 . 4 2647 - 2664 tpeftilntlhipsftid 266 18 dr8 - 3 - 80 2059 . 3 2073 . 5 2647 - 2662 tpeftilntlhipsft 267 16 dr8 - 3 - 80 1831 . 1 1841 . 6 2885 - 2900 sntkyfhklnipqldf 268 16 dr8 - 3 - 68 1965 . 2 1969 . 9 2072 - 2088 lpffkflpkyfekkrnt 269 17 dr8 - 3 - 75 2203 . 6 2207 . 0 2072 - 2086 lpffkflpkyfekkr 270 15 dr8 - 3 - 76 1988 . 4 1992 . 6 4022 - 4036 wnfyyspqsspdkkl 271 15 dr8 - 3 - 59 1860 . 0 1863 . 3bovine transferrin 261 - 281 dviwellnhaqehfgkdkske 272 21 dr8 - 3 - 76 2523 . 8 2524 . 9 261 - 275 dviwellinhaqehfg 273 15 dr8 - 3 - 78 1808 . 0 1818 . 1 261 - 273 dviwellnhaqeh 196 13 dr8 - 3 - 73 1603 . 8 1608 . 8von willebrand factor 617 - 636 ialllmasqepqrmsrnfvr 190 20 dr8 - 3 - 59 2360 . 8 2359 . 7 617 - 630 ialllmasqepqrm 189 14 dr8 - 3 - 59 1600 . 9 1601 . 3 mald - ms__________________________________________________________________________ table 9__________________________________________________________________________hom2 / hla - dr1 naturally processed peptidesprotein source position sequence seq id no . length fraction mw mass__________________________________________________________________________ specpseudo hla - a2 103 - 117 vgsdwrflrgyhqya 2 15 h2 / dr1 - 1 - 64 1855 . 0 1854 . 4 104 - 117 gsdwrflrgyhqya 4 14 h2 / dr1 - 1 - 63 1755 . 3 1755 . 2invariant chain 98 - 121 lpkppkpvskmrmatpllmqalpm 7 24 h2 / dr1 - 1 - 77 2676 . 4 2675 . 9 ( ii ) 99 - 122 pkppkpvskmrmatpllmqalpmg 8 24 h2 / dr1 - 1 - 72 2620 . 2 2619 . 7 98 - 120 lpkppkpvskmrmatpllmqalp 9 23 h2 / dr1 - 1 - 73 2545 . 2 2544 . 5 99 - 121 pkppkpvskmrmatpllmqalpm 10 23 h2 / dr1 - 1 - 75 2563 . 2 2562 . 3 100 - 121 kppkpvskmrmatpllmqalpm 11 22 h2 / dr1 - 1 - 75 2466 . 1 2465 . 8 99 - 120 pkppkpvskmrmatpllmqalp 12 22 h2 / dr1 - 1 - 72 2432 . 0 2431 . 7 100 - 120 kppkpvskmrmatpllmqalp 13 21 h2 / dr1 - 1 - 72 2334 . 9 2334 . 2 esi - ms__________________________________________________________________________ table 10__________________________________________________________________________summary of naturally processed peptides bound to nla - dr expressed innormal human spleenprotein source position sequence seq id no . length mw nass__________________________________________________________________________ spechla - dr α - chain 71 / 133 - 156 setvflpredhlfrkfhylpflps 140 24 2976 2982 71 / 136 - 156 vflpredhlfrkfhylpflps 141 21 2659 2666 71 / 136 - 155 vflpredhlfrkfhylpflp 142 20 2572 2579 71 / 136 - 151 vflpredhlfrkfhyl 143 16 2118 2126calgranulin b 33 / 25 - 33 klghpdtln 144 9 994 999 42 / 88 - 114 washekmhegdegpghhhkpglgegtp 145 27 2915 2927 43 / 88 - 114 washekmhegdegpghhhkpglgegtp 146 27 2017 2926hla - b51 42 / 104 - 121 gpdgrllrghnqydgk 188 16 2017 2023kinase c ζ chain ( rat ) 42 / 341 - 446 tlppfqpqitddygld 70 16 1704 1705hla - dr4 β chain 45 / 129 - 144 vrwfrngqeektgvvs 71 16 1892 1894 mald - ms__________________________________________________________________________ __________________________________________________________________________sequence listing ( 1 ) general information :( iii ) number of sequences : 274 ( 2 ) information for seq id no : 1 :( i ) sequence characteristics :( a ) length : 18 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 1 : valglyserasptrpargpheleuargglytyrhisglntyralatyr151015aspgly ( 2 ) information for seq id no : 2 :( i ) sequence characteristics :( a ) length : 15 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 2 : valglyserasptrpargpheleuargglytyrhisglntyrala151015 ( 2 ) information for seq id no : 3 :( i ) sequence characteristics :( a ) length : 14 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 3 : valglyserasptrpargpheleuargglytyrhisglntyr1510 ( 2 ) information for seq id no : 4 :( i ) sequence characteristics :( a ) length : 14 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 4 : glyserasptrpargpheleuargglytyrhisglntyrala1510 ( 2 ) information for seq id no : 5 :( i ) sequence characteristics :( a ) length : 13 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 5 : serasptrpargpheleuargglytyrhisglntyrala1510 ( 2 ) information for seq id no : 6 :( i ) sequence characteristics :( a ) length : 25 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 