Cell surface proteins of oral streptococci

Appelbaum, B; Rosan, Burton

doi:10.1128/iai.46.1.245-250.1984

Cited by 18 publications

(10 citation statements)

References 41 publications

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“…S. gordonii produces more than 20 polypeptides that are exposed at the cell surface (2,21). There is evidence that at least several of these polypeptides are involved in streptococcal cell adherence processes.…”

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confidence: 99%

Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces

et al. 1993

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Chem. 265:7120-7126, 1990).The region of the gene encoding an N-terminal segment of a related polypeptide (SspA) in S. gordonii DL1 (Challis) was isolated following polymerase chain reaction amplification of genomic DNA. The sspA gene in S. gordonii DL1 was insertionally inactivated by homologous recombination of the erythromycin resistance (Emr) determinant ermAM onto the streptococcal chromosome. The SspA polypeptide (apparent molecular mass, 210 kDa) was detected on Western blots (immunoblots) of spheroplast extracts and extracellular culture medium proteins from wild-type strain DL1 but was absent from Emr mutants. One SspAmutant (designated OB220) was not altered in rate or extent of aggregation by whole saliva or parotid saliva but showed reduced aggregation in the presence of purified salivary agglutinin. Mutant bacteria were unaffected in their ability to adhere to hydroxylapatite beads coated with whole or parotid saliva and were unaltered in cell surface hydrophobicity. However, the SspAstrain OB220 was deficient in binding salivary agglutinin and in binding to six strains of Actinomyces naeslhdii. Therefore, expression of SspA polypeptide in S. gordonii is associated with both agglutinin-dependent and agglutinin-independent aggregation and adherence reactions of streptococcal cells.

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confidence: 99%

Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces

et al. 1993

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“…Evidence suggests that surface proteins (16,24,33,35), and proteinaceous structures such as fimbriae (6,8,9,12) and fibrils (14,29) may contribute to surface hydrophobicity and to adherence. However, surface labelling of S. sanguis cells reveals that at least 30 proteins are exposed at the cell surface (1,16). The question arises as to how many of these are involved in adhesion processes and, if amongst these, different classes of adhesin can be identified.…”

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confidence: 99%

Cell surface mutants of Streptococcus sanguis with altered adherence properties

Jenkinson

Carter

1988

Oral Microbiology and Immunology

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Two mutants of Streptococcus sanguis (Challis) with altered cell‐surface hydrophobicities were isolated after mutagenesis with ethyl methanesulphonate. Cells of one mutant were more hydrophobic than those of the parent strain and they adhered better to hexadecane, octyl‐Sepharose, hydroxylapatite, saliva‐treated hydaroxylapatite, and to Actinomyces viscosus. The second mutant had reduced hydrophobicity, and cells adhered less well to all the above surfaces except the actinomycetes, adsorption to which was similar to that of the wild‐type strain. The differences in hydrophobicity of the mutants were associated with alterations in amount and exposure of surface proteins, in particular two envelope proteins (Mr 43,000 and 45,000). The properties of the mutants support the contention that hydrophobic forces are determinants in S. sanguis adherence.

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“…The cell surface of many strains of S. satiguis have been shown to eonsist of a number of surface proteins, polysaccharides, and teichoic acids (4,26,31,41,43). The complexity of this sur-face has made it difficult to identify and isolate the speeific adhesins involved in the binding of this organism to salivat-y pellieles.…”

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confidence: 99%

“…Radioiodination. Streptoeoccal surface proteins wer-e radioiodinated by the lactoperoxidase method as previously reported (4,30). An Intertechnique (Dover, NJ) CG4000 gamma counter was used for counting the radioiodinated samples.…”

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confidence: 99%

Isolation and characterization of a non‐adherent mutant of Streptococcus sanguis G9B

Rosan

Eifert

Baker

et al. 1988

Oral Microbiology and Immunology

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A spontaneous non‐adherent mutant (Adh−) of Streptococcus sanguis, strain G9B has been isolated from a chemostat culture employing a chemically defined medium (FMC) as a nutritional source. The Adh− mutant showed five‐fold less adhesion to saliva‐coated hydroxyapatite (SHA) compared with parent G9B. No difference in adhesion to uncoated hydroxyapatite (HA) was found between G9B and Adh−. The mutant had the same colonial, cellular morphology, and biochemical properties as the parent. A comparison of the antigens found in mutanolysin (M‐1, N‐acetylmuramidase) extracts of G9B and Adh− using crossed rocket immunoelectrophoresis (CIE), indicated that a surface antigen, designated A, reacted strongly in G9B but only weakly in Adh−. The adhesion of G9B but not Adh− to SHA was directly correlated with dilution rates in a chemostat. Adhesion to HA was not affected by the dilution rate. There was also a direct correlation between the concentration of the A antigen with adhesion of G9B to SHA. The concentration of A in Adh− was low at all dilution rates. Antibody to G9B specifically inhibited adhesion of G9B to SHA but antibody to Adh− had no effect on adhesion of either strain to SHA. Neither antibody affected adhesion to HA. A partially purified A antigen absorbed adhesion inhibitory activity of G9B IgG. Trypsin did not digest the A antigen but resulted in the extraction of the antigen from the surface causing the loss of the cells ability to adhere to SHA. Galactose oxidase treated G9B cells also showed a reduced adhesion to SHA but glucose oxidase had no effect. Periodate oxidation of G9B resulted in a loss of adhesion to SHA. The A antigen was found in purified cell walls and was labelled with 125I, indicating a surface location. The A antigen also reacted with affinity purified antibody against the G9B adhesin antigen. Immunoblots of the A antigen following SDS‐PAGE indicated it contained 80, 62, and 52 kDa polypeptides. These results suggest that the A antigen is a glycoprotein which is the native form of the adhesin responsible for the attachment of G9B to salivary pellicle.

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Cell surface proteins of oral streptococci

Cited by 18 publications

References 41 publications

Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces

Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces

Cell surface mutants of Streptococcus sanguis with altered adherence properties

Isolation and characterization of a non‐adherent mutant of Streptococcus sanguis G9B

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