HIV-Nef protein supports viral infectivity prior to proviral integrati
on. This requires Nef to be present before the expression of viral gen
es and suggests its delivery as part of the virion. We report here tha
t the Nef proteins of HiV-2-HOM and HIV-2-ROD are associated with the
virion. After the separation Of pelleted virus in st 20-60% sucrose de
nsity gradient, both proteins cosedimented with the virion-associated
reverse transcriptase (RT) activity at a density characteristic of ret
roviral particles. Whereas Nef-2-ROD was present in the virion only as
the full-length protein, HIV-2-HOM appeared as 32 and 35 kDa isoforms
. The smaller isoform is identical in molecular weight tb the protein
expected from proteolytic cleavage of full-length Nef-2-HOM by the vir
ion-based protease. Virion-association of Nef helps to explain the rec
ently redefined biological function of this regulatory protein. Copyri
ght (C) 1996 Elsevier Science B.V.