The envelope glycoproteins of HIV are required for viral infectivity.
Proteolgsis of the Precursor envelope glycoprotein gp160 results in th
e formation of gp120 acid gp41. Cleavage occurs after the sequence Arg
-Glu-Lys-Arg. This sequence is expected to be a substrate for the cell
ular protease furin. We examined whether furin is responsible for clea
vage of gp160 by using a furin-deficient CHO cell line and the same ce
ll line transfected with furin cDNA. Data obtained from viral transmis
sion assays suggested that furin increased viral infectivity but was n
ot essential for the maturation of gp160, implying that other proprote
in processing enzymes also recognize this putative furin cleavage site
.