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Literature summary for 3.4.21.72 extracted from

  • Besbes, A.; Le Goff, S.; Antunes, A.; Terrade, A.; Hong, E.; Giorgini, D.; Taha, M.K.; Deghmane, A.E.
    Hyperinvasive meningococci induce intra-nuclear cleavage of the NF-kappaB protein p65/RelA by meningococcal IgA protease (2015), PLoS Pathog., 11, e1005078 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.72

Cloned(Commentary)

Cloned (Comment) Organism
gene igaA, recombinant expression of C-terminally His6-tagged passenger domain of the strains LNP19995 (IgaP-19995) or LNP21019 (IgaP-21019) Neisseria meningitidis serogroup C

Protein Variants

Protein Variants Comment Organism
additional information generation of an isogenic iga knockout mutant strain, analysis of infection efficiency and persistence in infected cells Neisseria meningitidis serogroup C

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Neisseria meningitidis serogroup C
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additional information the secreted 150 kDa meningococcal ST-11 IgA protease is carrying nuclear localisation signals (NLS) in its alpha-peptide moiety that allow efficient intranuclear transport in the host cell Neisseria meningitidis serogroup C
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Neisseria meningitidis serogroup C cleavage of p65/RelA occurs at the C-terminal region which contains the transactivation domain (TAD). Removal of the TAD from the rest of the protein may therefore disable the activation capacity of the native p65/RelA molecule ?
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 ?
NF-kappaB p65/RelA component + H2O Neisseria meningitidis serogroup C specific cleavage at the C-terminal region of NF-kappaB p65/RelA component within the nucleus of infected cells ?
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 ?

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis serogroup C
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme performs autocatalysis at its autocleavage site. Proteolytic cleavage of IgA protease may occur at two cleavage sites in ST-11 isolates LNP19995: CS1 autocleavage site (separating the protease domain from the alpha peptide) and CS2 autocleavage site (separating the alpha peptide from the translocator domain). The proteolytic cleavage may occur at the unique CS1 site, leading to release of alpha-peptide-lacking IgA protease in non-ST-11 isolates Neisseria meningitidis serogroup C

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cleavage of p65/RelA occurs at the C-terminal region which contains the transactivation domain (TAD). Removal of the TAD from the rest of the protein may therefore disable the activation capacity of the native p65/RelA molecule Neisseria meningitidis serogroup C ?
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 ?
additional information the enzyme performs autocatalysis at its autocleavage site Neisseria meningitidis serogroup C ?
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 ?
NF-kappaB p65/RelA component + H2O specific cleavage at the C-terminal region of NF-kappaB p65/RelA component within the nucleus of infected cells Neisseria meningitidis serogroup C ?
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 ?
NF-kappaB p65/RelA component + H2O specific cleavage at the C-terminal region of NF-kappaB p65/RelA component Neisseria meningitidis serogroup C ?
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 ?

Synonyms

Synonyms Comment Organism
IgA protease
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 Neisseria meningitidis serogroup C
ST-11 IgA protease
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 Neisseria meningitidis serogroup C

General Information

General Information Comment Organism
additional information the secreted 150 kDa meningococcal ST-11 IgA protease is carrying nuclear localisation signals (NLS) in its alpha-peptide moiety that allow efficient intranuclear transport in the host Hec-1-B cells Neisseria meningitidis serogroup C
physiological function while non-invasive isolates of Neisseria meningitidis (e.g. non-ST-11 isolate LNP19995) provoke a sustained NF-kappaB activation in epithelial cells, hyperinvasive isolates only induce an early NF-kappaB activation followed by a sustained activation of JNK and apoptosis. Elucidation of the mechanism conferring this differential modulation, specifically showing that ST-11 hyperinvasive isolates promote specific cleavage of NF-kappaB p65/RelA component in a secreted IgA protease-dependent manner. This cleavage occurs within the nuclear compartment. Secreted IgA protease from non-invasive isolates is unable to reach the nuclear compartment of infected cells, resulting in a sustained activation of NF-kappaB activity and subsequent cytoprotective effect. Modulation of NF-kappaB-related signaling is likely a double-edged sword to decide the fate of meningococcal infection. Both ST-11 and non-ST-11 isolates cause IkappaBalpha degradation. Meningococcal ST-11 isolates promote nuclear cleavage of p65 at late steps of infection through secreted IgA protease, overview. ST-11 IgA protease-mediated nuclear cleavage of p65/RelA alters selectively expression of NF-kappaB responsive genes in Hec-1-B cells Neisseria meningitidis serogroup C