Multifaceted antiviral actions of APOBEC3 cytidine deaminases

被引:46
作者
Chiu, Ya-Lin
Greene, Warner C. [1 ]
机构
[1] Univ Calif San Francisco, Gladstone Inst Virol & Immunol, San Francisco, CA 94141 USA
[2] Univ Calif San Francisco, Dept Med, San Francisco, CA 94141 USA
[3] Univ Calif San Francisco, Dept Microbiol & Immunol, San Francisco, CA 94141 USA
关键词
D O I
10.1016/j.it.2006.04.003
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
To defend against external pathogens, metazoan organisms have evolved numerous defenses that generally fall within the innate and adaptive immune responses. Considerable effort continues to focus on developing a vaccine to manipulate the adaptive immune system to protect against or control HIV-1. However, recent advances in our understanding of the innate immune system have revealed that cells have a potent intrinsic antiretroviral defense in the form of APOBEC3G, which is a member of a larger family of cytidine deaminases that are active against HIV-1 and other retroviruses. Insights into how the action of A3G is circumvented by HIV-1 through the action of its Vif protein, and the surprising mechanisms by which A3G is regulated within the cell, offer exciting new opportunities for developing novel anti-HIV-1 therapies that exploit this intrinsic antiretroviral system.
引用
收藏
页码:291 / 297
页数:7
相关论文
共 82 条
[1]   APOBEC3G genetic variants and their influence on the progression to AIDS [J].
An, P ;
Bleiber, G ;
Duggal, P ;
Nelson, G ;
May, M ;
Mangeat, B ;
Alobwede, I ;
Trono, D ;
Vlahov, D ;
Donfield, S ;
Goedert, JJ ;
Phair, J ;
Buchbinder, S ;
O'Brien, SJ ;
Telenti, A ;
Winkler, CA .
JOURNAL OF VIROLOGY, 2004, 78 (20) :11070-11076
[2]   Cytidine deamination of retroviral DNA by diverse APOBEC proteins [J].
Bishop, KN ;
Holmes, RK ;
Sheehy, AM ;
Davidson, NO ;
Cho, SJ ;
Malim, MH .
CURRENT BIOLOGY, 2004, 14 (15) :1392-1396
[3]   APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells [J].
Bogerd, HP ;
Wiegand, HL ;
Doehle, BP ;
Lueders, KK ;
Cullen, BR .
NUCLEIC ACIDS RESEARCH, 2006, 34 (01) :89-95
[4]   A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor [J].
Bogerd, HP ;
Doehle, BP ;
Wiegand, HL ;
Cullen, BR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (11) :3770-3774
[5]   The interaction between HIV-1 Gag and APOBEC3G [J].
Cen, S ;
Guo, F ;
Niu, MJ ;
Saadatmand, J ;
Deflassieux, J ;
Kleiman, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (32) :33177-33184
[6]   APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons [J].
Chen, H ;
Lilley, CE ;
Yu, Q ;
Lee, DV ;
Chou, J ;
Narvaiza, I ;
Landau, NR ;
Weitzman, MD .
CURRENT BIOLOGY, 2006, 16 (05) :480-485
[7]   APOBEC3 cytidine deaminases: Distinct antiviral actions along the retroviral life cycle [J].
Chiu, YL ;
Green, WC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (13) :8309-8312
[8]   RETRACTED: Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells (Retracted Article. See vol 466, pg 276, 2010) [J].
Chiu, YL ;
Soros, VB ;
Kreisberg, JF ;
Stopak, K ;
Yonemoto, W ;
Greene, WC .
NATURE, 2005, 435 (7038) :108-114
[9]   The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G [J].
Conticello, SG ;
Harris, RS ;
Neuberger, MS .
CURRENT BIOLOGY, 2003, 13 (22) :2009-2013
[10]   Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors [J].
Cullen, BR .
JOURNAL OF VIROLOGY, 2006, 80 (03) :1067-1076