Loading…
Interaction of lysozyme with a surface protein antigen of Streptococcus mutans
Abstract The interaction of salivary lysozyme with the surface protein antigen (PAc) of Streptococcus mutans and the interaction of lysozyme with the pathogen were examined by ELISA using S. mutans MT8148 (PAc+) and the PAc-defective mutant EM-2 (PAc−). The lysozyme clearly bound to the S. mutans wi...
Saved in:
Published in: | FEMS microbiology letters 1996-06, Vol.139 (2-3), p.195-201 |
---|---|
Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c3955-fc0566ad63b7f3c263e54f7ce707e2070887c4902fd18977102d3c3988c5c4a73 |
---|---|
cites | cdi_FETCH-LOGICAL-c3955-fc0566ad63b7f3c263e54f7ce707e2070887c4902fd18977102d3c3988c5c4a73 |
container_end_page | 201 |
container_issue | 2-3 |
container_start_page | 195 |
container_title | FEMS microbiology letters |
container_volume | 139 |
creator | Senpuku, Hidenobu Kato, Hirohisa Todoroki, Megumi Hanada, Nobuhiro Nisizawa, Tosiki |
description | Abstract
The interaction of salivary lysozyme with the surface protein antigen (PAc) of Streptococcus mutans and the interaction of lysozyme with the pathogen were examined by ELISA using S. mutans MT8148 (PAc+) and the PAc-defective mutant EM-2 (PAc−). The lysozyme clearly bound to the S. mutans wild type but not to the S. mutans mutant. Furthermore, lysozyme bound directly in the fluid phase to the rPAc, of which the binding kinetics were determined (Kon= 3.63 ± 0.04 × 103M−1s−1, Koff= 1.72 ± 0.04 × 10−5s−1 and Kon / Koff= 2.11 × 108M−1) using surface plasmon resonance. The kinetics of both association and dissociation were relatively slow. In addition, anti-lysozyme antibody significantly inhibited the binding of salivary components to the rPAc. The present findings indicate that lysozyme is one of the major salivary components interacting with S. mutans PAc. |
doi_str_mv | 10.1111/j.1574-6968.1996.tb08202.x |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_78149902</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1111/j.1574-6968.1996.tb08202.x</oup_id><sourcerecordid>15626822</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3955-fc0566ad63b7f3c263e54f7ce707e2070887c4902fd18977102d3c3988c5c4a73</originalsourceid><addsrcrecordid>eNqVkUuLFDEURoMoYzv6E4RCxV2VN4_Kw8WADI4OtLpQ1yGdTrSaqkqbpJhpf70pu-iF-MBssrjn-7iXg9ATDA0u78Wuwa1gNVdcNlgp3uQNSAKkub2DVqfRXbQCKmSNQYn76EFKOwBgBPgZOpNcMCXlCr2_HrOLxuYujFXwVX9I4fthcNVNl79WpkpT9Ma6ah9Ddt1YmTF3X9xP9GOObp-DDdZOqRqmbMb0EN3zpk_u0fKfo89Xrz9dvq3XH95cX75a15aqtq29hZZzs-V0Izy1hFPXMi-sEyAcAQFSCssUEL_FUgmBgWxpiUppW8uMoOfo-bG37PVtcinroUvW9b0ZXZiSFhIzVfL_BHHLCZdkBp_-Au7CFMdyhCaUYglMElmol0fKxpBSdF7vYzeYeNAY9OxG7_QsQM8C9OxGL270bQmzv4QBcz370rMvXYIAmGFNS-zxstm0Gdz2FFoclvmzZW6SNb2PZrRdOmEUUyrxXHNxxG663h3-Y2999W6NVVsK2mNBmPZ_iNe_O_sHNZzKJQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2331804828</pqid></control><display><type>article</type><title>Interaction of lysozyme with a surface protein antigen of Streptococcus mutans</title><source>Oxford Journals Online</source><creator>Senpuku, Hidenobu ; Kato, Hirohisa ; Todoroki, Megumi ; Hanada, Nobuhiro ; Nisizawa, Tosiki</creator><creatorcontrib>Senpuku, Hidenobu ; Kato, Hirohisa ; Todoroki, Megumi ; Hanada, Nobuhiro ; Nisizawa, Tosiki</creatorcontrib><description>Abstract
