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Completeness of HIV-1 envelope glycan shield at transmission determines neutralization breadth

Abstract:

Densely arranged N-linked glycans shield the HIV-1 envelope (Env) trimer from antibody recognition. Strain-specific breaches in this shield (glycan holes) can be targets of vaccine-induced neutralizing antibodies that lack breadth. To understand the interplay between glycan holes and neutralization breadth in HIV-1 infection, we developed a sequence- and structure-based approach to identify glycan holes for individual Env sequences that are shielded in most M-group viruses. Applying this appr...

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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.2018.09.087

Authors


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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Subgroup:
Target Discovery Institute
Role:
Author
ORCID:
0000-0002-3877-9780
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Grant:
Duke CHAVI-ID, UM1 AI100645
Publisher:
Cell Press Publisher's website
Journal:
Cell Reports Journal website
Volume:
25
Issue:
4
Pages:
893-908.e7
Publication date:
2018-10-23
Acceptance date:
2018-09-26
DOI:
ISSN:
2211-1247
Pubs id:
pubs:923769
URN:
uri:fd2eecea-b29d-4b34-8c95-73d0f281adc4
UUID:
uuid:fd2eecea-b29d-4b34-8c95-73d0f281adc4
Local pid:
pubs:923769

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