The viral infectivity factor (Vif) is essential for the productive infection and 
dissemination of HIV-1 in non-permissive cells that involve most natural HIV-1 
target cells. Vif counteracts the packaging of two cellular cytidine deaminases 
named APOBEC3G (A3G) and A3F by diverse mechanisms including the recruitment of 
an E3 ubiquitin ligase complex and the proteasomal degradation of A3G/A3F, the 
inhibition of A3G mRNA translation or by a direct competition mechanism. In 
addition, Vif appears to be an active partner of the late steps of viral 
replication by participating in virus assembly and Gag processing, thus 
regulating the final stage of virion formation notably genomic RNA dimerization 
and by inhibiting the initiation of reverse transcription. Vif is a small 
pleiotropic protein with multiple domains, and recent studies highlighted the 
importance of Vif conformation and flexibility in counteracting A3G and in 
binding RNA. In this review, we will focus on the oligomerization and RNA 
chaperone properties of Vif and show that the intrinsic disordered nature of 
some Vif domains could play an important role in virus assembly and replication. 
Experimental evidence demonstrating the RNA chaperone activity of Vif will be 
presented.