Interaction of gag polyprotein-precursors p55 and p48 with p160gag-pol during formation of virus-like particles of HIV-1 with recombinant strains of vaccinia virus

• Published in: Voprosy virusologiĭ Vol. 42; no. 5; p. 205
• Main Authors: Iordanskiĭ, S N, Lideman, L F, Chikova, A K, Gibadulin, R A
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01-09-1997
• Subjects: Animals; Cell Line; Fusion Proteins, gag-pol - metabolism; Gene Products, gag - metabolism; HIV-1 - metabolism; HIV-1 - physiology; Protein Precursors - metabolism; Recombination, Genetic; Vaccinia virus - genetics; Virion - metabolism; Virion - physiology; Virus Replication
• ISSN: 0507-4088

The polypeptide composition of HIV-I virus-like particles produced by CV-I cells during mono- and coinfection with recombinant vaccinia virus (rVV) strains containing the whole (p55) and carboxyterminal truncated (p48) gag genes and gag-pol sequence is studied. In monoinfection both the gag-strains actively produced virus-like particles consisting of non-processed p55Gag and p48Gag polyprotein without p6 domain. In case of a coinfection of the cells with one of these strains and the rVV producing p160Gag-Pol polyprotein the virus-like particles consisted of p24 protein and a negligible amount of non-processed Gag precursors. The share of p24 protein increased in proportion to the duration of coinfection and decreased with a reduction of multiplicity of infection with rVV carrying p160Gag-Pol. Hence, the absence of p6 domain does not influence the processing of Gag proteins during virus-like particles assembly and budding. In contrast to the natural systems of HIV-I development, in the rVV expression system the p6Gag domain virtually does not contribute to reactions between Gag and Gag-Pol precursors and to the particles' morphogenesis.