Accession | VIRO:0000319 |
Definition | Mechanism 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. |
Classification | 9 ontology terms | Show + process or component of pathogenesis biology or chemistry + biological effect of virulence + virulence factor + host cell damaging + toxin [Virulence Factor] + exotoxin + molecular mechanism of bacterial virulence + Actin-affecting toxins [Virulence Mechanism] + ADP-Ribosylation [Virulence Mechanism] |
Parent Term(s) | 2 ontology terms | Show + molecular mechanism of bacterial virulence + participates_in Rho-protein activator toxins [Virulence Factor] |
Sub-Term(s) | 2 ontology terms | Show |
Publications | 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) |
Curator | Description | Most Recent Edit |
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