7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G

被引:133
作者
Wang, Tao
Tian, Chunjuan
Zhang, Wenyan
Luo, Kun
Sarkis, Phuong Thi Nguyen
Yu, Lillian
Liu, Bindong
Yu, Yunkai
Yu, Xiao-Fang
机构
[1] Zhejiang Univ, Sch Med, Affiliated Hosp 2, Hangzhou, Zhejiang, Peoples R China
[2] Jilin Univ, Changchun 130023, Peoples R China
[3] Johns Hopkins Bloomberg Sch Publ Hlth, Dept Mol Microbiol & Immunol, Baltimore, MD 21205 USA
关键词
D O I
10.1128/JVI.00892-07
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Cytidine deaminase APOBEC3G (A3G) has broad antiviral activity against diverse retroviruses and/or retrotransposons, and its antiviral functions are believed to rely on its encapsidation into virions in an RNA-dependent fashion. However, the cofactors of A3G virion packaging have not yet been identified. We demonstrate here that A3G selectively interacts with certain polymerase III (Pol III)-derived RNAs, including Y3 and 7SL RNAs. Among A3G-binding Pol III-derived RNAs, 7SL RNA was preferentially packaged into human immunodeficiency virus type 1 (HIV-1) particles. Efficient packaging of 7SL RNA, as well as A3G, was mediated by the RNA-binding nucleocapsid domain of HIV-1 Gag. A3G mutants that had reduced 7SL RNA binding but maintained wild-type levels of mRNA and tRNA binding were packaged poorly and had impaired antiviral activity. Reducing 7SL RNA packaging by overexpression of SRP19 proteins inhibited 7SL RNA and A3G virion packaging and impaired its antiviral function. Thus, 7SL RNA that is encapsidated into diverse retroviruses is a key cofactor of the antiviral A3G. This selective interaction of A3G with certain Pol III-derived RNAs raises the question of whether A3G and its cofactors may have as-yet-unidentified cellular functions.
引用
收藏
页码:13112 / 13124
页数:13
相关论文
共 80 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]  
Ausubel FM, 2003, CURRENT PROTOCOLS MO
[3]   LOW MOLECULAR WEIGHT RNAS OF ROUS SARCOMA VIRUS .2. 7-S-RNA [J].
BISHOP, JM ;
LEVINSON, WE ;
SULLIVAN, D ;
FANSHIER, L ;
QUINTRELL, N ;
JACKSON, J .
VIROLOGY, 1970, 42 (04) :927-+
[4]   Antiviral potency of APOBEC proteins does not correlate with cytidine deamination [J].
Bishop, Kate N. ;
Holmes, Rebecca K. ;
Malim, Michael H. .
JOURNAL OF VIROLOGY, 2006, 80 (17) :8450-8458
[5]   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
[6]   Cellular inhibitors of long interspersed element 1 and Alu retrotransposition [J].
Bogerd, Hal P. ;
Wiegand, Heather L. ;
Hulme, Amy E. ;
Garcia-Perez, Jose L. ;
O'Shea, K. Sue ;
Moran, John V. ;
Cullen, Bryan R. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (23) :8780-8785
[7]   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
[8]   PROPERTIES OF FELINE LEUKEMIA-VIRUS .3. ANALYSIS OF RNA [J].
BRIAN, DA ;
THOMASON, AR ;
ROTTMAN, FM ;
VELICER, LF .
JOURNAL OF VIROLOGY, 1975, 16 (03) :535-545
[9]   Tools and approaches for the construction of knowledge models from the neuroscientific literature [J].
Burns, GAPC ;
Khan, AM ;
Ghandeharizadeh, S ;
O'Neill, MA ;
Chen, YS .
NEUROINFORMATICS, 2003, 1 (01) :81-109
[10]   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