This Article Full Text Full Text (PDF) Other Versions of this Article: JVI.00189-08v1 82/12/5683    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Google Scholar Articles by Zhou, Y. Articles by Liang, C. PubMed PubMed Citation Articles by Zhou, Y. Articles by Liang, C.

 Previous Article  |  Next Article 

Journal of Virology, June 2008, p. 5683-5692, Vol. 82, No. 12
0022-538X/08/$08.00+0     doi:10.1128/JVI.00189-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Insulin-Like Growth Factor II mRNA Binding Protein 1 Associates with Gag Protein of Human Immunodeficiency Virus Type 1, and Its Overexpression Affects Virus Assembly

McGill AIDS Centre, Lady Davis Institute-Jewish General Hospital, Montreal, Quebec H3T 1E2, Canada,¹ Department of Medicine,² Department of Microbiology and Immunology, McGill University, Montreal, Quebec H3A 2B4, Canada³

Received 27 January 2008/ Accepted 21 March 2008

The assembly of human immunodeficiency virus type 1 (HIV-1) particles is driven by viral Gag protein. This function of Gag not only benefits from its self-multimerization property but also depends on its interaction with a number of cellular factors such as TSG101 and ALIX/AIP1 that promote virus budding and release from cell surfaces. However, interaction with Gag also allows some cellular factors such as APOBEC3G and Trim5 to access viral replication machinery and block viral replication. In this study, we report a new HIV-1 Gag-binding factor named insulin-like growth factor II mRNA binding protein 1 (IMP1). Gag-IMP1 interaction requires the second zinc finger of the nucleocapsid (NC) domain of Gag and the KH3 and KH4 domains of IMP1. A fourfold reduction of HIV-1 infectivity was seen with overexpression of the wild-type IMP1 and its mutant that is able to interact with Gag but not with overexpression of IMP1 mutants exhibiting Gag-binding deficiency. The decreased viral infectivity was further shown as a result of diminished viral RNA packaging, abrogated Gag processing on the cellular membranes, and impeded maturation of virus particles. Together, these results demonstrate that IMP1 interacts with HIV-1 Gag protein and is able to block the formation of infectious HIV-1 particles.

Published ahead of print on 2 April 2008.

This article has been cited by other articles:

• Didierlaurent, L., Houzet, L., Morichaud, Z., Darlix, J.-L., Mougel, M. (2008). The conserved N-terminal basic residues and zinc-finger motifs of HIV-1 nucleocapsid restrict the viral cDNA synthesis during virus formation and maturation. Nucleic Acids Res 36: 4745-4753 [Abstract] [Full Text]