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Journal article

Glycan microheterogeneity at the PGT135 antibody recognition site on HIV-1 gp120 reveals a molecular mechanism for neutralization resistance.

Abstract:

Broadly neutralizing antibodies have been isolated that bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392, and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity...

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

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Publisher copy:
10.1128/jvi.00230-15

Authors


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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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University of Oxford More from this funder
Oriel College, Oxford More from this funder
International AIDS Vaccine Initiative Neutralizing Antibody Center More from this funder
Publisher:
American Society for Microbiology Publisher's website
Journal:
Journal of Virology Journal website
Volume:
89
Issue:
13
Pages:
6952-6959
Publication date:
2015-07-05
DOI:
EISSN:
1098-5514
ISSN:
0022-538X
URN:
uuid:288fb4ce-9692-40b8-a162-b0bd5618db20
Source identifiers:
518361
Local pid:
pubs:518361

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