Proteolytic activity, the carboxy terminus of Gag, and the primer binding site are not required for Pol incorporation into foamy virus particles.
Human foamy virus (HFV) is the prototype member of the spumaviruses. While similar in genomic organization to other complex retroviruses, foamy viruses share several features with their more distant relatives, the hepadnaviruses such as human hepatitis B virus (HBV). Both HFV and HBV express their Pol proteins independently from the structural proteins. However unlike HBV, Pol is not required for assembly of HFV core particles or for packaging of viral RNA. These results suggest that the assembly of Pol into HFV particles must occur by a mechanism different from those used by retroviruses and hepadnaviruses. We have examined possible mechanisms for HFV Pol incorporation, including the role of proteolysis in assembly of Pol and the role of initiation of reverse transcription. We have found that proteolytic activity is not required for Pol incorporation. p4 Gag and the residues immediately upstream of the cleavage site in Gag are also not important. Deletion of the primer binding site had no effect on assembly, ruling out early steps of reverse transcription in the process of Pol incorporation.
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA.
D N
DN
Baldwin
M L
ML
Linial
D001665:Binding Sites; D015683:Gene Products, gag / Q000378:metabolism*; D015684:Gene Products, pol / Q000378:metabolism*; D006801:Humans; D011499:Protein Processing, Post-Translational; D012367:RNA, Viral; D016092:Spumavirus / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D014771:Virion; D019065:Virus Assembly
D015683:Gene Products, gag; D015684:Gene Products, pol; D012367:RNA, Viral