The interaction of salivary lysozyme with the surface protein antigen (PAc) of Streptococcus mutans and the interaction of lysozyme with the pathogen were examined by ELISA using S. mutans MT8148 (PAc+) and the PAc-defective mutant EM-2 (PAc−). The lysozyme clearly bound to the S. mutans wild type but not to the S. mutans mutant. Furthermore, lysozyme bound directly in the fluid phase to the rPAc, of which the binding kinetics were determined (Kon= 3.63 ± 0.04 × 103M−1s−1, Koff= 1.72 ± 0.04 × 10−5s−1 and Kon / Koff= 2.11 × 108M−1) using surface plasmon resonance. The kinetics of both association and dissociation were relatively slow. In addition, anti-lysozyme antibody significantly inhibited the binding of salivary components to the rPAc. The present findings indicate that lysozyme is one of the major salivary components interacting with S. mutans PAc.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1996.tb08202.x</identifier><identifier>PMID: 8674988</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adult ; Antibodies ; Antigens ; Antigens, Surface - metabolism ; Association kinetic constant ; Bacterial Adhesion - physiology ; Bacterial Proteins - metabolism ; Bacteriology ; Binding ; Biological and medical sciences ; Biosensing Techniques ; Defective mutant ; Dissociation kinetic constant ; Enzyme-Linked Immunosorbent Assay ; Fundamental and applied biological sciences. Psychology ; Humans ; Kinetics ; Lysozyme ; Male ; Microbiology ; Muramidase - antagonists & inhibitors ; Muramidase - metabolism ; Muramidase - pharmacology ; Mutation - physiology ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Protein Binding - physiology ; Proteins ; Saliva - enzymology ; Streptococcus infections ; Streptococcus mutans ; Streptococcus mutans - immunology ; Surface plasmon resonance ; Surface protein antigen</subject><ispartof>FEMS microbiology letters, 1996-06, Vol.139 (2-3), p.195-201</ispartof><rights>1996 Federation of European Microbiological Societies. All rights reserved 1996</rights><rights>1996 INIST-CNRS</rights><rights>1996 Federation of European Microbiological Societies. All rights reserved</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3955-fc0566ad63b7f3c263e54f7ce707e2070887c4902fd18977102d3c3988c5c4a73</citedby><cites>FETCH-LOGICAL-c3955-fc0566ad63b7f3c263e54f7ce707e2070887c4902fd18977102d3c3988c5c4a73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3133813$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8674988$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Senpuku, Hidenobu</creatorcontrib><creatorcontrib>Kato, Hirohisa</creatorcontrib><creatorcontrib>Todoroki, Megumi</creatorcontrib><creatorcontrib>Hanada, Nobuhiro</creatorcontrib><creatorcontrib>Nisizawa, Tosiki</creatorcontrib><title>Interaction of lysozyme with a surface protein antigen of Streptococcus mutans</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
The interaction of salivary lysozyme with the surface protein antigen (PAc) of Streptococcus mutans and the interaction of lysozyme with the pathogen were examined by ELISA using S. mutans MT8148 (PAc+) and the PAc-defective mutant EM-2 (PAc−). The lysozyme clearly bound to the S. mutans wild type but not to the S. mutans mutant. Furthermore, lysozyme bound directly in the fluid phase to the rPAc, of which the binding kinetics were determined (Kon= 3.63 ± 0.04 × 103M−1s−1, Koff= 1.72 ± 0.04 × 10−5s−1 and Kon / Koff= 2.11 × 108M−1) using surface plasmon resonance. The kinetics of both association and dissociation were relatively slow. In addition, anti-lysozyme antibody significantly inhibited the binding of salivary components to the rPAc. The present findings indicate that lysozyme is one of the major salivary components interacting with S. mutans PAc.