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PMID: 11435081 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

An abundance of bacterial ADP-ribosyltransferases--implications for the origin of exotoxins and their human homologues.

Trends in microbiology ·Vol. 9 ·No. 7 ·2001-07-00 ·Pages 302-7; discussion 308

Pallen MJ, Lam AC, Loman NJ, McBride A

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.

MeSH Terms
ADP Ribose Transferases/metabolism Amino Acid Sequence Bacillus/chemistry Bacteria/enzymology Bacterial Toxins/chemistry,metabolism Exotoxins/chemistry,metabolism Gram-Positive Bacteria/enzymology,metabolism Molecular Sequence Data Mycoplasma pneumoniae/chemistry Pertussis Toxin Pseudomonas/chemistry Salmonella typhi/chemistry Sequence Homology, Amino Acid Virulence Factors, Bordetella/chemistry,metabolism
Chemicals
Bacterial Toxins Exotoxins Virulence Factors, Bordetella ADP Ribose Transferases Pertussis Toxin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pallen M J
Microbial Genomics and Pathogenesis Unit, Division of Immunity and Infection, The Medical School, University of Birmingham, B15 2TT, Birmingham, UK. [email protected]
Lam A C
Loman N J
McBride A
Article Info
Journal
Trends in microbiology
Abbr.
Trends Microbiol
ISSN
0966-842X
DOI
10.1016/s0966-842x(01)02074-1
Email
[email protected]
Published
2001-07-00
Pages
302-7; discussion 308
Language
English
Region
England
NLM ID
9310916
Subset
IM
External Links
PubMed source DOI: 10.1016/s0966-842x(01)02074-1 View journal details
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