Analysis of the N-terminal positively charged residues of the simian immunodeficiency virus Vif reveals a critical amino acid required for the antagonism of rhesus APOBEC3D, G, and H

被引：2

作者：

Schmitt, Kimberly ^{[1
]}

Katuwal, Miki ^{[1
]}

Wang, Yaqiong ^{[1
]}

Li, Cicy ^{[1
]}

Stephens, Edward B. ^{[1
]}

机构：

[1] Univ Kansas, Med Ctr, Dept Microbiol Mol Genet & Immunol, Kansas City, KS 66160 USA

来源：

VIROLOGY | 2014年 / 449卷

关键词：

APOBEC3; proteins; HIV-1; SIV; SHIV; Vif; Structure-function; Virus restriction; Amino terminus; FUSION INHIBITOR T-20; CD4(+) T-CELLS; HIV-1; VIF; TYPE-1; CYTIDINE DEAMINASE; ANTIVIRAL ACTIVITY; PROVIDES INSIGHT; ENZYME APOBEC3G; RESTRICTS HIV-1; VPU SEQUENCES;

D O I：

10.1016/j.virol.2013.10.037

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Previous studies have shown that apolipoprotein B mRNA editing, enzyme catalytic, polypeptide G (APOBEC3G; hA3G) and F (APOBEC3F; hA3F) proteins interact with a nonlinear binding site located at the N-terminal region of the HIV-1 Vif protein. We have analyzed the role of 12 positively charged amino acids of the N-terminal region of the SIV Vif. Simian-human immunodeficiency viruses (SHIV) were constructed that expressed each of these amino acid substitutions. These viruses were examined for replication in the presence of rhesus macaque APOBEC3 proteins (rhA3A-rhA3H), incorporation of the different A3 proteins into virions, and replication in rhesus macaque PBMC. Similar to other studies, we found that K27 was essential for rhA3G activity and rhA3F but was not important for restriction of SHIV Delta vif by rhA3A, rhA3D or rhA3H. Our results identified the arginine at position 14 of the SIV Vif as a critical residue for virus restriction by rhA3D, rhA3G and rhA3H. (C) 2013 Elsevier Inc. All rights reserved.

引用

页码：140 / 149

页数：10

共 71 条

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