6 : leuprolysproprolysprovalserlysmetargmetalathrpro151015leuleumetglnalaleuprometgly2025 ( 2 ) information for seq id no : 7 :( i ) sequence characteristics :( a ) length : 24 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 7 : leuprolysproprolysprovalserlysmetargmetalathrpro151015leuleumetglnalaleupromet20 ( 2 ) information for seq id no : 8 :( i ) sequence characteristics :( a ) length : 24 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 8 : prolysproprolysprovalserlysmetargmetalathrproleu151015leumetglnalaleuprometgly20 ( 2 ) information for seq id no : 9 :( i ) sequence characteristics :( a ) length : 23 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 9 : leuprolysproprolysprovalserlysmetargmetalathrpro151015leuleumetglnalaleupro20 ( 2 ) information for seq id no : 10 :( i ) sequence characteristics :( a ) length : 23 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 10 : prolysproprolysprovalserlysmetargmetalathrproleu151015leumetglnalaleupromet20 ( 2 ) information for seq id no : 11 :( i ) sequence characteristics :( a ) length : 22 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 11 : lysproprolysprovalserlysmetargmetalathrproleuleu151015metglnalaleupromet20 ( 2 ) information for seq id no : 12 :( i ) sequence characteristics :( a ) length : 22 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 12 : prolysproprolysprovalserlysmetargmetalathrproleu151015leumetglnalaleupro20 ( 2 ) information for seq id no : 13 :( i ) sequence characteristics :( a ) length : 21 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 13 : lysproprolysprovalserlysmetargmetalathrproleuleu151015metglnalaleupro20 ( 2 ) information for seq id no : 14 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 14 : proprolysprovalserlysmetargmetalathrproleuleumet151015glnalaleupro20 ( 2 ) information for seq id no : 15 :( i ) sequence characteristics :( a ) length : 15 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 15 : lysmetargmetalathrproleuleumetglnalaleupromet151015 ( 2 ) information for seq id no : 16 :( i ) sequence characteristics :( a ) length : 14 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 16 : lysmetargmetalathrproleuleumetglnalaleupro1510 ( 2 ) information for seq id no : 17 :( i ) sequence characteristics :( a ) length : 18 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 17 : ileproalaaspleuargileileseralaasnglycyslysvalasp151015asnser ( 2 ) information for seq id no : 18 :( i ) sequence characteristics :( a ) length : 17 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 18 : argvalglutyrhispheleuserprotyrvalserprolysgluser151015pro ( 2 ) information for seq id no : 19 :( i ) sequence characteristics :( a ) length : 19 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 19 : tyrlyshisthrleuasnglnileaspservallysvaltrpproarg151015argprothr ( 2 ) information for seq id no : 20 :( i ) sequence characteristics :( a ) length : 18 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 20 : tyrlyshisthrleuasnglnileaspservallysvaltrpproarg151015argpro ( 2 ) information for seq id no : 21 :( i ) sequence characteristics :( a ) length : 19 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 21 : aspvalglyglutyrargalavalthrgluleuglyargproaspala151015glutyrtrp ( 2 ) information for seq id no : 22 :( i ) sequence characteristics :( a ) length : 15 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 22 : gluproglygluprogluphelystyrileglyasnmethisgly151015 ( 2 ) information for seq id no : 23 :( i ) sequence characteristics :( a ) length : 17 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 23 : tyrlyshisthrleuasnglnileaspservallysvaltrpproarg151015arg ( 2 ) information for seq id no : 24 :( i ) sequence characteristics :( a ) length : 13 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 24 : prolystyrvallysglnasnthrleulysleualathr1510 ( 2 ) information for seq id no : 25 :( i ) sequence characteristics :( a ) length : 15 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 25 : leuprolysproprolysprovalserlysmetargmetalathr151015 ( 2 ) information for seq id no : 26 :( i ) sequence characteristics :( a ) length : 13 