APOBEC3 cytidine deaminases: Distinct antiviral actions along the retroviral life cycle

被引：31
作者：
Chiu, YL
Green, WC
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, San Francisco, CA 94141 USA
[4] Univ Calif San Francisco, Dept Immunol, San Francisco, CA 94141 USA
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2006年 / 281卷 / 13期
关键词：
D O I：
10.1074/jbc.R500021200
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：
The field of human immunodeficiency virus ( HIV) biology has been galvanized by the discovery of innate APOBEC3 cytidine deaminases, which pose powerful barriers to the replication of HIV and other retroviruses. Rapid progress has been made in defining their action, intriguing regulation within cells, expanded range of retroviral targets, and counterstrikes utilized by retroviruses against them. Although scientifically fascinating, advances in APOBEC3 biology may lead to new antiviral drugs and improved lentiviral vectors for gene therapy.
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收藏
页码：8309 / 8312
页数：4
相关论文
共 83 条
[1]   APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein [J].
Alce, TM ;
Popik, W .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (33) :34083-34086
[2]   Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes:: Correlation with mutation spectra in vivo [J].
Beale, RCL ;
Petersen-Mahrt, SK ;
Watt, IN ;
Harris, RS ;
Rada, C ;
Neuberger, MS .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 337 (03) :585-596
[3]   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
[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]   Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase [J].
Bransteitter, R ;
Pham, P ;
Scharff, MD ;
Goodman, MF .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (07) :4102-4107
[6]   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
[7]   Optimization of apolipoprotein B mRNA editing by APOBEC1 apoenzyme and the role of its auxiliary factor, ACF [J].
Chester, A ;
Weinreb, V ;
Carter, CW ;
Navaratnam, N .
RNA, 2004, 10 (09) :1399-1411
[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]   Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif [J].
Doehle, BP ;
Schäfer, A ;
Cullen, BR .
VIROLOGY, 2005, 339 (02) :281-288
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