Interactions between salivary agglutinins and strains of Streptococcus mutans with varying degrees of surface hydrophobicity

Rundegren, Jan

doi:10.1016/0378-1097(87)90364-8

Cited by 2 publications

(1 citation statement)

References 4 publications

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“…showed that the variant cells adhered less well to saliva-coated hydroxyapatite than did the parent cells. The variant strains were agglutinated to a lower extent by parotid saliva or salivary agglutinin than the parent cells (Rundegren & Olsson, 1987). Moreover, McBride et af.…”

Section: Reactivity Of Anti-pac Serum and Anti-pags-5 Serum With Whmentioning

confidence: 94%

Characterization of a Cell-surface Protein Antigen of Hydrophilic Streptococcus mutans Strain GS-5

Ohta

Kato²,

Okahashi³

et al. 1989

Microbiology

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Fourteen strains of Streptococcus mutans serotype c were examined for their cell-surface protein antigens in terms of hydrophobicity, M , and immunochemical specificities. Thirteen strains were hydrophobic, while strain GS-5 was markedly hydrophilic as compared to the other strains tested. Cell-surface protein antigens were then analysed by sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE) and Western immunoblotting. A protein antigen of M , 190000 (PAC) was found in cell extracts and culture supernatants of all the hydrophobic strains. Neither culture supernatant nor cell extract of strain GS-5 contained PAC. Strain GS-5, however, produced extracellularly a large amount of a protein of M , 155000 (PAGS-5) which reacted with rabbit anti-PAC serum. Immunodiffusion analysis showed that PAGS-5 lacked a part of the antigenic moieties in the PAC molecule. SDS-PAGE and radioimmunoassay showed a small amount of PAGS-5 on the cell surface of strain GS-5. These findings suggest that PAGS-5 may correspond to PAC which lacks a region participating in binding of PAC to the streptococcal cell. I N T R O D U C T I O NStreptococcus mutans has been strongly implicated as a causative organism of dental caries (Hamada & Slade, 1980; Loesche, 1986). The organism possesses various kinds of cell-surface polymers such as proteinaceous antigens, serotype-specific polysaccharide antigens, lipoteichoic acid and peptidoglycan (Hamada & Slade, 1980). Among these cell-surface polymers, much attention has been focused on a high-M, protein antigen that has been variously designated as antigen B (Russell, 1979), 1/11 (Russell et al., 1980), IF (Hughes et al., 1980) and PI (Forester et al., 1983). Streptococcus sobrinus also possesses a cell-surface protein antigen that is immunologically and biochemically similar to that of S. mutans (Moro & Russell, 1983; Holt et al., 1982; Okahashi et al., 1986).The high-M, protein antigen of S. mutans serotype c (PAC) is an effective vaccine antigen for prevention of dental caries in monkeys (Lehner et al., 1981 ; Russell et al., 1982). Local passive immunization with monoclonal antibodies raised against PAC prevents the colonization by S. mutans of animal and human tooth surfaces (Lehner et al., 1985; Ma et af., 1987). Polyclonal antibodies to PAC are strongly opsonic for S. mutans (Scully et al., 1980). McBride et al. (1984) suggested that location of PAC on the streptococcal surface is important in forming hydrophobic bonds with hydrophobic regions of salivary pellicle. The organization of PAC on the cell surface, however, is poorly understood.

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Section: Reactivity Of Anti-pac Serum and Anti-pags-5 Serum With Whmentioning

confidence: 94%

Characterization of a Cell-surface Protein Antigen of Hydrophilic Streptococcus mutans Strain GS-5

Ohta

Kato²,

Okahashi³

et al. 1989

Microbiology

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The binding of delmopinol and chlorhexidine to Streptococcus mutans and Actinobacillus actinomycetemcomitans strains with varying degrees of surface hydrophobicity

Freitas

Rundegren²,

Arnebrant

1993

Oral Microbiology and Immunology

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This study evaluated the binding of chlorhexidine and the new surface-active anti-plaque agent delmopinol hydrochloride to Streptococcus mutans and Actinobacillus actinomycetemcomitans cells with various cell surface hydrophobicities. The influence of saliva concentration on the binding of these compounds was also investigated. The radiolabeled compounds were incubated with bacteria and the cells were recovered using a centrifugal filtering technique. Delmopinol had higher binding to the hydrophilic variant strains than to the hydrophobic parent strains; chlorhexidine had higher binding to hydrophobic than to hydrophilic A. actinomycetemcomitans strains and higher binding to hydrophilic than to hydrophobic S. mutans strains. The presence of salivary films decreased the binding of both compounds. Both delmopinol and chlorhexidine had stronger affinity to A. actinomycetemcomitans cells than to S. mutans cells. At equimolar concentrations, delmopinol had a lower binding to all strains tested than chlorhexidine. The high reversibility of the delmopinol binding might be related to a higher diffusion rate and solubility compared with that of chlorhexidine. The amphiphilicity of both molecules is an important feature in their retention to S. mutans and A. actinomycetemcomitans strains of varying hydrophobicities and could play an important role in the substantivity of delmopinol or chlorhexidine in the oral cavity.

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Interactions between salivary agglutinins and strains of Streptococcus mutans with varying degrees of surface hydrophobicity

Cited by 2 publications

References 4 publications

Characterization of a Cell-surface Protein Antigen of Hydrophilic Streptococcus mutans Strain GS-5

Characterization of a Cell-surface Protein Antigen of Hydrophilic Streptococcus mutans Strain GS-5

The binding of delmopinol and chlorhexidine to Streptococcus mutans and Actinobacillus actinomycetemcomitans strains with varying degrees of surface hydrophobicity

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