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Bacterial toxin and effector glycosyltransferases
- Source :
- Biochimica et biophysica acta. 1800(2)
- Publication Year :
- 2009
-
Abstract
- Clostridial glucosylating cytotoxins, including Clostridium difficile toxins A and B, Clostridium novyi alpha-toxin, and Clostridium sordellii lethal toxin, are major virulence factors and causative agents of human diseases. These toxins mono-O-glucosylate (or mono-O-GlcNAcylate) a specific threonine residue of Rho/Ras-proteins, which is essential for the function of the molecular switches. Recently, a related group of glucosyltransferases from Legionella pneumophila has been identified. These Legionella glucosyltransferases modify the large GTPase elongation factor eEF1A at a serine residue by mono-O-glucosylation, thereby inhibiting protein synthesis of target cells. Recent results on structures, functions and biological roles of both groups of bacterial toxin glucosyltransferases will be discussed.
- Subjects :
- Protein Conformation
Virulence Factors
Bacterial Toxins
Molecular Sequence Data
Biophysics
Virulence
Clostridium difficile toxin A
Biochemistry
Legionella pneumophila
Microbiology
Substrate Specificity
Glucosyltransferases
Peptide Elongation Factor 1
Humans
Amino Acid Sequence
Molecular Biology
biology
Effector
Glycosyltransferases
Clostridium difficile
biology.organism_classification
Clostridium novyi
Protein Structure, Tertiary
Elongation factor
ras Proteins
Sequence Alignment
Transcription Factors
Subjects
Details
- ISSN :
- 00063002
- Volume :
- 1800
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Biochimica et biophysica acta
- Accession number :
- edsair.doi.dedup.....b87564d833cc98691bed8f0b4f307619