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Hindi 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: pliwang@ucmerced.edu |
| 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. | |
Abstract
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 We have made a vMIP-II variant, “5P12-vMIP-II” in which the N-terminal amino acids of vMIP-II have been replaced by 10 amino acids that have been shown to greatly enhance the anti-HIV potency of the chemokine RANTES for R5 HIV strains.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.
