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 | 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 | 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 | 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 | 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 | 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 |