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 26 : seraspleuserpheserlysasptrpserphetyrleu1510 ( 2 ) information for seq id no : 27 :( i ) sequence characteristics :( a ) length : 18 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 27 : lysvalpheglyargcysgluleualaalaalametlysarghisgly151015leuasp ( 2 ) information for seq id no : 28 :( i ) sequence characteristics :( a ) length : 18 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 28 : argasnargcyslysglythraspvalglnalatrpileargglycys151015argleu ( 2 ) information for seq id no : 29 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 29 : hisproprohisilegluileglnmetleulysasnglylyslysile151015 ( 2 ) information for seq id no : 30 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 30 : asngluleuglyargphelyshisthraspalacyscysargthrhis151015 ( 2 ) information for seq id no : 31 :( i ) sequence characteristics :( a ) length : 14 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 31 : serlysprolysvaltyrglntrppheaspleuarglystyr1510 ( 2 ) information for seq id no : 32 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 32 : alathrserthrlyslysleuhislysgluproalathrleuilelys151015alaileaspgly20 ( 2 ) information for seq id no : 33 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 33 : proalathrleuilelysalaileaspglyaspthrvallysleumet151015tyrlysglygln20 ( 2 ) information for seq id no : 34 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 34 : aspargvallysleumettyrlysglyglnprometthrpheargleu151015leuleuvalasp20 ( 2 ) information for seq id no : 35 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 35 : valalatyrvaltyrlysproasnasnthrhisgluglnhisleuarg151015lyssergluala20 ( 2 ) information for seq id no : 36 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 36 : glnlysglngluproileasplysgluleutyrproleuthrserleu151015 ( 2 ) information for seq id no : 37 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 37 : glyalaargalaservalleuserglyglygluleuasplystrpglu151015 ( 2 ) information for seq id no : 38 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 38 : argthrleutyrglnasnvalglythrtyrvalservalglythrser151015thrleuasnlys20 ( 2 ) information for seq id no : 39 :( i ) sequence characteristics :( a ) length : 15 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 39 : leulyslysleuvalpheglytyrarglysproleuaspasnile151015 ( 2 ) information for seq id no : 40 :( i ) sequence characteristics :( a ) length : 13 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 40 : lyshisilegluglntyrleulyslysilelysasnser1510 ( 2 ) information for seq id no : 41 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 41 : aspvalphelysgluleulysvalhishisalaasngluasnilephe151015 ( 2 ) information for seq id no : 42 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 42 : glyaspthrargproargpheleutrpglnleulyspheglucyshis151015phepheasngly20 ( 2 ) information for seq id no : 43 :( i ) sequence characteristics :( a ) length : 22 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 43 : thrgluargvalargleuleugluargcysiletyrasnglngluglu151015servalargpheaspser20 ( 2 ) information for seq id no : 44 :( i ) sequence characteristics :( a ) length : 25 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 44 : aspleuleugluglnargargalaalavalaspthrtyrcysarghis151015asntyrglyvalglygluserphethr2025 ( 2 ) information for seq id no : 45 :( i ) sequence characteristics :( a ) length : 17 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 45 : lysalagluargalaaspleuilealatyrleulysglnalathrala151015lys ( 2 ) information for seq id no : 46 :( i ) sequence characteristics :( a ) length : 24 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 46 : glyargthrglnaspgluasnprovalvalhisphephelysasnile151015valthrproargthrpropropro20 ( 2 ) information for seq id no : 47 :( i ) sequence characteristics :( a ) length : 13 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 47 : proleulysalagluilealaglnargleugluaspval1510 ( 2 ) information for seq id no : 48 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 48 : argglnileleuglyglnleuglnproserleuglnthrglyserglu151015 ( 2 ) information for seq id no : 49 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 