</description><subject>Adult</subject><subject>Antibodies</subject><subject>Antigens</subject><subject>Antigens, Surface - metabolism</subject><subject>Association kinetic constant</subject><subject>Bacterial Adhesion - physiology</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Binding</subject><subject>Biological and medical sciences</subject><subject>Biosensing Techniques</subject><subject>Defective mutant</subject><subject>Dissociation kinetic constant</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Lysozyme</subject><subject>Male</subject><subject>Microbiology</subject><subject>Muramidase - antagonists & inhibitors</subject><subject>Muramidase - metabolism</subject><subject>Muramidase - pharmacology</subject><subject>Mutation - physiology</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Protein Binding - physiology</subject><subject>Proteins</subject><subject>Saliva - enzymology</subject><subject>Streptococcus infections</subject><subject>Streptococcus mutans</subject><subject>Streptococcus mutans - immunology</subject><subject>Surface plasmon resonance</subject><subject>Surface protein antigen</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqVkUuLFDEURoMoYzv6E4RCxV2VN4_Kw8WADI4OtLpQ1yGdTrSaqkqbpJhpf70pu-iF-MBssrjn-7iXg9ATDA0u78Wuwa1gNVdcNlgp3uQNSAKkub2DVqfRXbQCKmSNQYn76EFKOwBgBPgZOpNcMCXlCr2_HrOLxuYujFXwVX9I4fthcNVNl79WpkpT9Ma6ah9Ddt1YmTF3X9xP9GOObp-DDdZOqRqmbMb0EN3zpk_u0fKfo89Xrz9dvq3XH95cX75a15aqtq29hZZzs-V0Izy1hFPXMi-sEyAcAQFSCssUEL_FUgmBgWxpiUppW8uMoOfo-bG37PVtcinroUvW9b0ZXZiSFhIzVfL_BHHLCZdkBp_-Au7CFMdyhCaUYglMElmol0fKxpBSdF7vYzeYeNAY9OxG7_QsQM8C9OxGL270bQmzv4QBcz370rMvXYIAmGFNS-zxstm0Gdz2FFoclvmzZW6SNb2PZrRdOmEUUyrxXHNxxG663h3-Y2999W6NVVsK2mNBmPZ_iNe_O_sHNZzKJQ</recordid><startdate>199606</startdate><enddate>199606</enddate><creator>Senpuku, Hidenobu</creator><creator>Kato, Hirohisa</creator><creator>Todoroki, Megumi</creator><creator>Hanada, Nobuhiro</creator><creator>Nisizawa, Tosiki</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>IQODW</scope><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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199606</creationdate><title>Interaction of lysozyme with a surface protein antigen of Streptococcus mutans</title><author>Senpuku, Hidenobu ; Kato, Hirohisa ; Todoroki, Megumi ; Hanada, Nobuhiro ; Nisizawa, Tosiki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3955-fc0566ad63b7f3c263e54f7ce707e2070887c4902fd18977102d3c3988c5c4a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adult</topic><topic>Antibodies</topic><topic>Antigens</topic><topic>Antigens, Surface - metabolism</topic><topic>Association kinetic constant</topic><topic>Bacterial Adhesion - physiology</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Binding</topic><topic>Biological and medical sciences</topic><topic>Biosensing Techniques</topic><topic>Defective mutant</topic><topic>Dissociation kinetic constant</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Lysozyme</topic><topic>Male</topic><topic>Microbiology</topic><topic>Muramidase - antagonists & inhibitors</topic><topic>Muramidase - metabolism</topic><topic>Muramidase - pharmacology</topic><topic>Mutation - physiology</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Protein Binding - physiology</topic><topic>Proteins</topic><topic>Saliva - enzymology</topic><topic>Streptococcus infections</topic><topic>Streptococcus mutans</topic><topic>Streptococcus mutans - immunology</topic><topic>Surface plasmon resonance</topic><topic>Surface protein