The family of bacterial ADP-ribosylating exotoxins. Clin Microbiol Rev 1995 Jan;8(1):34-47
Date
01/01/1995Pubmed ID
7704894Pubmed Central ID
PMC172848DOI
10.1128/CMR.8.1.34Scopus ID
2-s2.0-0028981421 (requires institutional sign-in at Scopus site) 137 CitationsAbstract
Pathogenic bacteria utilize a variety of virulence factors that contribute to the clinical manifestation of their pathogenesis. Bacterial ADP-ribosylating exotoxins (bAREs) represent one family of virulence factors that exert their toxic effects by transferring the ADP-ribose moiety of NAD onto specific eucaryotic target proteins. The observations that some bAREs ADP-ribosylate eucaryotic proteins that regulate signal transduction, like the heterotrimeric GTP-binding proteins and the low-molecular-weight GTP-binding proteins, has extended interest in bAREs beyond the bacteriology laboratory. Molecular studies have shown that bAREs possess little primary amino acid homology and have diverse quaternary structure-function organization. Underlying this apparent diversity, biochemical and crystallographic studies have shown that several bAREs have conserved active-site structures and possess a conserved glutamic acid within their active sites.
Author List
Krueger KM, Barbieri JTAuthor
Joseph T. Barbieri PhD Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Adenosine Diphosphate RiboseAmino Acid Sequence
Bacterial Toxins
Molecular Sequence Data
Pertussis Toxin
Virulence Factors, Bordetella