Document Detail

SpyA is a membrane-bound ADP-ribosyltransferase of Streptococcus pyogenes which modifies a streptococcal peptide, SpyB.
MedLine Citation:
PMID:  22288436     Owner:  NLM     Status:  MEDLINE    
All sequenced genomes of Streptococcus pyogenes (Group A Streptococcus, GAS) encode a protein, SpyA, with homology to C3-like ADP-ribosyltransferase toxins. SpyA is a novel virulence factor which plays a role in pathogenesis in a mouse model of soft-tissue infection. In this study we demonstrate that SpyA is a surface-exposed membrane protein which is anchored to the streptococcal membrane by an N-terminal transmembrane sequence. We identified a small gene upstream of spyA, designated spyB, which encodes a peptide of 35 amino acids, and is co-transcribed with spyA. Expression of spyBA is strongly influenced by translational coupling: mutational inactivation of spyB translation completely abolishes translation of spyA. spyB expression increases with increasing cell density and reaches its maximum at late exponential growth phase. The SpyB N-terminus is predicted to fold into an amphipathic α-helix, a structural motif that targets a protein to the cytoplasmic membrane. Consistent with the prediction, we found that a SpyB fusion with peptide affinity tags is located in the streptococcal membrane. An ADP-ribosylation assay with recombinant SpyA demonstrated that SpyA modifies SpyB. Thus, our study suggests that ADP-ribosylation of SpyB may be an important function of SpyA.
Natalia Korotkova; Jessica S Hoff; Devon M Becker; John Kyle Heggen Quinn; Laura M Icenogle; Steve L Moseley
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-01-30
Journal Detail:
Title:  Molecular microbiology     Volume:  83     ISSN:  1365-2958     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-02-23     Completed Date:  2012-07-16     Revised Date:  2014-09-10    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  936-52     Citation Subset:  IM    
Copyright Information:
© 2012 Blackwell Publishing Ltd.
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MeSH Terms
ADP Ribose Transferases / genetics,  metabolism*
Bacterial Proteins / genetics,  metabolism*
DNA, Bacterial / genetics
Gene Expression Regulation, Bacterial
Membrane Proteins / genetics,  metabolism
Mutagenesis, Site-Directed
Protein Structure, Secondary
Streptococcus pyogenes / enzymology,  genetics*
Virulence Factors / genetics,  metabolism
Grant Support
2P20 RR020171/RR/NCRR NIH HHS; A1064515//PHS HHS; P20 RR020171/RR/NCRR NIH HHS; P20 RR020171-03/RR/NCRR NIH HHS; R01 AI064515/AI/NIAID NIH HHS; R01 AI064515-05/AI/NIAID NIH HHS
Reg. No./Substance:
0/Bacterial Proteins; 0/DNA, Bacterial; 0/Membrane Proteins; 0/Virulence Factors; EC 2.4.2.-/ADP Ribose Transferases

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

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