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Structural constraints determine the glycosylation of HIV-1 envelope trimers

Abstract:

A highly glycosylated, trimeric envelope glycoprotein (Env) mediates HIV-1 cell entry. The high density and heterogeneity of the glycans shield Env from recognition by the immune system, but paradoxically, many potent broadly neutralizing antibodies (bNAbs) recognize epitopes involving this glycan shield. To better understand Env glycosylation and its role in bNAb recognition, we characterized a soluble, cleaved recombinant trimer (BG505 SOSIP.664) that is a close structural and antigenic mim...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.celrep.2015.05.017

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
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Grant:
Neutralizing Antibody Center CAVD grant
Publisher:
Elsevier (Cell Press) Publisher's website
Journal:
Cell Reports Journal website
Volume:
11
Issue:
10
Pages:
1604-1613
Publication date:
2015-06-04
DOI:
EISSN:
2211-1247
ISSN:
2211-1247
URN:
uuid:2eb7909a-2ad5-4d89-a659-c7c56d1aace2
Source identifiers:
526799
Local pid:
pubs:526799
Language:
English

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