- Abstract:
-
Select lectins have powerful antiviral properties that effectively neutralize HIV-1 by targeting the dense glycan shield on the virus. Here, we reveal the mechanism by which one of the most potent lectins, BanLec, achieves its inhibition. We identify that BanLec recognises a subset of high-mannose glycans via bidentate interactions spanning the two binding sites present on each BanLec monomer that were previously considered separate carbohydrate recognition domains. We show that both sites ar...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted manuscript
- Files:
-
-
(pdf, 609.5KB)
-
- Publisher copy:
- 10.1016/j.str.2017.03.015
-
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- Funding agency for:
- Crispin, M
- Funding agency for:
- Crispin, M
- Funding agency for:
- Benesch, JLP
- Publisher:
- Elsevier Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 25
- Issue:
- 5
- Pages:
- 773-782.e5
- Publication date:
- 2017-04-20
- Acceptance date:
- 2017-03-23
- DOI:
- ISSN:
-
1878-4186 and 0969-2126
- Pubs id:
-
pubs:691199
- URN:
-
uri:d1c45d29-2a51-4672-a816-2042574deb37
- UUID:
-
uuid:d1c45d29-2a51-4672-a816-2042574deb37
- Local pid:
- pubs:691199
- Language:
- English
- Keywords:
- Copyright holder:
- Elsevier
- Copyright date:
- 2017
- Notes:
- © 2017 Published by Elsevier Ltd.. This is the accepted manuscript version of the article. The final version is available online from Elsevier at: http://dx.doi.org/10.1016/j.str.2017.03.015
Journal article
The tetrameric plant lectin BanLec neutralizes HIV through bidentate binding to specific viral glycans.
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+ International AIDS Vaccine Initiative Neutralizing Antibody Center
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+ National Institute of Allergy and Infectious Diseases
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+ Biotechnology and Biological Sciences Research Council
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