Deamidation [Virulence Mechanism]

Accession VIRO:0000319
DefinitionMechanism for intracellularly active bacterial toxins that target rho proteins in order to ultimately affect actin polymerization within host cells as a toxic effect. Involves the removal of the amide functional group from asparaginyl (Asn) and glutaminyl (Gln) residues to produce aspartyl (Asp) and glutamyl (Glu) residues within rho peptides. Generally results in a constitutively active rho protein which enhances actin polymerization.
Classification9 ontology terms | Show
Parent Term(s)2 ontology terms | Show
2 ontology terms | Show
+ CNFy participates_in
+ dermonecrotic toxin participates_in

Flatau G, et al. 1997. Nature 387(6634):729-33 Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine. (PMID 9192901)

Robinson NE, et al. 2001. Proc. Natl. Acad. Sci. U.S.A. 98(22):12409-13 Deamidation of human proteins. (PMID 11606750)

Schmidt G, et al. 1997. Nature 387(6634):725-9 Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. (PMID 9192900)