- Abstract:
-
The gp120/gp41 HIV-1 envelope glycoprotein (Env) is highly glycosylated, with up to 50% of its mass consisting of N-linked glycans. This dense carbohydrate coat has emerged as a promising vaccine target, with its glycans acting as epitopes for a number of potent and broadly neutralizing antibodies (bnAbs). Characterizing the glycan structures present on native HIV-1 Env is thus a critical goal for the design of Env immunogens. In this study, we used a complementary, multistep approach involvi...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 3.0MB)
-
- Publisher copy:
- 10.1128/JVI.01190-15
-
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- Publisher:
- American Society for Microbiology Publisher's website
- Journal:
- Journal of Virology Journal website
- Volume:
- 89
- Issue:
- 17
- Pages:
- 8932-8944
- Publication date:
- 2015-06-17
- Acceptance date:
- 2015-06-08
- DOI:
- ISSN:
-
0022-538X and 1098-5514
- Pubs id:
-
pubs:607248
- URN:
-
uri:6fdc7d93-b6fa-4b12-b895-b7da6a33fc8d
- UUID:
-
uuid:6fdc7d93-b6fa-4b12-b895-b7da6a33fc8d
- Local pid:
- pubs:607248
- Paper number:
- 17
- Copyright holder:
- American Society for Microbiology
- Copyright date:
- 2015
- Notes:
-
This is the
publisher's version of a journal article published by The American Society for Microbiology in Journal of Virology on 2015-06-17, available online: http://dx.doi.org/10.1128/JVI.01190-15
Journal article
Cell- and protein-directed glycosylation of native cleaved HIV-1 envelope
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