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Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies.

Abstract:

The envelope spike of HIV-1 employs a 'glycan shield' to protect itself from antibody-mediated neutralization. Paradoxically, however, potent broadly neutralizing antibodies (bnAbs) that target this shield have been isolated. The unusually high glycan density on the gp120 subunit limits processing during biosynthesis, leaving a region of under-processed oligomannose-type structures, which is a primary target of these bnAbs. Here we investigate the contribution of individual glycosylation site...

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

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Publisher copy:
10.1038/ncomms8479

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Spencer, DI More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Communications Journal website
Volume:
6
Pages:
7479
Publication date:
2015-06-24
DOI:
EISSN:
2041-1723
ISSN:
2041-1723
URN:
uuid:4d5b02a9-32c4-491f-9272-a06415e5cdf8
Source identifiers:
527922
Local pid:
pubs:527922

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