Accession | VIRO:0000316 |
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 addition of a glucose molecule to a protein residue in order to inactivate the target protein. Conventional acceptor amino acids that act as glycosyl-acceptors includes serine, threonine and asparagine. Unconventional glycosyl-acceptor amino acids includes tyrosine, tryptophan and arginine. Generally results in the inhibition of actin polymerization within the host cells. |
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 inactivator toxins [Virulence Factor] |
Publications | Jank T, et al. 2013. Nat. Struct. Mol. Biol. 20(11):1273-80 A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins. (PMID 24141704) Just I, et al. 1995. Nature 375(6531):500-3 Glucosylation of Rho proteins by Clostridium difficile toxin B. (PMID 7777059) |
Curator | Description | Most Recent Edit |
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