geneontology / go-ontology

Source ontology files for the Gene Ontology
http://geneontology.org/page/download-ontology
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NTR: symbiont-mediated disruption of host membrane #27132

Closed pgaudet closed 6 months ago

pgaudet commented 6 months ago

For GO-PathGO alignment

+[Term] +id: GO:0141171 +name: symbiont-mediated disruption of host membrane +namespace: biological_process +def: "The process in which a symbiont effects a change that impairs the structure or function of a host membrane. The host is defined as the larger of the organisms involved in a symbiotic interaction." [GOC:pg] +is_a: GO:0052008 ! symbiont-mediated disruption of host cellular anatomical entity +created_by: pg +creation_date: 2024-02-22T16:03:28Z +

@genegodbold to provide references

genegodbold commented 6 months ago

Cereolysin B (CerB; Phosphatidylcholine cholinephosphohydrolase; PC-PLC) from Bacillus cereus: Cereolysin AB is a membrane-disrupting complex that hydrolyzes sphingomyelin in intact red blood cells causing erythrocyte hemolysis. This results from membrane modification, not pore formation. CerA has phospholipase C (PLC) activity while CerB is a sphingomyelinase (sphingomyelin phosphodiesterase) [PMID:23748204]. Sphingomyelinase (Sph; SMase): The Sph secreted sphingomyelinase of Bacillus cereus contributes to cytotoxicity in vitro and pathogenicity in a wax moth infection larvae model. Sph complements the cytotoxicity of nonhemolytic enterotoxin for an intestinal epithelial cell line [PMID:23613846]. Vacuolating autotransporter toxin (Vat): Vat from avian pathogenic _Escherichia col_i (APEC) induces intracellular vacuole formation in chicken embryo fibroblasts (CEFs) similar to that seen with VacA cytotoxin from H. pylori. Infection of chickens with mutant APEC in which the encoding vat gene was deleted showed a much lower incidence of lesions, cellulitis, septicemia, and death [PMID:12933851]. Vat is a class II SPATE [PMID:23689588]. Clostridiolysin S from Clostridium botulinum: Clostridiolysin S requires a number of accessory enzymes (ClosB; ClosC; ClosE; ClosF; ClosG; ClosH, ClosI) to modify it to a functional cytolytic state [PMID:20581111].