Human immunodeficiency virus type 2 glycoprotein enhancement of particle budding: role of the cytoplasmic domain.
Previous studies have shown that the glycoprotein cytoplasmic domains of human immunodeficiency virus type 2 (HIV-2) or simian immunodeficiency virus of macaques modulate biological activities of the viral glycoprotein complex, including syncytium formation, exterior glycoprotein conformation, and glycoprotein incorporation into budding virus particles. We have now utilized a recombinant expression system to study interactions of full-length or truncated HIV-2 glycoproteins with coexpressed HIV-2 Gag proteins which self-assemble and bud as virus-like particles. Interestingly, budding of HIV-2 virus-like particles from cells was enhanced 5- to 24-fold when Gag was coexpressed with the full-length HIV-2 glycoprotein, compared with Gag expressed either alone or with a truncated HIV-2 glycoprotein. The results obtained in this model system indicate that an additional effect of the lengthy cytoplasmic domain of the glycoprotein of HIV-2 is enhancement of particle budding. We speculate that the cytoplasmic domain of the viral glycoprotein of HIV-2 enhances budding by (i) potentiation of Gag structure or function or (ii) membrane modulation.
Ritter
G D
GD
Department of Medicine, University of Alabama at Birmingham, USA.
Yamshchikov
G
G
Cohen
S J
SJ
Mulligan
M J
MJ
D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D017931:DNA Primers; D015683:Gene Products, gag / Q000235:genetics / Q000502:physiology; D006023:Glycoproteins / Q000235:genetics / Q000502:physiology*; D015498:HIV-2 / Q000235:genetics / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D014764:Viral Proteins / Q000235:genetics / Q000502:physiology*; D014779:Virus Replication
D017931:DNA Primers; D015683:Gene Products, gag; D006023:Glycoproteins; D014764:Viral Proteins