Document Detail


Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins.
MedLine Citation:
PMID:  18785839     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Bacterial pathogens utilize toxins to modify or kill host cells. The bacterial ADP-ribosyltransferases are a family of protein toxins that covalently transfer the ADP-ribose portion of NAD to host proteins. Each bacterial ADP-ribosyltransferase toxin modifies a specific host protein(s) that yields a unique pathology. These toxins possess the capacity to enter a host cell or to use a bacterial Type III apparatus for delivery into the host cell. Advances in our understanding of bacterial toxin action parallel the development of biophysical and structural biology as well as our understanding of the mammalian cell. Bacterial toxins have been utilized as vaccines, as tools to dissect host cell physiology, and more recently for the development of novel therapies to treat human disease.
Authors:
Qing Deng; Joseph T Barbieri
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review    
Journal Detail:
Title:  Annual review of microbiology     Volume:  62     ISSN:  0066-4227     ISO Abbreviation:  Annu. Rev. Microbiol.     Publication Date:  2008  
Date Detail:
Created Date:  2008-09-12     Completed Date:  2008-12-04     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372370     Medline TA:  Annu Rev Microbiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  271-88     Citation Subset:  IM    
Affiliation:
Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA. dengqing@mcw.edu
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MeSH Terms
Descriptor/Qualifier:
ADP Ribose Transferases / chemistry,  metabolism,  toxicity
Adenosine Diphosphate Ribose / metabolism*
Animals
Bacterial Toxins / chemistry,  metabolism*,  toxicity*
Cytotoxins / chemistry,  metabolism,  toxicity
Diphtheria Toxin / chemistry,  metabolism,  toxicity
Exotoxins / chemistry,  metabolism,  toxicity
GTPase-Activating Proteins / chemistry,  metabolism,  toxicity
Humans
Leukocidins / chemistry,  metabolism,  toxicity
Models, Biological
Models, Molecular
Peptide Elongation Factor 2 / metabolism
Virulence Factors / chemistry,  metabolism,  toxicity
Grant Support
ID/Acronym/Agency:
AI-30162/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Toxins; 0/Cytotoxins; 0/Diphtheria Toxin; 0/ExoT protein, Pseudomonas aeruginosa; 0/Exotoxins; 0/GTPase-Activating Proteins; 0/Leukocidins; 0/Peptide Elongation Factor 2; 0/Pseudomonas aeruginosa Cytotoxins; 0/Virulence Factors; 20762-30-5/Adenosine Diphosphate Ribose; EC 2.4.2.-/ADP Ribose Transferases; EC 2.4.2.31/exoenzyme S; EC 2.4.2.31/toxA protein, Pseudomonas aeruginosa

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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