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
    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
    [J]. JOURNAL OF VIROLOGY, 2004, 78 (20) : 11070 - 11076
  • [2] Cytidine deamination of retroviral DNA by diverse APOBEC proteins
    Bishop, KN
    Holmes, RK
    Sheehy, AM
    Davidson, NO
    Cho, SJ
    Malim, MH
    [J]. CURRENT BIOLOGY, 2004, 14 (15) : 1392 - 1396
  • [3] APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells
    Bogerd, HP
    Wiegand, HL
    Doehle, BP
    Lueders, KK
    Cullen, BR
    [J]. 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
    Bogerd, HP
    Doehle, BP
    Wiegand, HL
    Cullen, BR
    [J]. 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
    Cen, S
    Guo, F
    Niu, MJ
    Saadatmand, J
    Deflassieux, J
    Kleiman, L
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (32) : 33177 - 33184
  • [6] APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons
    Chen, H
    Lilley, CE
    Yu, Q
    Lee, DV
    Chou, J
    Narvaiza, I
    Landau, NR
    Weitzman, MD
    [J]. CURRENT BIOLOGY, 2006, 16 (05) : 480 - 485
  • [7] APOBEC3 cytidine deaminases: Distinct antiviral actions along the retroviral life cycle
    Chiu, YL
    Green, WC
    [J]. 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)
    Chiu, YL
    Soros, VB
    Kreisberg, JF
    Stopak, K
    Yonemoto, W
    Greene, WC
    [J]. NATURE, 2005, 435 (7038) : 108 - 114
  • [9] The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    Conticello, SG
    Harris, RS
    Neuberger, MS
    [J]. CURRENT BIOLOGY, 2003, 13 (22) : 2009 - 2013
  • [10] Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors
    Cullen, BR
    [J]. JOURNAL OF VIROLOGY, 2006, 80 (03) : 1067 - 1076