A Single Amino Acid in Human APOBEC3F Alters Susceptibility to HIV-1 Vif

被引：45

作者：

Albin, John S. ^{[2
,3
]}

LaRue, Rebecca S. ^{[2
,3
]}

Weaver, Jessalyn A. ^{[2
,3
]}

Brown, William L. ^{[2
,3
]}

Shindo, Keisuke ^{[2
,3
]}

Harjes, Elena ^{[1
,2
]}

Matsuo, Hiroshi ^{[1
,2
]}

Harris, Reuben S. ^{[1
,2
,3
]}

机构：

[1] Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USA

[2] Univ Minnesota, Inst Mol Virol, Minneapolis, MN 55455 USA

[3] Univ Minnesota, Ctr Genome Engn, Minneapolis, MN 55455 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2010年 / 285卷 / 52期

基金：

美国国家卫生研究院;

关键词：

ANTIRETROVIRAL ACTIVITY; RESTRICTION; SENSITIVITY; VARIANTS; HOST; DNA; IDENTIFICATION; DEAMINATION; INHIBITION; REPERTOIRE;

D O I：

10.1074/jbc.M110.173161

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human APOBEC3F (huA3F) potently restricts the infectivity of HIV-1 in the absence of the viral accessory protein virion infectivity factor (Vif). Vif functions to preserve viral infectivity by triggering the degradation of huA3F but not rhesus macaque A3F (rhA3F). Here, we use a combination of deletions, chimeras, and systematic mutagenesis between huA3F and rhA3F to identify Glu(324) as a critical determinant of huA3F susceptibility to HIV-1 Vif-mediated degradation. A structural model of the C-terminal deaminase domain of huA3F indicates that Glu(324) is a surface residue within the alpha 4 helix adjacent to residues corresponding to other known Vif susceptibility determinants in APOBEC3G and APOBEC3H. This structural clustering suggests that Vif may bind a conserved surface present in multiple APOBEC3 proteins.

引用

收藏

页码：40785 / 40792

页数：8

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