Characterization of APOBEC3G binding to 7SL RNA

Daniel Bach^*¹ , Shyam Peddi^*¹ , Bastien Mangeat¹^,2 , Asvin Lakkaraju³ , Katharina Strub³ and Didier Trono¹

¹Global Health Institute, School of Life Sciences and "Frontiers in Genetics", National Center for Competence in Research, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015, Lausanne, Switzerland

²Departments of Dermatology and Venerology, University Hospital, and of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland

³Department of Cell Biology, University of Geneva, CH-1211, Geneva, Switzerland

author email corresponding author email* Contributed equally

Retrovirology 2008, 5:54doi:10.1186/1742-4690-5-54


Published:	2 July 2008

Abstract

Human APOBEC3 proteins are editing enzymes that can interfere with the replication of exogenous retroviruses such as human immunodeficiency virus (HIV), hepadnaviruses such as hepatitis B virus (HBV), and with the retrotransposition of endogenous retroelements such as long-interspersed nuclear elements (LINE) and Alu. Here, we show that APOBEC3G, but not other APOBEC3 family members, binds 7SL RNA, the common ancestor of Alu RNAs that is specifically recruited into HIV virions. Our data further indicate that APOBEC3G recognizes 7SL RNA and Alu RNA by its common structure, the Alu domain, suggesting a mechanism for APOBEC3G- mediated inhibition of Alu retrotransposition. However, we also demonstrate that APOBEC3F and APOBEC3G are normally recruited into and inhibit the infectivity of ΔVif HIV1 virions when 7SLRNA is prevented from accessing particles by RNA interference against SRP14 or by over expression of SRP19, both components of the signal recognition particle. We thus conclude that 7SL RNA is not an essential mediator of the virion packaging of these antiviral cytidine deaminases.