Document Detail


Streptococcus pyogenes Ser/Thr kinase-regulated cell wall hydrolase is a cell division plane-recognizing and chain-forming virulence factor.
MedLine Citation:
PMID:  20643653     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cell division and cell wall synthesis are closely linked complex phenomena and play a crucial role in the maintenance and regulation of bacterial virulence. Eukaryotic-type Ser/Thr kinases reported in prokaryotes, including that in group A Streptococcus (GAS) (Streptococcus pyogenes Ser/Thr kinase (SP-STK)), regulate cell division, growth, and virulence. The mechanism of this regulation is, however, unknown. In this study, we demonstrated that SP-STK-controlled cell division is mediated under the positive regulation of secretory protein that possesses a cysteine and histidine-dependent aminohydrolases/peptidases (CHAP) domain with functionally active cell wall hydrolase activity (henceforth named as CdhA (CHAP-domain-containing and chain-forming cell wall hydrolase). Deletion of the CdhA-encoding gene resulted in severe cell division and growth defects in GAS mutants. The mutant expressing the truncated CdhA (devoid of the CHAP domain), although displayed no such defects, it became attenuated for virulence in mice and highly susceptible to cell wall-acting antibiotics, as observed for the mutant lacking CdhA. When CdhA was overexpressed in the wild-type GAS as well as in heterologous strains, Escherichia coli and Staphylococcus aureus, we observed a distinct increase in bacterial chain length. Our data reveal that CdhA is a multifunctional protein with a major function of the N-terminal region as a cell division plane-recognizing domain and that of the C-terminal CHAP domain as a virulence-regulating domain. CdhA is thus an important therapeutic target.
Authors:
Vijay Pancholi; Gregory Boël; Hong Jin
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-07-19
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  285     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-09-27     Completed Date:  2010-10-26     Revised Date:  2012-04-27    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  30861-74     Citation Subset:  IM    
Affiliation:
Department of Pathology, Ohio State University College of Medicine, Columbus, Ohio 43210-1214, USA. vijay.pancholi@osumc.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Bacterial Proteins / genetics,  metabolism*
Cell Wall / enzymology*,  metabolism
Escherichia coli / genetics
Gene Deletion
Humans
Hydrolases / genetics,  metabolism*
Mice
Mice, Inbred BALB C
Protein-Serine-Threonine Kinases / genetics,  metabolism*
Staphylococcus aureus / genetics
Streptococcal Infections / genetics,  metabolism*,  therapy
Streptococcus pyogenes / enzymology*,  genetics,  pathogenicity*
Virulence Factors / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
AI64912/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Virulence Factors; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 3.-/Hydrolases
Comments/Corrections

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