Document Detail

Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes.
MedLine Citation:
PMID:  15458407     Owner:  NLM     Status:  MEDLINE    
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.
Lisette H Coye; Carleen M Collins
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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    
Department of Microbiology and Immunology, University of Miami School of Medicine, Miami, FL 33136, USA.
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MeSH Terms
ADP Ribose Transferases / chemistry,  genetics,  metabolism*
Amino Acid Sequence
CHO Cells
Cytoskeletal Proteins / metabolism
Hela Cells
Molecular Sequence Data
Recombinant Proteins / genetics,  metabolism
Streptococcus pyogenes / chemistry,  enzymology*,  pathogenicity*
Grant Support
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

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