antigen</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Senpuku, Hidenobu</creatorcontrib><creatorcontrib>Kato, Hirohisa</creatorcontrib><creatorcontrib>Todoroki, Megumi</creatorcontrib><creatorcontrib>Hanada, Nobuhiro</creatorcontrib><creatorcontrib>Nisizawa, Tosiki</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Senpuku, Hidenobu</au><au>Kato, Hirohisa</au><au>Todoroki, Megumi</au><au>Hanada, Nobuhiro</au><au>Nisizawa, Tosiki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of lysozyme with a surface protein antigen of Streptococcus mutans</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>1996-06</date><risdate>1996</risdate><volume>139</volume><issue>2-3</issue><spage>195</spage><epage>201</epage><pages>195-201</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
The interaction of salivary lysozyme with the surface protein antigen (PAc) of Streptococcus mutans and the interaction of lysozyme with the pathogen were examined by ELISA using S. mutans MT8148 (PAc+) and the PAc-defective mutant EM-2 (PAc−). The lysozyme clearly bound to the S. mutans wild type but not to the S. mutans mutant. Furthermore, lysozyme bound directly in the fluid phase to the rPAc, of which the binding kinetics were determined (Kon= 3.63 ± 0.04 × 103M−1s−1, Koff= 1.72 ± 0.04 × 10−5s−1 and Kon / Koff= 2.11 × 108M−1) using surface plasmon resonance. The kinetics of both association and dissociation were relatively slow. In addition, anti-lysozyme antibody significantly inhibited the binding of salivary components to the rPAc. The present findings indicate that lysozyme is one of the major salivary components interacting with S. mutans PAc.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8674988</pmid><doi>10.1111/j.1574-6968.1996.tb08202.x</doi><tpages>7</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0378-1097 |
ispartof | FEMS microbiology letters, 1996-06, Vol.139 (2-3), p.195-201 |
issn | 0378-1097 1574-6968 |
language | eng |
recordid | cdi_proquest_miscellaneous_78149902 |
source | Oxford Journals Online |
subjects | Adult Antibodies Antigens Antigens, Surface - metabolism Association kinetic constant Bacterial Adhesion - physiology Bacterial Proteins - metabolism Bacteriology Binding Biological and medical sciences Biosensing Techniques Defective mutant Dissociation kinetic constant Enzyme-Linked Immunosorbent Assay Fundamental and applied biological sciences. Psychology Humans Kinetics Lysozyme Male Microbiology Muramidase - antagonists & inhibitors Muramidase - metabolism Muramidase - pharmacology Mutation - physiology Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Protein Binding - physiology Proteins Saliva - enzymology Streptococcus infections Streptococcus mutans Streptococcus mutans - immunology Surface plasmon resonance Surface protein antigen |
title | Interaction of lysozyme with a surface protein antigen of Streptococcus mutans |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T04%3A25%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Interaction%20of%20lysozyme%20with%20a%20surface%20protein%20antigen%20of%20Streptococcus%20mutans&rft.jtitle=FEMS%20microbiology%20letters&rft.au=Senpuku,%20Hidenobu&rft.date=1996-06&rft.volume=139&rft.issue=2-3&rft.spage=195&rft.epage=201&rft.pages=195-201&rft.issn=0378-1097&rft.eissn=1574-6968&rft.coden=FMLED7&rft_id=info:doi/10.1111/j.1574-6968.1996.tb08202.x&rft_dat=%3Cproquest_cross%3E15626822%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3955-fc0566ad63b7f3c263e54f7ce707e2070887c4902fd18977102d3c3988c5c4a73%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2331804828&rft_id=info:pmid/8674988&rft_oup_id=10.1111/j.1574-6968.1996.tb08202.x&rfr_iscdi=true |