Immunogenicity and Protective Immunity Induced by Synthetic Peptides Associated with Putative Immunodominant Regions of<i>Streptococcus mutans</i>Glucan-Binding Protein B

Smith, Daniel J.; King, William F.; Barnes, L. A.; Peacock, Zachary S.; Taubman, Martin A.

doi:10.1128/iai.71.3.1179-1184.2003

Cited by 51 publications

(71 citation statements)

References 30 publications

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“…The production and activity of S. mutans Gtfs and their association with virulence has been studied extensively in laboratory strains (16,18,23,26). Mutants of gtfB, gtfC, or gtfD from strain UA130 showed a significantly lower potential to induce caries on smooth tooth surfaces in animal models when compared to the wild type, suggesting that all Gtf isozymes are important for colonization and caries induction (26).…”

Section: Discussionmentioning

confidence: 99%

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Comparative Analysis of Gtf Isozyme Production and Diversity in Isolates of Streptococcus mutans with Different Biofilm Growth Phenotypes

et al. 2004

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Streptococcus mutans is the main pathogenic agent of dental caries. Glucosyltransferases (Gtfs) produced by these bacteria are important virulence factors because they catalyze the extracellular synthesis of glucans that are necessary for bacterial accumulation in the dental biofilm. The diversity of GtfB and GtfC isozymes was analyzed in 44 genotypes of S. mutans that showed a range of abilities to form biofilms in vitro. Several approaches were used to characterize these isozymes, including restriction fragment length polymorphism analysis of the gtfB and gtfC genes, zymographic analysis of the identified GtfB and GtfC genotypes, and quantitation of isozyme production in immunoblot experiments with specific monoclonal antibodies. A high diversity of gtf genes, patterns of enzymatic activity, and isozyme production was identified among the isolates tested. GtfC and, to a lesser extent, GtfB were produced in significantly higher amounts by strains that had high biofilm-forming ability than by strains with low biofilm-forming ability. Biofilm formation was independent of the GtfB and GtfC genotype. Atypical strains that showed an apparent single Gtf isozyme of intermediate size between GtfB and GtfC were also identified. The results indicate that various expression levels of GtfB and GtfC isozymes are associated with the ability of distinct S. mutans genotypes to grow as biofilms, strengthening the results of previous genetic and biochemical studies performed with laboratory strains. These studies also emphasize the need to identify factors that control gtf gene expression.

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Section: Discussionmentioning

confidence: 99%

“…Three distinct Gtfs (GtfB, GtfC, and GtfD) were demonstrated to participate in the sucrose-dependent adherence process (16,23,26). Antibodies raised against Gtfs have been shown to protect against dental caries in animal models (18,21). Gtfs have also been incorporated into vaccines used in human clinical trials (3,19,20).…”

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confidence: 99%

Comparative Analysis of Gtf Isozyme Production and Diversity in Isolates of Streptococcus mutans with Different Biofilm Growth Phenotypes

et al. 2004

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“…Phenotypic characteristics of this mutant were found to mimic growth-and cell division-defective S. agalactiae (group B Streptococcus) and S. pneumoniae mutants lacking PcsB protein (15,36), S. mutans lacking GbpB protein (19,37), and E. faecalis/faecium lacking SagA/SalA (22,21). PcsB, GbpB, and Saga/SalA are orthologs and are reported to possess similar structural characteristics, including the CHAP domain at their C-terminal ends (24,38,39).…”

Section: Sp-stk Positively Regulatesmentioning

confidence: 99%

“…CdhA Regulates GAS Growth-Based on the structural similarity of CdhA with six other Gram-positive orthologs (15,19,21,22,36,37), we predicted that the N-terminal coiled-coil portion may have a role in cell division/separation/aggregation, and the C-terminal region containing CHAP domain may have a cell wall hydrolysis/synthesis function. CdhA possesses a typical motif of the CHAP-domain at its C-terminal end (SSX 7 CX 13 GX 30 GX 10 GX 5 YGH*VXVV, where X represents a non-conserved amino acid and H* is a putative catalytic histidine residue) (24,38,39).…”

Section: Sp-stk Positively Regulatesmentioning

confidence: 99%

Streptococcus pyogenes Ser/Thr Kinase-regulated Cell Wall Hydrolase Is a Cell Division Plane-recognizing and Chain-forming Virulence Factor

Pancholi

Boël²,

Jin

2010

Journal of Biological Chemistry

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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.

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“…P [332][333][334][335] GTF and Antigen I/II As above Significant reduction in colonization following oral challenge of mice.…”

Section: Group B Streptococcal Vaccine Developmentmentioning

confidence: 99%

Human pathogenic streptococcal proteomics and vaccine development

Cole

Henningham

Gillen

et al. 2008

Proteomics Clinical Apps

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Gram-positive streptococci are non-motile, chain-forming bacteria commonly found in the normal oral and bowel flora of warm-blooded animals. Over the past decade, a proteomic approach combining 2-DE and MS has been used to systematically map the cellular, surface-associated and secreted proteins of human pathogenic streptococcal species. The public availability of complete streptococcal genomic sequences and the amalgamation of proteomic, genomic and bioinformatic technologies have recently facilitated the identification of novel streptococcal vaccine candidate antigens and therapeutic agents. The objective of this review is to examine the constituents of the streptococcal cell wall and secreted proteome, the mechanisms of transport of surface and secreted proteins, and describe the current methodologies employed for the identification of novel surface-displayed proteins and potential vaccine antigens.

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Immunogenicity and Protective Immunity Induced by Synthetic Peptides Associated with Putative Immunodominant Regions ofStreptococcus mutansGlucan-Binding Protein B

Cited by 51 publications

References 30 publications

Comparative Analysis of Gtf Isozyme Production and Diversity in Isolates of Streptococcus mutans with Different Biofilm Growth Phenotypes

Comparative Analysis of Gtf Isozyme Production and Diversity in Isolates of Streptococcus mutans with Different Biofilm Growth Phenotypes

Streptococcus pyogenes Ser/Thr Kinase-regulated Cell Wall Hydrolase Is a Cell Division Plane-recognizing and Chain-forming Virulence Factor

Human pathogenic streptococcal proteomics and vaccine development

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