Document Detail


Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes.
MedLine Citation:
PMID:  15458407     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Streptococcus pyogenes, the aetiological agent of both respiratory and skin infections, produces numerous exotoxins to establish infection. This report identifies a new exotoxin produced by this organism, termed SpyA, for S. pyogenesADP-ribosylating toxin. SpyA, MW 24.9, has amino acid identity with the ADP-riboslytransferases (ADPRTs) Staphylococcus aureus EDIN and Clostridium botulinum C3. Recombinant SpyA was able to hydrolyse beta-NAD(+), and this activity was dependent on a glutamate at position 187. SpyA has a putative biglutamate active site, and similar to most biglutamate ADPRTs, was able to ADP-ribosylate poly-l-arginine. SpyA modified numerous proteins in both CHO and HeLa cell lysates. Two-dimesional gel analysis and MALDI-TOF MS analysis of modified proteins indicated that vimentin, tropomyosin and actin, all cytoskeletal proteins, are targets. Expression of spyA in HeLa cells resulted in loss of actin microfilaments. We hypothesize that SpyA is produced by S. pyogenes to disrupt cytoskeletal structures and promote colonization of the host.
Authors:
Lisette H Coye; Carleen M Collins
Related Documents :
19939847 - Brooding fathers, not siblings, take up nutrients from embryos.
9136117 - Influence of ovine oviducal amino acid concentrations and an ovine oestrus-associated g...
15675147 - Comparison of the chemical composition and nutritional value of amaranthus cruentus flo...
23107717 - Taurine-nitrite interaction as a precursor of alkylation mechanisms.
7646007 - Characterization of a new lipopeptide surfactant produced by thermotolerant and halotol...
6408947 - Determination of dipicolinic acid in bacterial spores by derivative spectroscopy.
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular microbiology     Volume:  54     ISSN:  0950-382X     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2004 Oct 
Date Detail:
Created Date:  2004-10-01     Completed Date:  2004-12-10     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  89-98     Citation Subset:  IM    
Affiliation:
Department of Microbiology and Immunology, University of Miami School of Medicine, Miami, FL 33136, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
ADP Ribose Transferases / chemistry,  genetics,  metabolism*
Amino Acid Sequence
Animals
CHO Cells
Cricetinae
Cytoskeletal Proteins / metabolism
Hela Cells
Humans
Molecular Sequence Data
Recombinant Proteins / genetics,  metabolism
Streptococcus pyogenes / chemistry,  enzymology*,  pathogenicity*
Grant Support
ID/Acronym/Agency:
AI42353/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Cytoskeletal Proteins; 0/Recombinant Proteins; EC 2.4.2.-/ADP Ribose Transferases

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


Previous Document:  HmsP, a putative phosphodiesterase, and HmsT, a putative diguanylate cyclase, control Hms-dependent ...
Next Document:  Positioning of the MinE binding site on the MinD surface suggests a plausible mechanism for activati...