Salivary Amylase Promotes Adhesion of Oral Streptococci to Hydroxyapatite
Recent studies have demonstrated that several species of oral streptococci, such as Streptococcus gordonii, bind soluble salivary a-amylase. The goal of the present study was to determine if amylase immobilized onto a surface such as hydroxyapatite can serve as an adhesion receptor for S. gordonii....
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| Veröffentlicht in: | Journal of dental research 1995-07, Vol.74 (7), p.1360-1366 |
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| container_title | Journal of dental research |
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| creator | Scannapieco, F.A. Torres, G.I. Levine, M.J. |
| description | Recent studies have demonstrated that several species of oral streptococci, such as Streptococcus gordonii, bind soluble salivary a-amylase. The goal of the present study was to determine if amylase immobilized onto a surface such as hydroxyapatite can serve as an adhesion receptor for S. gordonii. Initially, human parotid saliva was fractionated on Bio-Gel P60, and fractions were screened for their ability to promote adhesion of S. gordonii to hydroxyapatite. Fractions containing a-amylase and proline-rich proteins promoted the adhesion of [3H]-labeled S. gordonii to hydroxyapatite. Similar findings were obtained with purified amylase and acidic proline-rich protein 1 (PRP1). Incubation of S. gordonii G9B in the presence of starch and maltotriose increased the binding of this strain to amylase-coated hydroxyapatite, while the adhesion of S. sanguis 10556 to amylase-coated hydroxyapatite was not affected by these saccharides. These results suggest that amylase may serve as a hydroxyapatite pellicle receptor for amylase-binding streptococci. Furthermore, starch and starch metabolites may enhance the adhesion of amylase-binding streptococci to amylase in dental pellicles to augment the formation of dental plaque. |
| doi_str_mv | 10.1177/00220345950740070701 |
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The goal of the present study was to determine if amylase immobilized onto a surface such as hydroxyapatite can serve as an adhesion receptor for S. gordonii. Initially, human parotid saliva was fractionated on Bio-Gel P60, and fractions were screened for their ability to promote adhesion of S. gordonii to hydroxyapatite. Fractions containing a-amylase and proline-rich proteins promoted the adhesion of [3H]-labeled S. gordonii to hydroxyapatite. Similar findings were obtained with purified amylase and acidic proline-rich protein 1 (PRP1). Incubation of S. gordonii G9B in the presence of starch and maltotriose increased the binding of this strain to amylase-coated hydroxyapatite, while the adhesion of S. sanguis 10556 to amylase-coated hydroxyapatite was not affected by these saccharides. These results suggest that amylase may serve as a hydroxyapatite pellicle receptor for amylase-binding streptococci. Furthermore, starch and starch metabolites may enhance the adhesion of amylase-binding streptococci to amylase in dental pellicles to augment the formation of dental plaque.</description><subject>Adhesins, Bacterial - drug effects</subject><subject>Adhesins, Bacterial - metabolism</subject><subject>Adult</subject><subject>Amylases - analysis</subject><subject>Amylases - isolation & purification</subject><subject>Amylases - metabolism</subject><subject>Amylases - pharmacology</subject><subject>Analysis of Variance</subject><subject>Bacterial Adhesion - drug effects</subject><subject>Dental Pellicle</subject><subject>Dentistry</subject><subject>Durapatite - metabolism</subject><subject>Enzymes, Immobilized - analysis</subject><subject>Enzymes, Immobilized - isolation & purification</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Enzymes, Immobilized - pharmacology</subject><subject>Humans</subject><subject>Male</subject><subject>Mouth - microbiology</subject><subject>Protein Binding - drug effects</subject><subject>Receptors, Immunologic - drug effects</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Saliva - chemistry</subject><subject>Saliva - enzymology</subject><subject>Streptococcus - metabolism</subject><subject>Streptococcus - pathogenicity</subject><subject>Streptococcus sanguis - metabolism</subject><subject>Streptococcus sanguis - pathogenicity</subject><issn>0022-0345</issn><issn>1544-0591</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEFLAzEQhYMotVb_gcKevK1ONslm91iK2oJQoXpe0uxEt-w2NcmK--9NafEkMoc5zPce8x4h1xTuKJXyHiDLgHFRCpAcQMahJ2RMBecpiJKekvEeSffMObnwfgNAy6xgIzKSIgdW5GOyWKm2-VJuSKbd0CqPyYuznQ3ok2n9gb6x28SaZOlUm6yCw12w2mrdJMEm86F29ntQOxWagJfkzKjW49VxT8jb48PrbJ4-L58Ws-lzqjkrQ5pLWaAuMiqYQV0Dz-LbhkmjTCYoFlBkksu1yZADzankjJW5KnOOsNZQMjYhtwffnbOfPfpQdY3X2LZqi7b3lYzZeC5oBPkB1M5679BUO9d0MWpFodo3WP3VYJTdHP37dYf1r-hYWbzTw92rd6w2tnfbGPd_zx-WSHf4</recordid><startdate>19950701</startdate><enddate>19950701</enddate><creator>Scannapieco, F.A.