Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Pseudomonas aeruginosa alkaline protease blocks complement activation via the classical and lectin pathways.
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AprA degrades human C1s and C2; the mechanism of complement inhibition is cleavage of C2, blocking C3b deposition via the classical and lectin pathways while sparing the alternative pathway.
"of action for complement inhibition is cleavage of C2. In summary, we showed"
Activation of the epithelial sodium channel (ENaC) by the alkaline protease from Pseudomonas aeruginosa.
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Purified AprA proteolytically activates ENaC (mapped to the gamma-subunit), increasing basal sodium current in primary human bronchial epithelia from CF and non-CF patients.
"ENaC in polarized monolayers indicated that AP activated ENaC in immortalized"
Pseudomonas evades immune recognition of flagellin in both mammals and plants.
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AprA degrades free monomeric flagellin (the TLR5/FLS2 ligand) but not polymeric flagellar flagellin or the receptors, allowing the bacterium to evade pattern-recognition-receptor detection while retaining motility.
"monomeric flagellin, while polymeric flagellin (involved in bacterial motility)"
Deep research report (falcon/Edison) for APRA
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AprA is a calcium-activated, zinc-dependent serralysin (M10B) secreted by the AprDEF type I secretion system, with an immune-biased substrate range (complement C2/C1q/C1s/C3/C5a, cytokines IFN-gamma/TNF-alpha, monomeric flagellin, ENaC, fibrin); aprA deletion attenuates virulence in a murine infection model.