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| Article Authors: | S S Tevethia; M Lewis; Y Tanaka; J Milici; B Knowles; W L Maloy; R Anderson |
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| Article Title: | Dissection of H-2Db-restricted cytotoxic T-lymphocyte epitopes on simian virus 40 T antigen by the use of synthetic peptides and H-2Dbm mutants. |
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| Reference ID: | 1008297 |
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| Abstract: | Five distinct cytotoxic T-lymphocyte (CTL) recognition sites were identified in the simian virus 40 (SV40) T antigen by using H-2b cells that express the truncated T antigen or antigens carrying internal deletions of various sizes. Four of the CTL recognition determinants, designated sites I, II, III, and V, are H-2Db restricted, while site IV is H-2Kb restricted. The boundaries of CTL recognition sites I, II, and III, clustered in the amino-terminal half of the T antigen, were further defined by use of overlapping synthetic peptides containing amino acid sequences previously determined to be required for recognition by T-antigen site-specific CTL clones by using SV40 deletion mutants. CTL clone Y-1, which recognizes epitope I and whose reactivity is affected by deletion of residues 193 to 211 of the T antigen, responded positively to B6/PY cells preincubated with a synthetic peptide corresponding to T-antigen amino acids 205 to 219. CTL clones Y-2 and Y-3 lysed B6/PY cells preincubated with large-T peptide LT220-233. To distinguish further between epitopes II and III, Y-2 and Y-3 CTL clones were reacted with SV40-transformed cells bearing mutations in the major histocompatibility complex class I antigen. Y-2 CTL clones lysed SV40-transformed H-2Dbm13 cells (bm13SV) which carry several amino acid substitutions in the putative antigen-binding site in the alpha 2 domain of the H-2Db antigen but not bm14SV cells, which contain a single amino acid substitution in the alpha 1 domain. Y-3 CTL clones lysed both mutant transformants. Y-1 and Y-5 CTL clones failed to lyse bm13SV and bm14SV cells; however, these cells could present synthetic peptide LT205-219 to CTL clone Y-1 and peptide SV26(489-503) to CTL clone Y-5, suggesting that the endogenously processed T antigen yields fragments of sizes or sequences different from those of synthetic peptides LT205-219 and SV26(489-503). |
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| Affiliations: | Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey 17033. |
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| Date: | 1990 |
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| Reference Type: | Literature |
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| PubMed ID: | 1689391 |
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| Journal: | J Virol |
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| Journal Volume: | 64 |
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| Article Pages: | 1192-200 |
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| Journal ISSN: | 1098-5514 |
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| Article Chemical List: | Antigens, Polyomavirus Transforming;Epitopes;H-2 Antigens;Peptides;histocompatibility antigen H-2D(b) |
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| Article MeSH List: | Amino Acid Sequence; Animals; Antigens, Polyomavirus Transforming(immunology); Cell Line; Clone Cells; Epitopes(analysis); Genes, MHC Class I; H-2 Antigens(genetics; immunology); Mice; Mice, Inbred C57BL; Molecular Sequence Data; Mutation; Peptide Mapping; Peptides(chemical synthesis); T-Lymphocytes, Cytotoxic(immunology) |
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| Curation Last Updated: | 2013-05-28 21:16:48 |
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