Abstract
Background Identification of cellular factors that negatively or positively regulate HIV-1 replication is essential to understand HIV-1 pathogenesis for development of novel antiviral treatments. The human cytidine deaminase APOBEC3G (A3G) is an intrinsic antiviral factor important for the host-mediated defence against HIV-1. We and others recently identified a panel of A3G-interacting RNA-binding proteins (RBPs) that focused our search for novel HIV-1 cofactors and restriction factors onto these proteins. Mov10, a superfamily-1 putative RNA helicase, interacts with A3G in an RNA-dependent manner. Mov10 associates with the RNA-induced silencing complex pathway and localises to mRNA processing bodies (PBs). Furthermore, orthologs of Mov10 in Arabidopsis thaliana and Drosophila melanogaster are necessary for antiviral small RNA-mediated silencing. Thus, we investigated whether Mov10 restricts HIV-1 replication.
Highlights
Identification of cellular factors that negatively or positively regulate HIV-1 replication is essential to understand HIV-1 pathogenesis for development of novel antiviral treatments
We and others recently identified a panel of A3G-interacting RNA-binding proteins (RBPs) that focused our search for novel HIV-1 cofactors and restriction factors onto these proteins
Materials and methods The effect of Mov10 on HIV-1 virus production and ínfectivity was determined by ectopic expression and silencing of Mov10 in virus-producing HeLa and 293T cell lines
Summary
Identification of cellular factors that negatively or positively regulate HIV-1 replication is essential to understand HIV-1 pathogenesis for development of novel antiviral treatments. We and others recently identified a panel of A3G-interacting RNA-binding proteins (RBPs) that focused our search for novel HIV-1 cofactors and restriction factors onto these proteins. Orthologs of Mov in Arabidopsis thaliana and Drosophila melanogaster are necessary for antiviral small RNA-mediated silencing. Mov induced a significant reduction in the accumulation of minus strand strong stop DNA in the target cell, which likely accounted for the considerable loss in virion infectivity. Mov comprises a 495 residue amino-terminal domain with no known protein motifs, and a 508 residue carboxy-terminal putative RNA helicase domain. To begin to identify important attributes in Mov we mutated known helicase motifs in the full-length protein; overexpression of these mutants determined that the carboxy-terminal putative RNA helicase domain of Mov is necessary for its antiviral activity. RNAi-mediated silencing of endogenous Mov moderately enhanced HIV-1 virion production with no discernable effect on virion infectivity. We tested A3G antiviral activity in the context of Mov silencing, which was unaffected
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