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Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gpl60
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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“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”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Hallenberger et al. 1992
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Metadata
- 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
- Licence
- 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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