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Literature summary for 3.4.22.29 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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
eukaryotic translation initiation factor 4G + H2O Coxsackievirus B3 eIF4G ?
-
?
eukaryotic translation initiation factor 4G + H2O Enterovirus A71 eIF4G ?
-
?
eukaryotic translation initiation factor 4G + H2O Enterovirus D68 eIF4G ?
-
?
eukaryotic translation initiation factor 4G + H2O Coxsackievirus A21 eIF4G ?
-
?
MAVS + H2O Coxsackievirus B3 a cellular protein ?
-
?
MAVS + H2O Enterovirus A71 a cellular protein ?
-
?
MAVS + H2O Enterovirus D68 a cellular protein ?
-
?
MAVS + H2O Coxsackievirus A21 a cellular protein ?
-
?
MDA5 + H2O Coxsackievirus B3 a cellular protein ?
-
?
MDA5 + H2O Enterovirus A71 a cellular protein ?
-
?
MDA5 + H2O Enterovirus D68 a cellular protein ?
-
?
MDA5 + H2O Coxsackievirus A21 a cellular protein ?
-
?

Organism

Organism UniProt Comment Textmining
Coxsackievirus A21
-
CV-A21
-
Coxsackievirus B3
-
CV-B3
-
Enterovirus A71
-
EV-A71
-
Enterovirus D68
-
EV-D68
-
no activity in Encephalomyocarditis virus
-
EMCV, the 2A protein of the cardiovirus is not a protease
-

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.
eukaryotic translation initiation factor 4G + H2O eIF4G Coxsackievirus B3 ?
-
?
eukaryotic translation initiation factor 4G + H2O eIF4G Enterovirus A71 ?
-
?
eukaryotic translation initiation factor 4G + H2O eIF4G Enterovirus D68 ?
-
?
eukaryotic translation initiation factor 4G + H2O eIF4G Coxsackievirus A21 ?
-
?
MAVS + H2O a cellular protein Coxsackievirus B3 ?
-
?
MAVS + H2O a cellular protein Enterovirus A71 ?
-
?
MAVS + H2O a cellular protein Enterovirus D68 ?
-
?
MAVS + H2O a cellular protein Coxsackievirus A21 ?
-
?
MDA5 + H2O a cellular protein Coxsackievirus B3 ?
-
?
MDA5 + H2O a cellular protein Enterovirus A71 ?
-
?
MDA5 + H2O a cellular protein Enterovirus D68 ?
-
?
MDA5 + H2O a cellular protein Coxsackievirus A21 ?
-
?

Synonyms

Synonyms Comment Organism
2A protease
-
Coxsackievirus B3
2A protease
-
Enterovirus A71
2A protease
-
Enterovirus D68
2A protease
-
Coxsackievirus A21
2Apro
-
Coxsackievirus B3
2Apro
-
Enterovirus A71
2Apro
-
Enterovirus D68
2Apro
-
Coxsackievirus A21
enterovirus 2A protease
-
Coxsackievirus B3
enterovirus 2A protease
-
Enterovirus A71
enterovirus 2A protease
-
Enterovirus D68
enterovirus 2A protease
-
Coxsackievirus A21

General Information

General Information Comment Organism
physiological function enterovirus 2Apro plays a key role in inhibiting innate antiviral cellular responses. The direct cleavage of eIF4G by 2Apro contributes to the suppression of stress granule (SG) formation. Cleavage of eIF4G impairs the recruitment of 40S ribosomes to mRNAs, thereby altering the composition of mRNPs, which, in turn, may affect their recruitment to SGs. The observation that 2Apro triggers SG formation by cleavage of eIF4G. 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 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells. 2Apro is a major enteroviral security protein Enterovirus A71
physiological function enterovirus 2Apro plays a key role in inhibiting innate antiviral cellular responses. The direct cleavage of eIF4G by 2Apro contributes to the suppression of stress granule (SG) formation. Cleavage of eIF4G impairs the recruitment of 40S ribosomes to mRNAs, thereby altering the composition of mRNPs, which, in turn, may affect their recruitment to SGs. The observation that 2Apro triggers SG formation by cleavage of eIF4G. 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 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells. 2Apro is a major enteroviral security protein Enterovirus D68
physiological function enterovirus 2Apro plays a key role in inhibiting innate antiviral cellular responses. The direct cleavage of eIF4G by 2Apro contributes to the suppression of stress granule (SG) formation. Cleavage of eIF4G impairs the recruitment of 40S ribosomes to mRNAs, thereby altering the composition of mRNPs, which, in turn, may affect their recruitment to SGs. The observation that 2Apro triggers SG formation by cleavage of eIF4G. 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 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells. 2Apro is a major enteroviral security protein Coxsackievirus A21
physiological function enterovirus 2Apro plays a key role in inhibiting innate antiviral cellular responses. The direct cleavage of eIF4G by 2Apro contributes to the suppression of stress granule (SG) formation. Cleavage of eIF4G impairs the recruitment of 40S ribosomes to mRNAs, thereby altering the composition of mRNPs, which, in turn, may affect their recruitment to SGs. The observation that 2Apro triggers SG formation by cleavage of eIF4G. 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). Enzyme 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. Enterovirus 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells. Heterologous expression of 2Apro during EMCV infection (EMCV-2Apro) nearly completely blocks IFN-beta gene transcription (about 500fold reduction) indicates that it is unlikely that suppression of SG formation by 2Apro is the major contributing factor in the viral suppression of IFN-beta gene transcription. 2Apro is a major enteroviral security protein Coxsackievirus B3