Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates

被引:85
作者
Zennou, Veronique
Bieniasz, Paul D. [1 ]
机构
[1] Aaron Diamond AIDS Res Ctr, New York, NY 10016 USA
[2] Rockefeller Univ, New York, NY 10016 USA
关键词
HIV-1; Vif; APOBEC3G; APOBEC3F; hypermutation;
D O I
10.1016/j.virol.2005.12.035
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
APOBEC3G and APOBEC3F exhibit antiretroviral activity primarily as a consequence of their ability to deaminate cytidines in retroviral DNA. Here, we compare the properties of APOBEC3F and APOBEC3G from human, macaque, and African green monkey (AGM). While all APOBEC proteins tested exhibited anti-HIV-1 activity, human APOBEC3F was, surprisingly, 10- to 50-fold less potent than human APOBEC3G. However, similar discrepancies in antiviral potency were not found when pairs of proteins from macaque and AGM were compared. Intrinsic differences in the ability of each APOBEC protein to induce hypermutation, rather than differences in packaging efficiency, partially accounted for variable antiretroviral activity. Each of four primate lentivirus Vif proteins reduced human and AGM APOBEC3F expression and antiviral activity, but all were only partially effective and species-specific effects were relatively minor. Overall, highly efficient and species-specific neutralization of APOBEC3G, and less efficient neutralization of APOBEC3F, appears to be a general property of Vif proteins. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:31 / 40
页数:10
相关论文
共 36 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]   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]   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
[4]   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
[5]   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
[6]   Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120 [J].
Derdeyn, CA ;
Decker, JM ;
Sfakianos, JN ;
Wu, XY ;
O'Brien, WA ;
Ratner, L ;
Kappes, JC ;
Shaw, GM ;
Hunter, E .
JOURNAL OF VIROLOGY, 2000, 74 (18) :8358-8367
[7]   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
[8]   Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion [J].
Doehle, BP ;
Schäfer, A ;
Wiegand, HL ;
Bogerd, HP ;
Cullen, BR .
JOURNAL OF VIROLOGY, 2005, 79 (13) :8201-8207
[9]   HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles [J].
Douaisi, M ;
Dussart, S ;
Courcoul, M ;
Bessou, G ;
Vigne, R ;
Decroly, E .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2004, 321 (03) :566-573
[10]   DNA determination mediates innate immunity to retroviral infection [J].
Harris, RS ;
Bishop, KN ;
Sheehy, AM ;
Craig, HM ;
Petersen-Mahrt, SK ;
Watt, IN ;
Neuberger, MS ;
Malim, MH .
CELL, 2003, 113 (06) :803-809