Journal article
Completeness of HIV-1 envelope glycan shield at transmission determines neutralization breadth
- Abstract:
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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
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(Version of record, pdf, 7.0MB)
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- Publisher copy:
- 10.1016/j.celrep.2018.09.087
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Authors
Funding
Bibliographic Details
- 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:
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2211-1247
- Source identifiers:
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923769
Item Description
- Keywords:
- Pubs id:
-
pubs:923769
- UUID:
-
uuid:fd2eecea-b29d-4b34-8c95-73d0f281adc4
- Local pid:
- pubs:923769
- Deposit date:
- 2018-10-05
Terms of use
- Copyright holder:
- Wagh et al
- Copyright date:
- 2018
- Notes:
- This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
- Licence:
- CC Attribution (CC BY)
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