Characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells
Abstract The T cell recognition of globular protein antigens requires the cell surface presentation of the protein by Ia‐expressing antigen‐presenting cells (APC). The mechanisms by which APC function remain to be elucidated. To gain a better understanding of association of antigen with APC surfaces...
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crwiley:10.1002/eji.1830200502 2024-06-02T08:14:54+00:00 Characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells Smolenski, Lori A. Kaumaya, Pravin Zouhair Atassi, M. Pierce, Susan K. 1990 http://dx.doi.org/10.1002/eji.1830200502 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Feji.1830200502 https://onlinelibrary.wiley.com/doi/pdf/10.1002/eji.1830200502 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Immunology volume 20, issue 5, page 953-960 ISSN 0014-2980 1521-4141 journal-article 1990 crwiley https://doi.org/10.1002/eji.1830200502 2024-05-03T11:51:55Z Abstract The T cell recognition of globular protein antigens requires the cell surface presentation of the protein by Ia‐expressing antigen‐presenting cells (APC). The mechanisms by which APC function remain to be elucidated. To gain a better understanding of association of antigen with APC surfaces, a large panel of peptides of diverse physicochemical properties was assayed for the ability to compete with presented antigen for binding sites on the APC surface. Competition was measured by the ability of a peptide to block the I‐E k ‐restricted T cell response to pigeon cytochrome c (P c ) as presented by APC. The panel assayed included overlapping peptides representing the entire length of sperm whale myoglobin and the α and β chains of human adult hemoglobin as well as synthetic conformational peptides of lactate dehydrogenase C4 exhibiting stable secondary, α‐helical structures. The results presented hereshow that several peptides of this group compete with the presented form of P c forbinding sites on the APC. However, there is no single biochemical property or amino acid sequence algorithm which predicts the blocking ability. The peptides which compete with presented P c are not predicted to assume the amphipathic α‐helical conformation hypothesized by De Lisi and Berzofsky ( Proc. Natl. Acad. Sci. USA 1986. 82: 7048) for T cell antigenic peptides. However, peptides designed and synthesized to adopt a stable α‐helical secondary structure show more potent blocking activity than the corresponding linear peptides, suggesting that the secondary structure may indeed be a contributing factor in the ability of presented antigenic peptides to be bound by the APC. The results with the myoglobin and hemoglobin peptides show no connection between any particular secondary structure of the peptide in the native proteins and the ability of the peptides to block presentation. Further, there is no correlation between the major histocompatibility complex restriction of the competing peptides and their ability to block the ... Article in Journal/Newspaper Sperm whale Wiley Online Library European Journal of Immunology 20 5 953 960 |
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Open Polar |
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Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
Abstract The T cell recognition of globular protein antigens requires the cell surface presentation of the protein by Ia‐expressing antigen‐presenting cells (APC). The mechanisms by which APC function remain to be elucidated. To gain a better understanding of association of antigen with APC surfaces, a large panel of peptides of diverse physicochemical properties was assayed for the ability to compete with presented antigen for binding sites on the APC surface. Competition was measured by the ability of a peptide to block the I‐E k ‐restricted T cell response to pigeon cytochrome c (P c ) as presented by APC. The panel assayed included overlapping peptides representing the entire length of sperm whale myoglobin and the α and β chains of human adult hemoglobin as well as synthetic conformational peptides of lactate dehydrogenase C4 exhibiting stable secondary, α‐helical structures. The results presented hereshow that several peptides of this group compete with the presented form of P c forbinding sites on the APC. However, there is no single biochemical property or amino acid sequence algorithm which predicts the blocking ability. The peptides which compete with presented P c are not predicted to assume the amphipathic α‐helical conformation hypothesized by De Lisi and Berzofsky ( Proc. Natl. Acad. Sci. USA 1986. 82: 7048) for T cell antigenic peptides. However, peptides designed and synthesized to adopt a stable α‐helical secondary structure show more potent blocking activity than the corresponding linear peptides, suggesting that the secondary structure may indeed be a contributing factor in the ability of presented antigenic peptides to be bound by the APC. The results with the myoglobin and hemoglobin peptides show no connection between any particular secondary structure of the peptide in the native proteins and the ability of the peptides to block presentation. Further, there is no correlation between the major histocompatibility complex restriction of the competing peptides and their ability to block the ... |
format |
Article in Journal/Newspaper |
author |
Smolenski, Lori A. Kaumaya, Pravin Zouhair Atassi, M. Pierce, Susan K. |
spellingShingle |
Smolenski, Lori A. Kaumaya, Pravin Zouhair Atassi, M. Pierce, Susan K. Characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells |
author_facet |
Smolenski, Lori A. Kaumaya, Pravin Zouhair Atassi, M. Pierce, Susan K. |
author_sort |
Smolenski, Lori A. |
title |
Characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells |
title_short |
Characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells |
title_full |
Characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells |
title_fullStr |
Characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells |
title_full_unstemmed |
Characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells |
title_sort |
characteristics of peptides which compete for presented antigen‐binding sites on antigen‐presenting cells |
publisher |
Wiley |
publishDate |
1990 |
url |
http://dx.doi.org/10.1002/eji.1830200502 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Feji.1830200502 https://onlinelibrary.wiley.com/doi/pdf/10.1002/eji.1830200502 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
European Journal of Immunology volume 20, issue 5, page 953-960 ISSN 0014-2980 1521-4141 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/eji.1830200502 |
container_title |
European Journal of Immunology |
container_volume |
20 |
container_issue |
5 |
container_start_page |
953 |
op_container_end_page |
960 |
_version_ |
1800738908783247360 |