instruction:
In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.
question:
Synthetic decapeptides (N ¼ 206) covering the entire sequence of mouse liver fumarylacetoacetate hydrolase (FAH) were used to analyze the specificities of the autoantibodies (autoAb) elicited towards this enzyme in mice infected with mouse hepatitis virus (MHV). These autoAb bound mainly to N-and C-terminal FAH peptides, the most reactive sequences being 1e50 and 390e420, respectively. Surprisingly, although FAH sequence 1e50 shares a high degree of homology with various MHV proteins, the C-terminal portion does not. Moreover, whereas the autoAb reacted with homologous peptides surrounding residues 70, 160 and 360, non-similar sequences around residues 130, 210, 240, 250, and 300 were also recognized, indicating that autoAb were not restricted to epitopes with sequence homologies. There was also a lack of correlation between the amount of anti-MHV or anti-FAH antibodies produced and the reactivity towards the peptides. Moreover, the spectrum of peptides recognized by the autoAb of a given mouse did not change significantly with time, which suggests that the MHV-elicited autoimmune response does not induce an epitope recognition spreading. Finally, anti-FAH Ab produced after immunization with rat liver FAH recognized essentially the same mouse FAH regions than autoAb from MHV-infected mice. Results indicated that the induction of the autoAb is not only related to molecular or structural mimicry, but rather supports the Danger model, in which any aggression, in this case the MHV infection, is susceptible to trigger the production of autoAb.
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The peptide specificities of the autoantibodies elicited by mouse hepatitis virus A59


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Ability of CD8 + T cells to act as cytolytic effectors and produce IFN-γ was shown to mediate resistance to Toxoplasma gondii in murine models due to recognition of peptides restricted by murine MHC Class I molecules. However, no T. gondii specific HLA-B07 restricted peptides were proven protective against T gondii. Recently, two T gondii-specific HLA-B*0702-restricted T cell epitopes, GRA7 20-28 (LPQFATAAT) and GRA3 27-35 (VPFVVFLVA), displayed highaffinity binding to HLA-B*0702, and elicited IFN-γ from PBMCs of seropositive HLA-B*0702 persons. Herein, these peptides were evaluated to determine whether they could elicit IFN-γ in splenocytes of HLA-B*0702 transgenic mice when administered with adjuvants and protect against subsequent challenge. Peptide-specific IFN-γ producing T cells were identified by ELISPOT and proliferation assays utilizing splenic T lymphocytes from HLA transgenic mice. When HLA-B*0702 mice were immunized with one of the epitopes identified, GRA7 20-28 in conjunction with a universal CD4 + T cell epitope (PADRE) and adjuvants (CD4 + T cell adjuvant, GLA-SE, and TLR2 stimulatory Pam 2 Cys for CD8 + T cells), this immunization induced CD8 + T cells to produce IFN-γ and protected mice against high parasite burden when challenged with T gondii. This work demonstrates feasibility of bioinformatics followed by an empirical approach based on HLA binding to test this biological activity for identifying protective HLA-B*0702 restricted T gondii peptides and adjuvants that elicit protective immune responses in HLA-B*0702 mice.
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Toxoplasma gondii HLA-B*0702 restricted GRA7 20-28 peptide with adjuvants and an universal helper T cell epitope elicits CD8 + T cells producing IFN-γ and reduces parasite burden in HLA- B*0702 mice 1 NIH Public Access


