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...

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Main Authors: Collins, A, Brodie, D, Gilbert, R, Iaboni, A, Manso-Sancho, R, Walse, B, Stuart, D, Van Der Merwe, P, Davis, S
Format: Journal article
Language:English
Published: 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.
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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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