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Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes
Since class I MHC glycoproteins may function by "screening and selecting" degraded proteins, we wished to determine whether very short peptides made within a cell were detected and bound by MHC, and presented for T cell perusal. We show that a 22 amino acid viral sequence containing a Db-r...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1989
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189441/ https://www.ncbi.nlm.nih.gov/pubmed/2475568 |
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collection | PubMed |
description | Since class I MHC glycoproteins may function by "screening and selecting" degraded proteins, we wished to determine whether very short peptides made within a cell were detected and bound by MHC, and presented for T cell perusal. We show that a 22 amino acid viral sequence containing a Db-restricted nonameric CTL epitope is sufficient to direct CTL recognition/lysis of H2b target cells. The mechanism of epitope presentation is by the "natural" endogenous route, and appears to direct lysis as effectively as wild-type virus infection, in which the epitope is part of a 236 residue glycoprotein. |
format | Text |
id | pubmed-2189441 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1989 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21894412008-04-17 Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes J Exp Med Articles Since class I MHC glycoproteins may function by "screening and selecting" degraded proteins, we wished to determine whether very short peptides made within a cell were detected and bound by MHC, and presented for T cell perusal. We show that a 22 amino acid viral sequence containing a Db-restricted nonameric CTL epitope is sufficient to direct CTL recognition/lysis of H2b target cells. The mechanism of epitope presentation is by the "natural" endogenous route, and appears to direct lysis as effectively as wild-type virus infection, in which the epitope is part of a 236 residue glycoprotein. The Rockefeller University Press 1989-09-01 /pmc/articles/PMC2189441/ /pubmed/2475568 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes |
title | Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes |
title_full | Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes |
title_fullStr | Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes |
title_full_unstemmed | Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes |
title_short | Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes |
title_sort | class i mhc can present an endogenous peptide to cytotoxic t lymphocytes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189441/ https://www.ncbi.nlm.nih.gov/pubmed/2475568 |