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Literature summary for 3.4.22.28 extracted from

  • Xie, L.; Lu, B.; Zheng, Z.; Miao, Y.; Liu, Y.; Zhang, Y.; Zheng, C.; Ke, X.; Hu, Q.; Wang, H.
    The 3C protease of enterovirus A71 counteracts the activity of host zinc-finger antiviral protein (ZAP) (2018), J. Gen. Virol., 99, 73-85 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of FLAG-tagged enzyme in HEK-293T cells Enterovirus A71

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by benzyloxycarbonyl-VAD-(O-methyl)-fluoromethylketone Enterovirus A71

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
host zinc-finger antiviral protein + H2O Enterovirus A71 cleavage specifically at Gln369, ZAP cleavage is dependent on its amino acid pair Q369 and G370 ?
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Organism

Organism UniProt Comment Textmining
Enterovirus A71
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EV-A71
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Source Tissue

Source Tissue Comment Organism Textmining
additional information ZAP is passaged in HeLa and RD cells Enterovirus A71
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
host zinc-finger antiviral protein + H2O cleavage specifically at Gln369, ZAP cleavage is dependent on its amino acid pair Q369 and G370 Enterovirus A71 ?
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?
additional information no activity with Q369A ZAP mutant Enterovirus A71 ?
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?

Synonyms

Synonyms Comment Organism
3C protease
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Enterovirus A71
3Cpro
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Enterovirus A71

General Information

General Information Comment Organism
metabolism the 3C protease of enterovirus A71 counteracts the activity of host zinc-finger antiviral protein (ZAP or PARP13/ZC3HAV1). EV-A71 infection upregulates ZAP mRNA in RD and HeLa cells. Moreover, ZAP overexpression renders 293T cells resistant to EV-A71 infection, whereas siRNA-mediated depletion of endogenous ZAP enhances EV-A71 infection. The EV-A71 infection stimulates site-specific proteolysis of two ZAP isoforms, leading to the accumulation of a 40 kDa N-terminal ZAP fragment in virus-infected cells. The 3C protease (3Cpro) of EV-A71 mediates ZAP cleavage, which requires protease activity. Furthermore, ZAP variants with single amino acid substitutions at Gln369 are resistant to 3Cpro cleavage, implying that Gln369 is the sole cleavage site in ZAP. Although ZAP overexpression inhibits EV-A71 replication, the cleaved ZAP fragments do not show this effect. An equilibrium between ZAP and enterovirus 3Cpro controls viral infection Enterovirus A71
physiological function the 3C protease (3Cpro) of EV-A71 mediates ZAP cleavage, which requires protease activity. The viral 3Cpro mediated ZAP cleavage may represent a mechanism to escape host antiviral responses Enterovirus A71