Characteristics of a protease of Streptococcus sanguis G9B which degrades the major salivary adhesin

Lamont, Richard J.

doi:10.1016/0378-1097(89)90350-9

Cited by 4 publications

(4 citation statements)

References 19 publications

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“…The specimens were finally examined in an electron microscope (Philips CM 12) at an accelerating voltage of 80 kV Extraction of S. sanguis OMZ 9 ceii surface proteins Bacteria were harvested from a 2-liter batch culture in FUM, by centrifuging at 10,000 x^^ for 10 min at 4"C. They were washed three times with distilled water (48,000 xg, 15 min, 4 C) and subjected to the barbital extraction procedure described by Lamont et al (30) with the following modifications. The pellet was suspended in 550 ml of cold 2 mM sodium 5,5-diethylbarbiturate buffer (pH 8.6) supplemented with 1 mM iodoacetic acid, to inhibit endogenous protease activities (28). After shaking for 30 min at 4°C, the suspension was centrifuged (48,000 x^, 15 min, 4"C), and the supernatant collected.…”

Section: Binding Of Colioidal Goid-labeiied Cgp To Oral Bacteriamentioning

confidence: 99%

In vitro modulation of oral bacterial adhesion to saliva‐coated hydroxyapatite beads by milk casein derivatives

Neeser

Golliard

Woltz

et al. 1994

Oral Microbiology and Immunology

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Bovine caseinate, derivatives of its glycosylated moiety [caseinoglycomacropeptide (CGP)], and caseinophosphopeptides were evaluated as inhibitors of adhesion of oral bacteria to saliva-coated hydroxyapatite beads (S-HA). All milk casein-derived components behaved as potent inhibitors of Streptococcus sanguis OMZ 9 and Streptococcus sobrinus OMZ 176 adhesion to S-HA, whereas neither bovine serum albumin nor polyethyleneglycol were able to interfere with the adhesion of these strains. By contrast, none of the molecular species tested was able to inhibit the attachment of Actinomyces viscosus Ny 1 to S-HA. On the other hand, casein derivatives were shown to displace human serum albumin from S-HA beads. They were also able to bind to the bacterial cell surface of all strains examined. Collectively, these findings suggest that interactions between acidic casein-derived milk components and the biological surfaces involved in bacterial adhesion to S-HA result in an inhibitory effect that is selective for the oral streptococci examined.

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Section: Binding Of Colioidal Goid-labeiied Cgp To Oral Bacteriamentioning

confidence: 99%

In vitro modulation of oral bacterial adhesion to saliva‐coated hydroxyapatite beads by milk casein derivatives

Neeser

Golliard

Woltz

et al. 1994

Oral Microbiology and Immunology

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“…Their metabolic activities will modify the newly colonized habitat and influence subsequent events during ecologic succession. Previous investigators have demonstrated that protease activity from S. sanguis can modify human salivary molecules (12). Immunofluorescence studies demonstrate that the 146-kDa protease is detectable on the bacterial cell surface and may therefore modify salivary molecules on the tooth surface.…”

Section: Discussionmentioning

confidence: 98%

“…Although studies describe and characterize specific immunoglobulin A (IgA) proteases from these early colonizers (1,16), less is known regarding specific molecules mediating the general proteolytic activities elaborated by these organisms. S. oralis and related streptococci are known to produce protease and peptidase activities (2,4,12,18,19). These investigations have focused on the physiological role of these activities, in particular, their probable role in meeting the amino nitrogenous demands of the organism's metabohsm.…”

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confidence: 99%

Identification and characterization of a protease from Streptococcus oralis C104

Hughes¹

1996

Oral Microbiology and Immunology

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Streptococcus oralis is among the earliest colonizers of the tooth surface during plaque formation. As such, its enzymatic activities may influence ecologic succession on the tooth surface. In the current study, we use zymograms and preparative polyacrylamide gel electrophoresis to identify and purify a protease from S. oralis (sanguis) C104. Proteases from S. oralis C104 were detected in cell pellets at 133, 146 and 176 kDa as clear proteolytic bands on gelatin-substrate zymograms. Preparation of the major (146 kDa) protease were obtained by continuous-elution electrophoresis. The protease was active over the pH range of 7 to 9 with optimum activity between pH 8 and 9. Protease activity was inhibited by several serine protease inhibitors including phenylmethylsulfonyl fluoride, di-isopropyl-phosphofluoridate and aprotinin. The protease showed highest hydrolytic activity against azoalbumin and Bz-Pro-Phe-Arg-NA. Immunofluorescence studies with a polyclonal antiserum to the 146-kDa protease suggest it is present on the cell surface of S. oralis C104. Zymograms of cell pellets from other S. oralis strains as well as S. sanguis and Streptococcus mitis suggest that functionally similar proteases are elaborated by many early colonizers of the tooth surface.

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“…A more plausible explanation is that the lower molecular mass molecules were generated by proteolytic activity. Oral streptococci produce a number of proteases that can be released from the cells and may degrade surface proteins (Cowman & Baron, 1991 ;Floders et al, 1987 ;Lamont & Rosan, 1989;Rodgers e t al., 1990). The importance of proteolytic activity in the co-adherence of P. gingivalis and S. gordonii was demonstrated by Stinson et al (1992) Ray & Payne, 1988).…”

Section: Discussionmentioning

confidence: 99%

Molecules of Streptococcus gordonii that bind to Porphyromonas gingivalis

et al. 1994

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lnterbacterial binding is considered an important colonization mechanism for many of the organisms that inhabit dental plaque. Porphyromonas gingivalis, a periodontal pathogen, can adhere to species that comprise early plaque, such as Streptococcus gordonii. In this study, the molecules of S. godonii G9B that mediate binding to P. gingivalis were investigated. Biotinylated surface molecules of 5. gordonii were extracted and mixed with P. gingivalis cells. Interactive streptococcal components were identified by SDS-PAGE of the P. gingivalis cells followed by electroblotting, and visualization of the adsorbed streptococcal molecules with streptavidin-alkaline phosphatase. 5. gordonii molecules of 45 kDa and a doublet of 62/60 kDa were observed to bind to P. gingivalis. Polyclonal antibodies raised to the 62/60 kDa proteins inhibited the binding interaction. These antibodies demonstrated an antigenic relationship between the 62/60 kDa molecules and the 45 kDa protein. Both molecules were also antigenically related to, and may be breakdown products of, a larger molecule of 170 kDa which is antigenically related to the P I antigen of S. mutans. Cloning and expression in Enterococcus faecalis of the gene for the P Ilike molecule from S. gordonii M5 resulted in a phenotype that expressed the 62/60 kDa and 45 kDa antigens and was capable of binding to P. gingivalis.These results suggest that a P1-like molecule in 5. gordonii is involved in adherence to P. gingivalis. Processing of the PI-like molecule into smaller fragments of 62/60 kDa and 45 kDa may be required for binding activity.

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Characteristics of a protease of Streptococcus sanguis G9B which degrades the major salivary adhesin

Cited by 4 publications

References 19 publications

In vitro modulation of oral bacterial adhesion to saliva‐coated hydroxyapatite beads by milk casein derivatives

In vitro modulation of oral bacterial adhesion to saliva‐coated hydroxyapatite beads by milk casein derivatives

Identification and characterization of a protease from Streptococcus oralis C104

Molecules of Streptococcus gordonii that bind to Porphyromonas gingivalis

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