BACKGROUND: Few antibodies are available to study the function of the @entity29003 @entity19 immunoglobulin receptor. @entity1 phage display libraries represent a potential source of single-chain Fv ( @entity3598 ) to facilitate the study of the @entity29003 @entity19 immunoglobulin receptor. OBJECTIVES: To isolate @entity1 @entity3598 specific for @entity19 @entity29003 . STUDY DESIGN: Two @entity1 phage display libraries were selected for reactivity to @entity19 @entity29003 . Those human anti-mouse @entity29003 @entity3598 that were derived from the libraries were characterized with respect to kinetics, cellular binding, epitope specificity and @entity535 sequence. RESULTS: Nine anti-mouse @entity29003 @entity3598 molecules were isolated from two @entity1 phage display libraries (Marks et al., J Mol Biol 1991;222:581-597; Sheets et al., Proc Natl Acad Sci USA, in press). Surface plasmon resonance (SPR) analysis revealed that the human anti-mouse @entity29003 @entity3598 had off-rates ranging from 10(-2) to 10(-3) s-1, with @entity573 values calculated to range between 10(-7) and 10(-9) M. The binding of the @entity2823 -labeled human anti-mouse @entity29003 @entity3598 to @entity19 peritoneal neutrophils was not detected by flow cytometry, due to the rapid off-rates of these monomeric proteins. However, when the human anti-mouse @entity29003 @entity3598 were coated on yellow-green latex particles, all of the @entity1 @entity3598 were found to specifically bind to @entity19 peritoneal neutrophils. Deglycosylation of @entity19 @entity29003 did not diminish the binding of these @entity3598 , suggesting that the @entity3598 molecules recognize a polypeptide epitope on @entity19 @entity29003 . In contrast, denaturation of @entity19 @entity29003 dramatically reduced the binding of the @entity1 @entity3598 , suggesting that the epitopes are conformational. Sequence analysis of the human anti-mouse @entity29003 @entity3598 revealed a high degree of structural similarity among the nine @entity3598 . The DP73 VH gene segment was utilized by four of the nine @entity3598 , while seven of the nine @entity3598 contained the DPL16 V lambda gene segment. The sequence similarities between these @entity3598 suggested that several of the @entity1 @entity3598 may recognize a common epitope on @entity19 @entity29003 . Epitope mapping studies demonstrated that eight of the nine human anti-mouse @entity29003 @entity3598 recognized overlapping epitopes. All of these human anti-mouse @entity29003 @entity3598 competed with the 2.4G2 rat monoclonal anti-mouse @entity29003 /III antibody for binding with @entity19 @entity29003 , suggesting that the targeted epitopes reside in or near the Fc binding pocket of @entity19 @entity29003 . CONCLUSIONS: The availability of novel @entity3598 recognizing @entity19 @entity29003 will facilitate the study of receptor triggering events. Such @entity3598 may prove useful to engage @entity19 @entity29003 for targeted @entity137 or immunization strategies.

Characterization of anti-mouse @entity29003 single-chain Fv fragments derived from XXXX phage display libraries.

@entity1 :: ('9606', 'Species') :: ['human', 'Human'] @entity137 :: ('MESH:D064420', 'Disease') :: ['cytotoxicity'] @entity3598 :: ('10271', 'Species') :: ['sFv'] @entity29003 :: ('14130(Tax:10090)', 'Gene') :: ['Fc gamma RII'] @entity573 :: ('MESH:C537014', 'Disease') :: ['KD'] @entity19 :: ('10090', 'Species') :: ['mouse', 'murine'] @entity535 :: ('CHEBI:33704', 'Chemical') :: ['amino acid'] @entity2823 :: ('MESH:D016650', 'Chemical') :: ['FITC']
@entity1 :: (9606,Species) :: ['human']
