The interaction properties of costimulatory molecules revisited.
B7-1 and B7-2 are generally thought to have comparable structures and affinities for their receptors, CD28 and CTLA-4, each of which is assumed to be bivalent. We show instead (1) that B7-2 binds the two receptors more weakly than B7-1, (2) that, relative to its CTLA-4 binding affinity, B7-2 binds C...
Main Authors: | , , , , , , , , |
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Format: | Journal article |
Language: | English |
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2002
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author | Collins, A Brodie, D Gilbert, R Iaboni, A Manso-Sancho, R Walse, B Stuart, D Van Der Merwe, P Davis, S |
author_facet | Collins, A Brodie, D Gilbert, R Iaboni, A Manso-Sancho, R Walse, B Stuart, D Van Der Merwe, P Davis, S |
author_sort | Collins, A |
collection | OXFORD |
description | B7-1 and B7-2 are generally thought to have comparable structures and affinities for their receptors, CD28 and CTLA-4, each of which is assumed to be bivalent. We show instead (1) that B7-2 binds the two receptors more weakly than B7-1, (2) that, relative to its CTLA-4 binding affinity, B7-2 binds CD28 2- to 3-fold more effectively than B7-1, (3) that, unlike B7-1, B7-2 does not self-associate, and (4) that, in contrast to CTLA-4 homodimers, which are bivalent, CD28 homodimers are monovalent. Our results indicate that B7-1 markedly favors CTLA-4 over CD28 engagement, whereas B7-2 exhibits much less bias. We propose that the distinct structures and binding properties of B7-1 and B7-2 account for their overlapping but distinct effects on T cell responses. |
first_indexed | 2024-03-07T02:52:24Z |
format | Journal article |
id | oxford-uuid:ae1cda3a-34b9-4022-bbea-17fabe95ec1a |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T02:52:24Z |
publishDate | 2002 |
record_format | dspace |
spelling | oxford-uuid:ae1cda3a-34b9-4022-bbea-17fabe95ec1a2022-03-27T03:40:26ZThe interaction properties of costimulatory molecules revisited.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:ae1cda3a-34b9-4022-bbea-17fabe95ec1aEnglishSymplectic Elements at Oxford2002Collins, ABrodie, DGilbert, RIaboni, AManso-Sancho, RWalse, BStuart, DVan Der Merwe, PDavis, SB7-1 and B7-2 are generally thought to have comparable structures and affinities for their receptors, CD28 and CTLA-4, each of which is assumed to be bivalent. We show instead (1) that B7-2 binds the two receptors more weakly than B7-1, (2) that, relative to its CTLA-4 binding affinity, B7-2 binds CD28 2- to 3-fold more effectively than B7-1, (3) that, unlike B7-1, B7-2 does not self-associate, and (4) that, in contrast to CTLA-4 homodimers, which are bivalent, CD28 homodimers are monovalent. Our results indicate that B7-1 markedly favors CTLA-4 over CD28 engagement, whereas B7-2 exhibits much less bias. We propose that the distinct structures and binding properties of B7-1 and B7-2 account for their overlapping but distinct effects on T cell responses. |
spellingShingle | Collins, A Brodie, D Gilbert, R Iaboni, A Manso-Sancho, R Walse, B Stuart, D Van Der Merwe, P Davis, S The interaction properties of costimulatory molecules revisited. |
title | The interaction properties of costimulatory molecules revisited. |
title_full | The interaction properties of costimulatory molecules revisited. |
title_fullStr | The interaction properties of costimulatory molecules revisited. |
title_full_unstemmed | The interaction properties of costimulatory molecules revisited. |
title_short | The interaction properties of costimulatory molecules revisited. |
title_sort | interaction properties of costimulatory molecules revisited |
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