Document 0519
 DOCN  M9590519
 TI    Furin is important but not essential for the proteolytic maturation of
       gp160 of HIV-1.
 DT    9509
 AU    Gu M; Rappaport J; Leppla SH; Laboratory of Microbial Ecology, National
       Institute of Dental; Research, National Institutes of Health, Bethesda,
       MD 20892, USA.
 SO    FEBS Lett. 1995 May 22;365(1):95-7. Unique Identifier : AIDSLINE
       MED/95293134
 AB    The envelope glycoproteins of HIV are required for viral infectivity.
       Proteolysis of the precursor envelope glycoprotein gp160 results in the
       formation of gp120 and gp41. Cleavage occurs after the sequence
       Arg-Glu-Lys-Arg. This sequence is expected to be a substrate for the
       cellular protease furin. We examined whether furin is responsible for
       cleavage of gp160 by using a furin-deficient CHO cell line and the same
       cell line transfected with furin cDNA. Data obtained from viral
       transmission assays suggested that furin increased viral infectivity but
       was not essential for the maturation of gp160, implying that other
       proprotein processing enzymes also recognize this putative furin
       cleavage site.
 DE    Amino Acid Sequence  Animal  CHO Cells  Gene Products, env/*METABOLISM
       Hamsters  Human  HIV Core Protein p24/ANALYSIS  HIV-1/*METABOLISM  Mice
       Molecular Sequence Data  Polymerase Chain Reaction  Protein
       Precursors/*METABOLISM  *Protein Processing, Post-Translational
       Recombinant Proteins/METABOLISM  Subtilisins/GENETICS/*METABOLISM
       Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
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