Endoproteolytic cleavage of HIV-1 gp160 envelope precursor occurs after exit from the trans-Golgi network (TGN)

Publisher Website
Google Scholar
Abstract
Summary Endoproteolytic processing of human immunodeficiency virus type 1 (HIV-1) gp160 membrane glycoprotein precursor into gp120 and gp41 is necessary for formation of infectious HIV particles [1]. We have studied the intracellular site of this processing using inhibition of transport at reduced temperature (20 °C). That reduced temperature (20 °C) inhibits the intracellular transport also in Jurkat-tat cells was demonstrated using the Semliki Forest virus p62 precursor processing as model. In HIV-1 infected Jurkat-tat cells the proteolytic processing of gp160 precursor did not occur when the protein was accumulated in the TGN at 20 °C temperature. When the temperature was shifted to 37 °C the HIV-1 gp160, which had accumulated in the TGN at the reduced temperature, was proteolytically processed. The processing of gp160 was inhibited when the temperature reversion was carried out in the presence of brefeldin A (BFA) or aluminium fluoride (ALFn) indicating that the exit from the TGN is required for the proteolytic cleavage of HIV-1 gp160 precursor. The results suggest that the processing of gp160 takes place at a yet unidentified transport step which is distal to the TGN/20 °C block site.