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

Hopper, J.T.S. and Ambrose, S. and Grant, O.C. and Krumm, S.A. and Allison, T.M. and Degiacomi, M.T. and Tully, M.D. and Pritchard, L.K. and Ozorowski, G. and Ward, A.B. and Crispin, M. and Doores, K.J. and Woods, R.J. and Benesch, J.L.P. and Robinson, C.V. and Struwe, W.B. (2017) 'The tetrameric plant lectin BanLec neutralizes HIV through bidentate binding to specific viral glycans.', Structure., 25 (5). 773-782.e5.


Select lectins have powerful anti-viral 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 recognizes 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 are required for high-affinity glycan binding and virus neutralization. Unexpectedly we find that BanLec adopts a tetrameric stoichiometry in solution whereby the glycan-binding sites are positioned to optimally target glycosylated viral spikes. The tetrameric architecture, together with bidentate binding to individual glycans, leads to layers of multivalency that drive viral neutralization through enhanced avidity effects. These structural insights will prove useful in engineering successful lectin therapeutics targeting the dense glycan shield of HIV.

Item Type:Article
Full text:(AM) Accepted Manuscript
Available under License - Creative Commons Attribution Non-commercial No Derivatives.
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Publisher statement:© 2017 This manuscript version is made available under the CC-BY-NC-ND 4.0 license
Date accepted:23 March 2017
Date deposited:11 July 2018
Date of first online publication:20 April 2017
Date first made open access:11 July 2018

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