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Structural principles controlling HIV envelope glycosylation

Abstract:

The heavily glycosylated, trimeric HIV-1 envelope (Env) protein is the sole viral protein exposed on the HIV-1 virion surface and is thus a main focus of antibody-mediated vaccine development. Dense glycosylation at the outer domain of Env constrains normal enzymatic processing, stalling the glycans at immature oligomannose-type structures. Furthermore, native trimerization imposes additional steric constraints, which generate an extensive ‘trimer-induced mannose patch’. Importantly, the imma...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.sbi.2017.03.008

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Institution:
University of Oxford
Oxford college:
Corpus Christi College
Role:
Author
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Funding agency for:
Behrens, A
Grant:
Chris Scanlan Memorial Scholarship
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Funding agency for:
Crispin, M
Grant:
Fellowship
Publisher:
Elsevier Publisher's website
Journal:
Current Opinion in Structural Biology Journal website
Volume:
44
Pages:
125-133
Publication date:
2017-03-01
Acceptance date:
2017-03-27
DOI:
EISSN:
1879-033X
ISSN:
0959-440X
Source identifiers:
687301
Pubs id:
pubs:687301
UUID:
uuid:fd2b89ea-0a38-456f-934f-6029c4682975
Local pid:
pubs:687301
Deposit date:
2017-03-29

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