</creator><creator>Torres, G.I.</creator><creator>Levine, M.J.</creator><general>SAGE Publications</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19950701</creationdate><title>Salivary Amylase Promotes Adhesion of Oral Streptococci to Hydroxyapatite</title><author>Scannapieco, F.A. ; Torres, G.I. ; Levine, M.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-6778ec82153fecd042701f37faf251e8082747bf2e40161743396a964e0bc0933</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adhesins, Bacterial - drug effects</topic><topic>Adhesins, Bacterial - metabolism</topic><topic>Adult</topic><topic>Amylases - analysis</topic><topic>Amylases - isolation & purification</topic><topic>Amylases - metabolism</topic><topic>Amylases - pharmacology</topic><topic>Analysis of Variance</topic><topic>Bacterial Adhesion - drug effects</topic><topic>Dental Pellicle</topic><topic>Dentistry</topic><topic>Durapatite - metabolism</topic><topic>Enzymes, Immobilized - analysis</topic><topic>Enzymes, Immobilized - isolation & purification</topic><topic>Enzymes, Immobilized - metabolism</topic><topic>Enzymes, Immobilized - pharmacology</topic><topic>Humans</topic><topic>Male</topic><topic>Mouth - microbiology</topic><topic>Protein Binding - drug effects</topic><topic>Receptors, Immunologic - drug effects</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Saliva - chemistry</topic><topic>Saliva - enzymology</topic><topic>Streptococcus - metabolism</topic><topic>Streptococcus - pathogenicity</topic><topic>Streptococcus sanguis - metabolism</topic><topic>Streptococcus sanguis - pathogenicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scannapieco, F.A.</creatorcontrib><creatorcontrib>Torres, G.I.</creatorcontrib><creatorcontrib>Levine, M.J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of dental research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scannapieco, F.A.</au><au>Torres, G.I.</au><au>Levine, M.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Salivary Amylase Promotes Adhesion of Oral Streptococci to Hydroxyapatite</atitle><jtitle>Journal of dental research</jtitle><addtitle>J Dent Res</addtitle><date>1995-07-01</date><risdate>1995</risdate><volume>74</volume><issue>7</issue><spage>1360</spage><epage>1366</epage><pages>1360-1366</pages><issn>0022-0345</issn><eissn>1544-0591</eissn><abstract>Recent studies have demonstrated that several species of oral streptococci, such as Streptococcus gordonii, bind soluble salivary a-amylase. The goal of the present study was to determine if amylase immobilized onto a surface such as hydroxyapatite can serve as an adhesion receptor for S. gordonii. Initially, human parotid saliva was fractionated on Bio-Gel P60, and fractions were screened for their ability to promote adhesion of S. gordonii to hydroxyapatite. Fractions containing a-amylase and proline-rich proteins promoted the adhesion of [3H]-labeled S. gordonii to hydroxyapatite. Similar findings were obtained with purified amylase and acidic proline-rich protein 1 (PRP1). Incubation of S. gordonii G9B in the presence of starch and maltotriose increased the binding of this strain to amylase-coated hydroxyapatite, while the adhesion of S. sanguis 10556 to amylase-coated hydroxyapatite was not affected by these saccharides. These results suggest that amylase may serve as a hydroxyapatite pellicle receptor for amylase-binding streptococci. 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| subjects | Adhesins, Bacterial - drug effects Adhesins, Bacterial - metabolism Adult Amylases - analysis Amylases - isolation & purification Amylases - metabolism Amylases - pharmacology Analysis of Variance Bacterial Adhesion - drug effects Dental Pellicle Dentistry Durapatite - metabolism Enzymes, Immobilized - analysis Enzymes, Immobilized - isolation & purification Enzymes, Immobilized - metabolism Enzymes, Immobilized - pharmacology Humans Male Mouth - microbiology Protein Binding - drug effects Receptors, Immunologic - drug effects Receptors, Immunologic - metabolism Saliva - chemistry Saliva - enzymology Streptococcus - metabolism Streptococcus - pathogenicity Streptococcus sanguis - metabolism Streptococcus sanguis - pathogenicity |
| title | Salivary Amylase Promotes Adhesion of Oral Streptococci to Hydroxyapatite |
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