Scytovirin Engineering Improves Carbohydrate Affinity and HIV-1 Entry Inhibition | OMICS International | Abstract
ISSN: 2168-9652

Biochemistry & Physiology: Open Access
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Research Article

Scytovirin Engineering Improves Carbohydrate Affinity and HIV-1 Entry Inhibition

Hana McFeeters1, Morgan J. Gilbert1, Alexandra M. Wood1, Charity B. Haggenmaker1, Jennifer Jones2, Olaf Kutsch2 and Robert L. McFeeters1*
1Department of Chemistry, University of Alabama in Huntsville, 301 Sparkman Dr, Huntsville, AL 35899, USA
2Department of Medicine, Division of Infectious Diseases, University of Alabama at Birmingham, Birmingham, AL 35294, USA
*Corresponding Author : Robert L. McFeeters
Department of Chemistry
University of Alabama in Huntsville
301 Sparkman Dr, Huntsville
AL 35899, USA
Tel: (+1)-256-824-6023
Fax: (+1)-256-824-6349
Email: [email protected]
Received December 13, 2012; Accepted January 15, 2013; Published January 21, 2013
Citation: McFeeters H, Gilbert MJ, Wood AM, Haggenmaker CB, Jones J, et al. (2013) Scytovirin Engineering Improves Carbohydrate Affinity and HIV-1 Entry Inhibition. Biochem Physiol S2:003. doi:10.4172/2168-9652.S2-003
Copyright: © 2013 McFeeters H, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


Scytovirin, a cyanobacterium derived carbohydrate binding protein, acts as a potent HIV-1 entry inhibitor and could hold promise as a potential topical microbicide. Viral specificity is achieved as Scytovirin recognizes carbohydrate moieties rarely found in the extracellular matrix, but which are abundant on viral proteins. With the goal to improve the anti-viral capacity of Scytovirin, we here analyze the factors contributing to the Scytovirin anti-viral effect. We show that aromatic substitutions in the lower affinity C-terminal domain of Scytovirin lead to tighter carbohydrate binding. Several other mutations or an addition to the N-terminal abolish carbohydrate binding and abrogate the antiviral effect. Moreover, the increased binding affinity translates directly to improved antiviral efficacy. These studies improve our understanding of the Scytovirin:carbohydrate interaction and provide a blueprint for additional targeted mutations to advance Scytovirin as an entry inhibitor.


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