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Journal of Virology, September 2007, p. 9577-9583, Vol. 81, No. 17
0022-538X/07/$08.00+0     doi:10.1128/JVI.02800-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Differential Inhibition of Long Interspersed Element 1 by APOBEC3 Does Not Correlate with High-Molecular-Mass-Complex Formation or P-Body Association{triangledown}

Anna Maria Niewiadomska,1 Chunjuan Tian,1 Lindi Tan,1 Tao Wang,1 Phuong Thi Nguyen Sarkis,1 and Xiao-Fang Yu1,2*

Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland 21205,1 Second Affiliated Hospital, School of Medicine, Zhejiang University, Zhejiang, China2

Received 19 December 2006/ Accepted 8 June 2007

The human cytidine deaminase APOBEC3G (A3G) and other APOBEC3 proteins exhibit differential inhibitory activities against diverse endogenous retroelements and retroviruses, including Vif-deficient human immunodeficiency virus type 1. The potential inhibitory activity of human APOBEC proteins against long interspersed element 1 (LINE-1) has not been fully evaluated. Here, we demonstrate inhibition of LINE-1 by multiple human APOBEC3 cytidine deaminases, including previously unreported activity for A3DE and A3G. More ancient members of APOBEC, cytidine deaminases AID and APOBEC2, had no detectable activity against LINE-1. A3A, which did not form high-molecular-mass (HMM) complexes and interacted poorly with P bodies, was the most potent inhibitor of LINE-1. A3A specifically recognizes LINE-1 RNA but not the other cellular RNAs tested. However, in the presence of LINE-1, A3A became associated with HMM complexes containing LINE-1 RNA. The ability of A3A to recognize LINE-1 RNA required its catalytic domain and was important for its LINE-1 suppression. Although the mechanism of LINE-1 restriction did not seem to involve DNA editing, A3A inhibited the accumulation of nascent LINE-1 DNA, suggesting interference with LINE-1 reverse transcription and/or integration or intracellular movement of LINE-1 ribonucleoprotein. Thus, association with P bodies or cellular HMM complexes could not predict the potency of APOBEC3 anti-LINE-1 activities. The catalytic domain of APOBEC3 proteins may be important for proper folding and target factors such as RNA or protein interaction in addition to cytidine deamination.

* Corresponding author. Mailing address: Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD 21205. Phone: (410) 955-3768. Fax: (410) 955-0105. E-mail: xfyu{at}jhsph.edu

{triangledown} Published ahead of print on 20 June 2006.

Journal of Virology, September 2007, p. 9577-9583, Vol. 81, No. 17
0022-538X/07/$08.00+0     doi:10.1128/JVI.02800-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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