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Literature summary for 3.4.22.28 extracted from

  • Walker, E.; Jensen, L.; Croft, S.; Wei, K.; Fulcher, A.J.; Jans, D.A.; Ghildyal, R.
    Rhinovirus 16 2A protease affects nuclear localization of 3CD during infection (2016), J. Virol., 90, 11032-11042 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant GFP-tagged or mCherry-tagged enzymes in Escherichia coli and in COS-7 cells rhinovirus A16

Protein Variants

Protein Variants Comment Organism
K22A/K24A PCR-based site-directed mutagenesis is performed to mutate the lysine residues in the putative NLS in 3Dpol to generate GFP-3CDucNLSm. Uncleavable 3CD is unable to target GFP to the nucleus rhinovirus A16
additional information an additional form of 3CD that cannot be cleaved due to inactivation of the 3Cpro is generated (GFP-3CinacD). The mutant is mutated to the putative NLS in 3Dpol to generate GFP-3CinacD-NLSm. Uncleavable 3CD is unable to target GFP to the nucleus rhinovirus A16
Q183A/G184A site-directed mutagenesis of the cleavage site, the P1 and P1' residues are mutated to alanine rhinovirus A16

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information early in infection, 3Cpro is present as its precursor 3CD, which is found in the nucleus as well as the cytoplasm. Enzyme 2Apro activity (EC 3.4.22.29) is required for 3CD nuclear localization. Nuclear localization of 3CD correlates with 2Apro activity and not 3Cpro activity, which is observed only later in infection. 3Cpro is located in the cytoplasm and the nucleus, whereas 3CD and 3D are localized predominantly in the cytoplasm, implying that 3D lacks nuclear targeting ability and that 3Cpro activity within 3CD is not sufficient to allow the larger protein into the nucleus. The activity of both 2Apro and 3Cpro is required for 3CD entry into the nucleus rhinovirus A16
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Organism

Organism UniProt Comment Textmining
rhinovirus A16
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HRV-A16
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification 3Cpro precursor 3CD rhinovirus A16

Source Tissue

Source Tissue Comment Organism Textmining
additional information the virus is propagated in Ohio-HeLa cells and COS-7 cells rhinovirus A16
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Synonyms

Synonyms Comment Organism
3C protease
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rhinovirus A16
3Cpro
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rhinovirus A16
HRV 3C protease
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rhinovirus A16

General Information

General Information Comment Organism
physiological function the human rhinovirus (HRV) 3C and 2A proteases (3Cpro and 2Apro, respectively) are critical in HRV infection, as they are required for viral polyprotein processing as well as proteolysing key host factors to facilitate virus replication. Temporal activities of 2Apro and 3CD/3Cpro activities in HRV serotype16 infection rhinovirus A16