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

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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

DOI 10.1038/360358a0

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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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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
Publisher: Springer Science and Business Media LLC
Published: 1992-11-26
Volume: 360
Issue: 6402
Pages: 358-361
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/360358a0
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
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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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Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gpl60

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