49 : ileglnvaltyrserarghisproprogluasnglylysproasnile151015 ( 2 ) information for seq id no : 50 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 50 : ileasnthrlyscystyrlysleugluhisprovalthrglycysgly151015 ( 2 ) information for seq id no : 51 :( i ) sequence characteristics :( a ) length : 14 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 51 : tyrlysleuasnphetyrpheaspleuleuargalalysleu1510 ( 2 ) information for seq id no : 52 :( i ) sequence characteristics :( a ) length : 13 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 52 : ileaspthrleulyslysasngluasnilelysgluleu1510 ( 2 ) information for seq id no : 53 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 53 : aspvalglyglutyrargalavalthrgluleuglyargproaspala151015glutyrtrpasn20 ( 2 ) information for seq id no : 54 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 54 : gluargphealavalasnproglyleuleugluthrsergluglycys151015 ( 2 ) information for seq id no : 55 :( i ) sequence characteristics :( a ) length : 23 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 55 : aspasntyrargglytyrserleuglyasntrpvalcysalaalalys151015phegluserasnphethrgln20 ( 2 ) information for seq id no : 56 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 56 : glualaleuvalargglnglyleualalysvalalatyrvaltyrlys151015proasnasnthr20 ( 2 ) information 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atggccataagtggagtccctgtgctaggatttttcatcatagctgtg48metalaileserglyvalprovalleuglyphepheileilealaval151015ctgatgagcgctcaggaatcatgggctcttcccaagcctcccaagcct96leumetseralaglnglusertrpalaleuprolysproprolyspro202530gtgagcaagatgcgcatggccaccccgctgctgatgcaggcgctgccc144valserlysmetargmetalathrproleuleumetglnalaleupro354045atgtaa150met ( 2 ) information for seq id no : 149 :( i ) sequence characteristics :( a ) length : 10 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 149 : thrglnphevalargpheaspseraspala1510 ( 2 ) information for seq id no : 150 :( i ) sequence characteristics :( a ) length : 10 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 150 : asptrpargpheleuargglytyrhisgln1510 ( 2 ) information for seq id no : 151 :( i ) sequence characteristics :( a ) length : 10 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id 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seq id no : 242 :( i ) sequence characteristics :( a ) length : 18 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 242 : tyrglnleuleuargsermetileglytyrileglugluleualapro151015ileval ( 2 ) information for seq id no : 243 :( i ) sequence characteristics :( a ) length : 17 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 243 : glyasnhisleutyrlystrplysglnileproaspcysgluasnval151015lys ( 2 ) information for seq id no : 244 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 244 : leuprophepheleupheargglnalatyrhisproasnasnserser151015provalcystyr20 ( 2 ) information for seq id no : 245 :( i ) sequence characteristics :( a ) length : 28 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 245 : glnalalysphephealacysilelysargseraspglysercysala151015trptyrargglyalaalaproprolysglngluphe2025 ( 2 ) information for seq id no : 246 :( i ) sequence characteristics :( a ) length : 19 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 246 : glnalalysphephealacysilelysargseraspglysercysala151015trptyrarg ( 2 ) information for seq id no : 247 :( i ) sequence characteristics :( a ) length : 15 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 247 : sergluglupheleuilealaglylysleuglnaspglyleuleu151015 ( 2 ) information for seq id no : 248 :( i ) sequence characteristics :( a ) length : 12 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 248 : asnargsergluglupheleuilealaglylysleu1510 ( 2 ) information for seq id no : 249 :( i ) sequence characteristics :( a ) length : 24 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 249 : glnasnphethrvalilepheaspthrglyserserasnleutrpval151015proservaltyrcysthrserpro20 ( 2 ) information for seq id no : 250 :( i ) sequence characteristics :( a ) length : 18 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 250 : aspglutyrtyrargargleuleuargvalleuargalaargglugln151015ileval ( 2 ) information for seq id no : 251 :( i ) sequence characteristics :( a ) length : 17 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 251 : glualailetyraspilecysargargasnleuaspilegluargpro151015thr ( 2 ) information for seq id no : 252 :( i ) sequence characteristics :( a ) length : 13 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 252 : glualailetyraspilecysargargasnleuaspile1510 ( 2 ) information for seq id no : 253 :( i ) sequence characteristics :( a ) length : 21 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 253 : hisgluleuglulysilelyslysglnvalgluglnglulyscysglu151015ileglnalaalaleu20 ( 2 ) information for seq id no : 254 :( i ) sequence characteristics :( a ) length : 10 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 254 : argprosermetleuglnhisleuleuarg1510 ( 2 ) information for seq id no : 255 :( i ) sequence characteristics :( a ) length : 22 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 255 : aspaspphemetglyglnleuleuasnglyargvalleupheproval151015asnleuglnleuglyala20 ( 2 ) information for seq id no : 256 :( i ) sequence characteristics :( a ) length : 17 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 256 : ileproargleuglnlysiletrplysasntyrleusermetasnlys151015tyr ( 2 ) information for seq id no : 257 :( i ) sequence characteristics :( a ) length : 14 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 257 : lysargserphephealaleuargaspglnileproaspleu1510 ( 2 ) information for seq id no : 258 :( i ) sequence characteristics :( a ) length : 17 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 258 : argglntyrargleulyslysileserlysgluglulysthrprogly151015cys ( 2 ) information for seq id no : 259 :( i ) sequence characteristics :( a ) length : 13 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 259 : alagluvaltyrhisaspvalalaalasergluphephe1510 ( 2 ) information for seq id no : 260 :( i ) sequence characteristics :( a ) length : 19 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 260 : aspargpropheleuphevalvalarghisasnprothrglythrval151015leuphemet ( 2 ) information for seq id no : 261 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 261 : metprohisphepheargleupheargserthrvallysglnvalasp151015 ( 2 ) information for seq id no : 262 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 262 : lysasnilephehisphelysvalasnglngluglyleulysleuser151015asnaspmetmet20 ( 2 ) information for seq id no : 263 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 263 : lysasnilephehisphelysvalasnglngluglyleulysleuser151015 ( 2 ) information for seq id no : 264 :( i ) sequence characteristics :( a ) length : 20 ( b ) type : amino 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sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 268 : serasnthrlystyrphehislysleuasnileproglnleuaspphe151015 ( 2 ) information for seq id no : 269 :( i ) sequence characteristics :( a ) length : 17 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 269 : leuprophephelyspheleuprolystyrpheglulyslysargasn151015thr ( 2 ) information for seq id no : 270 :( i ) sequence characteristics :( a ) length : 15 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 270 : leuprophephelyspheleuprolystyrpheglulyslysarg151015 ( 2 ) information for seq id no : 271 :( i ) sequence characteristics :( a ) length : 15 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 271 : trpasnphetyrtyrserproglnserserproasplyslysleu151015 ( 2 ) information for seq id no : 272 :( i ) sequence characteristics :( a ) length : 21 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 272 : aspvaliletrpgluleuleuasnhisalaglngluhispheglylys151015asplysserlysglu20 ( 2 ) information for seq id no : 273 :( i ) sequence characteristics :( a ) length : 16 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 273 : aspvaliletrpgluleuleuileasnhisalaglngluhisphegly151015 ( 2 ) information for seq id no : 274 :( i ) sequence characteristics :( a ) length : 23 ( b ) type : amino acid ( c ) strandedness :( d ) topology : linear ( xi ) sequence description : seq id no : 274 : metproargserargalaleuileleuglyvalleualaleuthrthr151015metleuserleucysglygly20__________________________________________________________________________