The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-I SU) and gp41 (HIV-I TM)

Etienne Decroly, Michel Vandenbranden, Jean Marie Ruysschaert, Jacqueline Cogniaux, Gary S. Jacob, Susan C. Howard, Garland Marshall, Ashok Kompelli, Ajoy Basak, François Jean, Claude Lazure, Suzanne Benjannet, Michel Chrétien, Robert Day, Nabil G. Seidah

Research output: Contribution to journalArticlepeer-review

118 Scopus citations

Abstract

Intracellular proteolytic processing of human immunodeficiency virus envelope glycoprotein precursor (gp160) is an essential step for virus infectivity. Northern blot analysis provided evidence that furin and PC1, but not PC2, are expressed in the CD4+ human lymphoblastoid H9 cell line, suggesting the possible participation of these convertases in human immunodeficiency virus (HIV) gp160 proteolytic processing. Purified PC1 and furin cleaved specifically in vitro gp160 into gp120 (HIV-I SU) and gp41 (HIV-I TM). NH2-terminal sequence analysis of the produced gp41 (HIV-I TM) demonstrated that the cleavage occurred within the sequence Arg-Glu-Lys-Arg ↓ Ala-Val-Gly-Ile, which is identical to the bond cleaved in vivo. Transition state analog peptides were designed and tested in vitro for their ability to inhibit the PC1- or furin-mediated gp160 cleavage. The best inhibitor was decanoyl-Arg-Lys-Arg-Arg-Ψ[CH2NH]-Phe-Leu-Gly-Phe-NH2.

Original languageEnglish
Pages (from-to)12240-12247
Number of pages8
JournalJournal of Biological Chemistry
Volume269
Issue number16
StatePublished - Apr 22 1994

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