PMID:
     2450679
Authors:
     McCune JM, Rabin LB, Feinberg MB, Lieberman M, Kosek JC, Reyes GR,
     Weissman IL.
Title:
     Endoproteolytic cleavage of gp160 is required for the activation of human 
     immunodeficiency virus.
Journal:
     Cell. 1988 Apr 8;53(1):55-67. doi: 10.1016/0092-8674(88)90487-4.
Abstract:
     The envelope protein of human immunodeficiency virus (HIV) is synthesized as a 
     polyprotein (gp160) and cleaved intracellularly to a gp120-gp41 heterodimer. In 
     this study, the tryptic-like endoproteolytic cleavage site was removed by 
     site-directed mutagenesis and replaced with a chymotryptic-like site. The 
     resultant mutant, RIP7/mut10, was found to be indistinguishable from wild-type 
     HIV when analyzed at the level of proviral replication, RNA processing, protein 
     expression, and viral assembly. However, the gp160 polyprotein was not cleaved 
     and the mutated virions were biologically inactive, until and unless they were 
     exposed to limiting concentrations of chymotrypsin. As is the case for other 
     enveloped mammalian viruses, endoproteolytic cleavage of the HIV envelope protein 
     and release of a unique hydrophobic domain appear to be necessary for the full 
     expression of viral infectivity.

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