An ultrastructural study was performed on rabbit epithelial RK-13 cells and CD4 human T lymphocyte lines infected with various recombinant vaccinia viruses (RVVs) expressing genes of human immunodeficiency virus (HIV): the mature p17 or p24 gag domain alone, the entire or truncated gene, the reverse transcriptase domain, or the genes with a frameshift mutation. Cells infected with RVVs that produced the gag polyprotein with a predicted of more than 48K showed budding and release of HIV-like particles into the extracellular space. These particles were not observed in cells expressing a truncated gene (p17 and p24 regions). Mature HIV-like particles were observed extracellularly when the entire gene and the protease region of the gene were expressed. In contrast, in cells infected with RVVs that contained the gene with a frameshift mutation, neither recognizable budding structures nor extracellular HIV-like particles could be detected. These results suggest that the gene, particularly its 3′ terminus, is necessary for the assembly of HIV particles. In addition, the protease region of the gene seems to be required for morphological maturation of HIV particles, but complete proteolytic cleavage of the gag protein may prevent bud formation.


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