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Literature summary for 3.4.22.28 extracted from

  • Mukherjee, A.; Morosky, S.; Delorme-Axford, E.; Dybdahl-Sissoko, N.; Oberste, M.; Wang, T.; Coyne, C.
    The coxsackievirus B 3Cpro protease cleaves MAVS and TRIF to attenuate host type I interferon and apoptotic signaling (2011), PLoS Pathog., 7, e1001311.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.28

Protein Variants

Protein Variants Comment Organism
C147A inactive mutant does not induce the appearance of a MAVS cleavage product Coxsackievirus B3

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
mitochondrial antiviral signaling protein + H2O Coxsackievirus B3 3Cpro-mediated MAVS cleavage occurs within its proline-rich region, leads to its relocalization from the mitochondrial membrane, and ablates its downstream signaling ?
-
 ?
Toll/IL-1 receptor domain-containing adaptor inducing interferon-beta + H2O Coxsackievirus B3 3Cpro cleaves both the N- and C-terminal domains of TRIF and localizes with TRIF to signalosome complexes within the cytoplasm ?
-
 ?

Organism

Organism UniProt Comment Textmining
Coxsackievirus B3
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
mitochondrial antiviral signaling protein + H2O 3Cpro-mediated MAVS cleavage occurs within its proline-rich region, leads to its relocalization from the mitochondrial membrane, and ablates its downstream signaling Coxsackievirus B3 ?
-
 ?
Toll/IL-1 receptor domain-containing adaptor inducing interferon-beta + H2O 3Cpro cleaves both the N- and C-terminal domains of TRIF and localizes with TRIF to signalosome complexes within the cytoplasm Coxsackievirus B3 ?
-
 ?

Synonyms

Synonyms Comment Organism
3Cpro protease
-
 Coxsackievirus B3

General Information

General Information Comment Organism
physiological function infection of cells with coxsackievirus leads to the cleavage of the adaptor molecules MAVS and TRIF through 3Cpro, indicating that a single protease suppresses innate immune signaling through two pathways. 3Cpro cleaves specific residues within MAVS and TRIF that render these molecules deficient in type I IFN signaling and apoptotic signaling Coxsackievirus B3