Furin is important but not essential for the proteolytic maturation of gp160 of HIV-1

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....

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Bibliographic Details
Published in:FEBS letters 1995-05, Vol.365 (1), p.95-97
Main Authors: Gu, MiLi, Rappapor, Jay, Leppla, Stephen H.
Format: Article
Language:English
Subjects:
AIDS/HIV
Amino Acid Sequence
Animals
CHO Cells
Cricetinae
Furin
Furin-deficient CHO
Gene Products, env - metabolism
HIV Core Protein p24 - analysis
HIV envelope
HIV Envelope Protein gp160
HIV-1 - metabolism
Humans
Mice
Molecular Sequence Data
Polymerase Chain Reaction
Protein Precursors - metabolism
Protein Processing, Post-Translational
Recombinant Proteins - metabolism
Subtilisins - genetics
Subtilisins - metabolism
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00447-H