The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein was expressed by a vaccinia vector that encodes the late promotor P11. The envelope protein synthesized mediated syncytia formation with SupT1 cells and was efficiently cleaved to produce mature gp120 and gp41 in CV-1 cells. gp160 precursor processing was neither affected by a change in culture medium nor by a heterologous vesicular stomatitis virus coinfection. These results suggest that the proteolytic cleavage of gp160 is an efficient process and that coinfection with other viruses may not affect precursor processing of the HIV-1 Env protein.

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