A Comparison of 5P12-vMIP-II and vMIP-II as HIV-1 Entry Inhibitors | OMICS International | Abstract
ISSN: 2168-9652

Biochemistry & Physiology: Open Access
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Research Article

A Comparison of 5P12-vMIP-II and vMIP-II as HIV-1 Entry Inhibitors

Patricia J LiWang*, Jie Xue, Nai-Wei Kuo and Megan Schill
Molecular Cell Biology, University of California Merced, 5200 North Lake Road, Merced, CA 95343, USA
*Corresponding Author : Patricia J LiWang
Molecular Cell Biology, University of California Merced
5200 North Lake Road, Merced, CA 95343, USA
Tel: 209-228- 4568
Fax: 209-724-4459
E-mail: [email protected]
Received February 22, 2013; Accepted April 23, 2013; Published April 26, 2013
Citation: LiWang PJ, Xue J, Kuo NW, Schill M (2013) A Comparison of 5P12-vMIPII and vMIP-II as HIV-1 Entry Inhibitors. Biochem Physiol S2:005. doi:10.4172/2168-9652.S2-005
Copyright: © 2013 LiWang PJ, 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.


vMIP-II (viral macrophage inflammatory protein-II) is a chemokine analog expressed by human herpesvirus-8 that has the unique ability to bind multiple human chemokine receptors, including CCR5 and CXCR4, representative receptors of two major chemokine subfamilies. This broad binding ability gives vMIP-II powerful anti-inflammatory properties, which have been demonstrated in vitro and in vivo. In addition, vMIP-II is of great interest due to its ability to inhibit HIV infection by both major HIV strains: R5 (strains that enter the host cell using CCR5 as a co-receptor), and X4 (strains that use CXCR4). We have made a vMIP-II variant, “5P12-vMIP-II” in which the N-terminal amino acids of vMIP-II have been replaced by 10 amino acids that have been shown to greatly enhance the anti-HIV potency of the chemokine RANTES for R5 HIV strains. This 5P12-vMIP-II is shown by NMR to be fully folded and similar in structure to wild type vMIP-II. Both vMIP-II and 5P12-vMIP-II showed the ability to inhibit multiple strains of HIV, including several R5 strains and an X4 strain. While the 5P12 N-terminus did not improve the potency of the protein, our results suggest that vMIP-II does not bind CCR5 in the same way as human chemokines. Rather, vMIP-II has sacrificed some binding ability to particular chemokine receptors in order to obtain the ability to bind a broader array of receptors.