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RIPK1 Is Cleaved by 3C Protease of Rhinovirus A and B Strains and Minor and Major Groups.
- Source :
-
Viruses [Viruses] 2021 Nov 30; Vol. 13 (12). Date of Electronic Publication: 2021 Nov 30. - Publication Year :
- 2021
-
Abstract
- Rhinoviruses (RV), like many other viruses, modulate programmed cell death to their own advantage. The viral protease, 3C has an integral role in the modulation, and we have shown that RVA-16 3C protease cleaves Receptor-interacting protein kinase-1 (RIPK1), a key host factor that modulates various cell death and cell survival pathways. In the current study, we have investigated whether this cleavage is conserved across selected RV strains. RIPK1 was cleaved in cells infected with strains representing diversity across phylogenetic groups (A and B) and receptor usage (major and minor groups). The cleavage was abrogated in the presence of the specific 3C protease inhibitor, Rupintrivir. Interestingly, there appears to be involvement of another protease (maybe 2A protease) in RIPK1 cleavage in strains belonging to genotype B. Our data show that 3C protease from diverse RV strains cleaves RIPK1, highlighting the importance of the cleavage to the RV lifecycle.
- Subjects :
- 3C Viral Proteases genetics
Antiviral Agents chemistry
Antiviral Agents pharmacology
Apoptosis drug effects
HeLa Cells
Host-Pathogen Interactions
Humans
Isoxazoles chemistry
Isoxazoles pharmacology
Phenylalanine analogs & derivatives
Phenylalanine chemistry
Phenylalanine pharmacology
Picornaviridae Infections genetics
Picornaviridae Infections virology
Protease Inhibitors chemistry
Protease Inhibitors pharmacology
Pyrrolidinones chemistry
Pyrrolidinones pharmacology
Rhinovirus chemistry
Rhinovirus drug effects
Rhinovirus genetics
Valine analogs & derivatives
Valine chemistry
Valine pharmacology
3C Viral Proteases metabolism
Picornaviridae Infections enzymology
Rhinovirus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1999-4915
- Volume :
- 13
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Viruses
- Publication Type :
- Academic Journal
- Accession number :
- 34960671
- Full Text :
- https://doi.org/10.3390/v13122402