Cited by 586HIV Research and TreatmentProtease and Inhibitor MechanismsHIV/AIDS drug development and treatment

Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gpl60

Hallenberger, Sabine, Bosch, Valerie, Angliker, Herbert, Shaw, Elliott, Klenk, Hans-Dieter, Garten, Wolfgang·1992·Nature

Abstract

The envelope glycoprotein of human immunodeficiency virus (HIV) initiates infection by mediating fusion of the viral envelope with the cell membrane. Fusion activity requires proteolytic cleavage of the gp160 protein into gp120 and gp41 at a site containing several arginine and lysine residues. Activation at basic cleavage sites is observed with many membrane proteins of cellular and viral origin. We have recently found that the enzyme activating the haemagglutinin of fowl plague virus (FPV), an avian influenza virus, is furin. Furin, a subtilisin-like eukaryotic endoprotease, has a substrate specificity for the consensus amino-acid sequence Arg-X-Lys/Arg-Arg at the cleavage site. We show here that the glycoprotein of HIV-1, which has the same protease recognition motif as the FPV haemagglutinin, is also activated by furin.

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Crossref · 10.1038/360358a0

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  • In HIV-1, the Env glycoproteins precursor, gp160, is cleaved in the Golgi by cellular furin or furin-like PRs into a mature surface glycoprotein gp120 and the transmembrane glycoprotein gp41.

    “In case of HIV-1, the Env glycoproteins precursor, gp160, is cleaved in the Golgi by cellular furin or furin-like PRs into: (i) a mature surface glycoprotein gp120 and (ii) the transmembrane glycoprotein gp41”

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Authors
Hallenberger, S., Bosch, V., Angliker, H., Shaw, E., Klenk, H.-D., & Garten, W.
Affiliations
  • Philipps University of Marburg (DE)
  • German Cancer Research Center (DE)
  • Friedrich Miescher Institute (CH)
Venue
Nature
Published
1992-11-26
Volume
360
Issue
6402
Pages
358-361
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
OpenAlex
W2001675486
Cited by
582
References
23
Citations by year
2026: 5 · 2025: 5 · 2024: 14 · 2023: 18 · 2022: 13 · 2021: 24 · 2020: 23 · 2019: 14 · 2018: 20 · 2017: 9 · 2016: 14 · 2015: 23 · 2014: 24 · 2013: 17 · 2012: 27
FWCI
10.83
Type
journal article
Language
en
Open access
closed
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Keywords
furin, HIV-1 envelope glycoprotein, gp160, proteolytic cleavage, furin inhibitors, viral fusion, infectious virus particles, endopeptidase
MeSH terms
Amino Acid Chloromethyl Ketones, Amino Acid Sequence, HeLa Cells, Humans, Molecular Sequence Data, Protein Precursors, Substrate Specificity, Subtilisins, Virus Replication, CD4-Positive T-Lymphocytes, HIV-1, Gene Products, env, Gene Expression, Consensus Sequence, HIV Envelope Protein gp160, Furin

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