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Literature summary for 3.4.22.28 extracted from

  • Croft, S.N.; Walker, E.J.; Ghildyal, R.
    Human rhinovirus 3C protease cleaves RIPK1, concurrent with caspase 8 activation (2018), Sci. Rep., 8, 1569 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.28

Activating Compound

Activating Compound Comment Organism Structure
additional information the accessibility of the HRV 3C cleavage site within RIPK1 in-vitro is probably increased by concurrent cleavage of RIPK1 through caspase-8 rhinovirus A16

Protein Variants

Protein Variants Comment Organism
additional information subconfluent layers of A549 cells are transfected with GFP-tagged active 3C protease (GFP-3C) or an inactive mutant of 3C (GFP-3Cinac). Cleavage of a known target of 3C, PABP, is used to confirm activity of the 3C protease. RIPK1 cleavage product is detected in the GFP-3C expressing sample, but not in the GFP-3Cinac or untransfected samples. GFP-3Cinac is expressed to higher levels than GFP-3C, but PABP is cleaved only in the GFP-3C transfected sample rhinovirus A16

Inhibitors

Inhibitors Comment Organism Structure
rupintrivir the activity of HRV16 3C protease is clearly inhibited by Rupintrivir treatment as viral polyprotein (P1) processing is downregulated rhinovirus A16

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
receptor-interacting protein kinase-1 + H2O rhinovirus A16 i.e. RIPK1 ?
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 ?

Organism

Organism UniProt Comment Textmining
rhinovirus A16 Q82122 HRV-16
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Source Tissue

Source Tissue Comment Organism Textmining
additional information HRV16 3C protease cleaves RIPK1 in human host lung alveolar cells rhinovirus A16
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the accessibility of the HRV 3C cleavage site within RIPK1 in-vitro is probably increased by concurrent cleavage of RIPK1 through caspase-8. Prior to cleavage of RIPK1 by caspase 8 does not abrogate 3C protease-mediated cleavage in vitro rhinovirus A16 ?
-
 ?
receptor-interacting protein kinase-1 + H2O i.e. RIPK1 rhinovirus A16 ?
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 ?
receptor-interacting protein kinase-1 + H2O i.e. RIPK1, HRV 3C protease cleaves RIPK1 to produce a 23 kDa cleavage product rhinovirus A16 ?
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 ?

Synonyms

Synonyms Comment Organism
HRV16 3C protease
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 rhinovirus A16
Human rhinovirus 3C protease
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 rhinovirus A16

General Information

General Information Comment Organism
physiological function 3C protease is responsible for the cleavage of P1 to derive virus capsid proteins (VP1-4). HRV16 3C protease cleaves a key intermediate in extrinsic apoptosis. Receptor-interacting protein kinase-1 (RIPK1), an extrinsic apoptosis adaptor protein, is cleaved by caspase 8 during chemical induction of apoptosis. RIPK1 is cleaved in HRV infection albeit at a different site. Caspase 8 activation, which is associated with extrinsic apoptosis, is concurrent with HRV 3C protease-mediated cleavage of RIPK1, and potentially increases the accessibility of the HRV 3C cleavage site within RIPK1 in-vitro. The caspase 8-mediated RIPK1 cleavage product has a proapoptotic function, and further cleavage of this pro-apoptotic cleavage product by HRV 3C may provide a mechanism by which HRV limits apoptosis. HRV16 infection alters ActoD induced cell death rhinovirus A16