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Literature summary for 3.4.22.28 extracted from

  • Visser, L.J.; Langereis, M.A.; Rabouw, H.H.; Wahedi, M.; Muntjewerff, E.M.; de Groot, R.J.; van Kuppeveld, F.J.M.
    Essential role of enterovirus 2A protease in counteracting stress granule formation and the induction of type I Interferon (2019), J. Virol., 93, e00222-19 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Coxsackievirus A21
-
CV-A21
-
Coxsackievirus B3
-
CV-B3
-
Enterovirus A71
-
EV-A71
-
Enterovirus D68
-
EV-D68
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information the virus is propagated in HeLa R19 cells Coxsackievirus B3
-
additional information the virus is propagated in HeLa R19 cells Enterovirus A71
-
additional information the virus is propagated in HeLa R19 cells Enterovirus D68
-
additional information the virus is propagated in HeLa R19 cells Coxsackievirus A21
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with cellular protein MAVS Coxsackievirus B3 ?
-
?
additional information no activity with cellular protein MAVS Enterovirus A71 ?
-
?
additional information no activity with cellular protein MAVS Enterovirus D68 ?
-
?
additional information no activity with cellular protein MAVS Coxsackievirus A21 ?
-
?

Synonyms

Synonyms Comment Organism
3C protease
-
Coxsackievirus B3
3C protease
-
Enterovirus A71
3C protease
-
Enterovirus D68
3C protease
-
Coxsackievirus A21
3Cpro
-
Coxsackievirus B3
3Cpro
-
Enterovirus A71
3Cpro
-
Enterovirus D68
3Cpro
-
Coxsackievirus A21
enterovirus 3C protease
-
Coxsackievirus B3
enterovirus 3C protease
-
Enterovirus A71
enterovirus 3C protease
-
Enterovirus D68
enterovirus 3C protease
-
Coxsackievirus A21

General Information

General Information Comment Organism
metabolism during enterovirus infection, several signaling molecules in the RLR pathway have been suggested to be cleaved by 2Apro and 3Cpro (EC 3.4.22.28). 2Apro is the viral protease responsible for cleaving MAVS. Addition of recombinant 2Apro, but not 3Cpro, to cell lysates results in the appearance of MAVS cleavage products of the same size as those observed in infected cells. These cleavage products are also observed when 2Apro, but not 3Cpro, is expressed by a recombinant encephalomyocarditis virus (EMCV), a picornavirus that by itself does not cleave components of the RLR pathway. 3Cpro, when expressed by a recombinant EMCV, fails to cleave the cellular protein MAVS. Enterovirus enzyme 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells Coxsackievirus B3
physiological function enterovirus 3Cpro plays a key role in inhibiting innate antiviral cellular responses. During enterovirus infection, several signaling molecules in the RLR pathway have been suggested to be cleaved by 2Apro and 3Cpro (EC 3.4.22.28). Enterovirus enzyme 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells Enterovirus A71
physiological function enterovirus 3Cpro plays a key role in inhibiting innate antiviral cellular responses. During enterovirus infection, several signaling molecules in the RLR pathway have been suggested to be cleaved by 2Apro and 3Cpro (EC 3.4.22.28). Enterovirus enzyme 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells Enterovirus D68
physiological function enterovirus 3Cpro plays a key role in inhibiting innate antiviral cellular responses. During enterovirus infection, several signaling molecules in the RLR pathway have been suggested to be cleaved by 2Apro and 3Cpro (EC 3.4.22.28). Enterovirus enzyme 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells Coxsackievirus A21