title: An abundance of bacterial ADP-ribosyltransferases--implications for the origin of exotoxins and their human homologues.
abstract: ADP-ribosylation is a post-translational modification that can be seen in many contexts, including as the primary mechanism of action of many important bacterial exotoxins. By data-mining complete and incomplete bacterial genome sequences, we have discovered >20 novel putative ADP-ribosyltransferases, including several new potential toxins.
authors: Microbial Genomics and Pathogenesis Unit, Division of Immunity and Infection, The Medical School, University of Birmingham, B15 2TT, Birmingham, UK. m.j.pallen@bham.ac.uk
authors: M J
authors: MJ
authors: Pallen
authors: A C
authors: AC
authors: Lam
authors: N J
authors: NJ
authors: Loman
authors: A
authors: A
authors: McBride
mesh_terms: D036002:ADP Ribose Transferases / Q000378:metabolism*; D000595:Amino Acid Sequence; D001407:Bacillus / Q000737:chemistry; D001419:Bacteria / Q000201:enzymology*; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism; D005098:Exotoxins / Q000737:chemistry* / Q000378:metabolism; D006094:Gram-Positive Bacteria / Q000201:enzymology / Q000378:metabolism; D008969:Molecular Sequence Data; D009177:Mycoplasma pneumoniae / Q000737:chemistry; D037342:Pertussis Toxin; D011549:Pseudomonas / Q000737:chemistry; D012485:Salmonella typhi / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D010566:Virulence Factors, Bordetella / Q000737:chemistry / Q000378:metabolism
chemical_list: D001427:Bacterial Toxins; D005098:Exotoxins; D010566:Virulence Factors, Bordetella; D036002:ADP Ribose Transferases; D037342:Pertussis Toxin