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The tetrameric plant lectin BanLec neutralizes HIV through bidentate binding to specific viral glycans.

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...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.str.2017.03.015

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
More from this funder
Name:
European Research Council
Funding agency for:
Robinson, C
Grant:
Professorship
More from this funder
Name:
Medical Research Council
Funding agency for:
Robinson, C
Grant:
Professorship
MR/K024426/1
More from this funder
Name:
Royal Society
Funding agency for:
Benesch, J
Robinson, C
Grant:
BB/L017733/1
Professorship
More from this funder
Name:
Biotechnology and Biological Sciences Research Council
Funding agency for:
Benesch, J
Struwe, W
Grant:
BB/L017733/1
BB/L017733/1
More from this funder
Name:
National Institute of Allergy and Infectious Diseases
Funding agency for:
Crispin, M
Grant:
1UM1AI100663
Publisher:
Elsevier
Journal:
Structure More from this journal
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
Language:
English
Keywords:
Pubs id:
pubs:691199
UUID:
uuid:d1c45d29-2a51-4672-a816-2042574deb37
Local pid:
pubs:691199
Source identifiers:
691199
Deposit date:
2017-05-11

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