NTR: symbiont-mediated suppression of host complement activation by recruitment of host proteases

[pgaudet]

NTR: symbiont-mediated suppression of host complement activation by recruitment of host proteases

For GO-PathGO alignment

@genegodbold to provide references

[pgaudet]

+[Term] +id: GO:0141203 +name: symbiont-mediated suppression of host complement activation by recruitment of host proteases +namespace: biological_process +def: "A process by which a symbiont prevents host complement activation by recruiting host proteases, destroying the complement before it has its effect on the symbiont." [GOC:pg] +is_a: GO:0042784 ! symbiont-mediated suppression of host complement activation +property_value: term_tracker_item "https://github.com/geneontology/go-ontology/issues/27788" xsd:anyURI +created_by: pg +creation_date: 2024-04-30T13:17:35Z

[pgaudet]

PR is here: https://github.com/geneontology/go-ontology/pull/27789

[genegodbold]

Hey @pgaudet I'd like to make a correction to the title: instead of "recruitment", can this be changed to "activation"? See staphylokinase

• Staphylokinase from Staphylococcus aureus: Staphylokinase is secreted by S_aureus and it activates human plasminogen into plasmin. SAK is anti-opsonic, inhibiting S_aureus from being phagocytosed by host neutrophils in vitro. S_aureus has several plasminogen-binding receptors at the cell surface which bind host plasminogen. Surface bound plasminogen can be activated into the active plasmin protease by SAK on the surface of the bacterium. This allows the surface-bound plasmin to cleave both immunoglobulin G (IgG) and the complement proteins C3b and C3bi, thus inhibiting bacterial destruction by complement. Thus SAK activation of bacteria-bound host plasminogen to plasmin on the bacterial surface protects the bacterium from host defenses [PMID:15792635].
• M protein from Streptococcus: Fibrils of M protein form a dense, covalently attached coat on the streptococcal surface blocking the deposition of antibodies and complement [PMID:18323455]. Human factor H is recruited to the streptococcal surface by PAM along with human plasminogen/ plasmin. These contribute to the degradation of the opsonin human C3b to its inactive product (iC3b), protecting the bacterium from phagocytosis. Factor H and factor I cleave C3b while plasmin cuts iC3b into smaller peptides [PMID:26945067].
• Endopeptidase O (PepO; Neprilysin) from Streptococcus suis: Host plasminogen bound to SsPepO can be converted to plasmin via proteolysis by host uPA and can then degrade host complement C3b and enabling the control of complement activation. A bacterial mutant lacking PepO has impaired adherence to plasminogen, invasion of rat brain microvessel endothelial cells, and is efficiently killed by human serum and blood [PMID:34305859].

[pgaudet]

• [ ] updated term label
• [ ] added references