Document 0634
 DOCN  M9550634
 TI    Biochemical and genetic definition of the cellular protease required for
       HIV-1 gp160 processing.
 DT    9505
 AU    Franzusoff A; Volpe AM; Josse D; Pichuantes S; Wolf JR; Department of
       Cellular and Structural Biology, University of; Colorado Medical School,
       Denver 80262.
 SO    J Biol Chem. 1995 Feb 17;270(7):3154-9. Unique Identifier : AIDSLINE
       MED/95155403
 AB    The surface glycoproteins of enveloped viruses bind to target cell
       receptors and trigger membrane fusion for infection. The human
       immunodeficiency virus 1 (HIV-1) envelope glycoprotein gp120 (CD4
       binding protein) and gp41 (transmembrane fusion protein) are initially
       synthesized as a gp160 precursor. The intracellular cleavage of gp160 by
       a host cell protease during transit through the secretory pathway is
       essential for viral activities such as infectivity, membrane fusion, and
       T-cell syncytium formation. We report that gp160 biogenesis, protein
       processing, and cell-surface expression have been successfully
       reproduced in the yeast Saccharomyces cerevisiae. Genetic and
       biochemical approaches are used for defining that the unique cellular
       protease, Kex2p, is directly responsible for HIV-gp160 processing in
       yeast, in vivo and in vitro. The yeast system described in this report
       represents a powerful strategy for identifying, characterizing and
       inhibiting the host T-cell protease essential for HIV infectivity and
       AIDS.
 DE    Cell Membrane/METABOLISM  Cloning, Molecular  Gene Expression  Gene
       Products, env/*BIOSYNTHESIS/ISOLATION & PURIF  HIV-1/*METABOLISM
       Plasmids  Polymerase Chain Reaction  Protein
       Precursors/*BIOSYNTHESIS/ISOLATION & PURIF  *Protein Processing,
       Post-Translational  Recombinant Proteins/BIOSYNTHESIS/ISOLATION & PURIF
       Saccharomyces cerevisiae/*ENZYMOLOGY  Subtilisins/*METABOLISM  Support,
       Non-U.S. Gov't  Support, U.S. Gov't, P.H.S.  Viral Envelope
       Proteins/BIOSYNTHESIS/ISOLATION & PURIF/METABOLISM  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).