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Vectors for expression of h9/14, h9/14A5, h9-3A/14 were described in (1,2). Plasmids encoding the eukaryotic translation initiation factors eIF1, 1A, 4A, 4B, 4G, 5, 5B and Escherichia coli Met-tRNA synthetase were described in (3). pGL3R-βglo, pGL3R-βact, pGL3R-L1, pGL3R-HCV, pGL3R-EMCV, pGl3R-CrPV were the kind gift of Dr. Sergey Dmitriev (4). PCR fragments amplified from these constructs and containing the Firefly luciferase ORF fused to 5ʼ-UTRs of β-globin, β-actin, LINE-1, HCV IRES or CrPV IRES under the control of SP6 promoter was inserted to pUC18 plasmid digested by HindIII and EcoRI to generate pUCβglo, pUCβact and pUCL1, and by PstI and EcoRI to generate pUCHCV and pUCCrPV. Vectors for in vivo expression of monocistronic mRNAs containing Firefly luciferase ORF fused to 5ʼ-UTRs of β-globin, β-actin and LINE-1 were prepared by insertion of PCR fragment containing respective 5ʼ-UTRs to pGL3R-EMCV digested by AflII and NcoI to remove upstream Renilla luciferase ORF and EMCV IRES. Plasmid pCrPV-VHLM was constructed by insertion of T7 promoter, CrPV IRES nucleotides 6028 to 6216 followed by a short ORF encoding Val-His-Leu-Met tripeptide, UAA stop codon and 100 nt random sequence taken from β-glucuronidase (GUS) gene, into the pUC18 vector. Plasmids pscAluYb8, pscAluYf2, pscAluYj4 were obtained from the plasmids pscAlu/α-feto and pSscAlu/LDL (1) using quick change protocol. pSAlu110 and pSAlu151 contained the Alu portion of 7SL RNA gene (nucleotides 1-74; 271-299 and 1-99; 251-299, respectively) with a closing loop GATT following position 74 or 99, preceded by the T7 promoter. [ 32 P]-MVHL-stop mRNA synthesis [ 32 P]-UTP was added to the transcription reaction. Preprolactin and MVHL-stop mRNAs were synthesized with SP6 RNA polymerase from plasmids pSP-BP4 (8) and MVHL-stop (9) linearized with EcoRI and XhoI. Capped and uncapped RNAs encoding Firefly luciferase fused to various 5ʼ-UTRs were synthesized with SP6 RNA polymerase from plasmids pUCβglo, pUCβact, pUCL1, pUCCHV and pUCCrPV linearized with EcoRI. HCV-NSʼ and CrPV-VHLM mRNAs were synthesized with T7 RNA polymerase from plasmids pXL.HCV(40-373).NSʼ (10) and pCrPV-VHLM linearized with EcoRI and SspI, respectively. The mRNAs were purified by LiCl precipitation, G50 sepharose chromatography, ethanol precipitation, and resuspended in water. Non-coding AluY A , scAluY A , scAluY L , and 4.5S RNAs were synthesized with T7 RNA polymerase from plasmids pPAlu, pPscAlu/a feto, pSscAlu/LDL and pS4.5S (1) linearized with SspI, SpeI, SpeI and Andreev, D.E., Dmitriev, S.E., Terenin, I.M., Prassolov, V.S., Merrick, W.C. and Shatsky, I.N. (2009) Differential contribution of the m7G-cap to the 5' end-dependent translation initiation of mammalian mRNAs. Nucleic Acids Res., 37, 6135-6147. 5. Dewannieux, M., Esnault, C. and Heidmann, T. (2003) LINE-mediated retrotransposition of marked Alu sequences. Nat. Genet., 35, 41-48. 6. Gurevich, V.V., Pokrovskaya, I.D., Obukhova, T.A. and Zozulya, S.A. (1991) Preparative in vitro mRNA synthesis using SP6 and T7 RNA polymerases. Anal. Biochem., 195, 207-213. 7. Milligan, J.F. and Uhlenbeck, O.C. (1989) Synthesis of small RNAs using T7 RNA polymerase. Methods Enzymol., 180, 51-62. 8. Siegel, V. and Walter, P. (1988) Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP. Cell, 52, 39-49. 9. Alkalaeva, E.Z., Pisarev, A.V., Frolova, L.Y., Kisselev, L.L. and Pestova, T.V. (2006) In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell, 125, 1125-1136.
answer:

SUPPLEMENTARY DATA Alu RNA regulates the cellular pool of active ribosomes by targeted delivery of SRP9/14 to 40S subunits