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Journal article

HIV-1 glycan density drives the persistence of the mannose patch within an infected individual

Abstract:

The HIV envelope (Env) is extensively modified with host-derived N-linked glycans. The high density of glycosylation on the viral spike limits enzymatic processing resulting in numerous under-processed oligomannose-type glycans. This extensive glycosylation not only shields conserved regions of the protein from the immune system but also act as targets for HIV broadly neutralizing antibodies (bnAbs). In response to the host immune system, the HIV glycan shield is constantly evolving thro...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1128/JVI.01542-16

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Publisher:
American Society for Microbiology
Journal:
Journal of Virology More from this journal
Volume:
90
Issue:
24
Pages:
11132-11144
Publication date:
2016-01-01
Acceptance date:
2016-09-26
DOI:
EISSN:
1098-5514
ISSN:
0022-538X
Pubs id:
pubs:647229
UUID:
uuid:2464679b-7e1e-4012-9970-847fe0789009
Local pid:
pubs:647229
Source identifiers:
647229
Deposit date:
2016-09-30

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