Binding selectivity of Streptococcus pyogenes and M-protein to epithelial cells differs from that of lipoteichoic acid

The ability of M-protein-positive (M super(+)) and M-protein-negative (M super(-)) strains (including an M super(-) mutant lacking the structural gene for M-protein) of Streptococcus pyogenes) to attach to human pharyngeal, and tongue epithelial cells was compared. M super(+) strains of S. pyogenes)...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Current microbiology 1988-01, Vol.16 (4), p.209-216
Hauptverfasser: TYLENSKA, S. K, FISCHETTI, V. A, GIBBONS, R. J
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 216
container_issue 4
container_start_page 209
container_title Current microbiology
container_volume 16
creator TYLENSKA, S. K
FISCHETTI, V. A
GIBBONS, R. J
description The ability of M-protein-positive (M super(+)) and M-protein-negative (M super(-)) strains (including an M super(-) mutant lacking the structural gene for M-protein) of Streptococcus pyogenes) to attach to human pharyngeal, and tongue epithelial cells was compared. M super(+) strains of S. pyogenes) attached in higher numbers to human pharyngeal epithelial cells than to human buccal or tongue cells. M super(-) strains did not exhibit high-level binding to any type of epithelial cell. Adhesion of an M super(+) and an M super(-) strain of S. pyogenes) was low to all types of rat epithelial cells. The differences in the surface components between human pharyngeal and buccal epithelial cells were confirmed by studies utilizing radiolabeled lectins. Ulex europaeus lectin with a specificity for fucosyl residues, and Triticum vulgaris lectin with a specificity for N-acetyl glucosamine and N-acetyl neuraminic acid residues, bound in higher amounts to human pharyngeal cells than to buccal cells.
doi_str_mv 10.1007/bf01568531
format Article
fullrecord <record><control><sourceid>proquest_pasca</sourceid><recordid>TN_cdi_proquest_miscellaneous_14952508</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>14952508</sourcerecordid><originalsourceid>FETCH-LOGICAL-n242t-cba5a530000b36249c0aec8f0ef61bbf005b014d0ddfa82c3e37478c1e51a63a3</originalsourceid><addsrcrecordid>eNotTz1PwzAUtBBIlMLCL_CA2ALPcZw4I1R8SUUMwBy9OM-tkRuH2K3Uf08qejfccne6Y-xawJ0AqO5bC0KVWklxwmaikHkGdS1O2QxkITNdKnHOLmL8ARB5DWLGdo-u71y_4pE8meR2Lu15sPwzjTSkYIIx28iHfVhRT5Fj3_H3bBhDItfzFDgNLq3JO_TckPeRd85aGiO3Y9jwtMZ0aPNuOCTMOjjD0bjukp1Z9JGujjpn389PX4vXbPnx8rZ4WGZ9XuQpMy0qVBImtLLMi9oAktEWyJainc6CakEUHXSdRZ0bSbIqKm0EKYGlRDlnt_-90-TfLcXUbFw8DMWewjY2oqhVrkBPxpujEaNBb0fsjYvNMLoNjvum0mKiln_2rW1J</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14952508</pqid></control><display><type>article</type><title>Binding selectivity of Streptococcus pyogenes and M-protein to epithelial cells differs from that of lipoteichoic acid</title><source>SpringerLink Journals - AutoHoldings</source><creator>TYLENSKA, S. K ; FISCHETTI, V. A ; GIBBONS, R. J</creator><creatorcontrib>TYLENSKA, S. K ; FISCHETTI, V. A ; GIBBONS, R. J</creatorcontrib><description>The ability of M-protein-positive (M super(+)) and M-protein-negative (M super(-)) strains (including an M super(-) mutant lacking the structural gene for M-protein) of Streptococcus pyogenes) to attach to human pharyngeal, and tongue epithelial cells was compared. M super(+) strains of S. pyogenes) attached in higher numbers to human pharyngeal epithelial cells than to human buccal or tongue cells. M super(-) strains did not exhibit high-level binding to any type of epithelial cell. Adhesion of an M super(+) and an M super(-) strain of S. pyogenes) was low to all types of rat epithelial cells. The differences in the surface components between human pharyngeal and buccal epithelial cells were confirmed by studies utilizing radiolabeled lectins. Ulex europaeus lectin with a specificity for fucosyl residues, and Triticum vulgaris lectin with a specificity for N-acetyl glucosamine and N-acetyl neuraminic acid residues, bound in higher amounts to human pharyngeal cells than to buccal cells.</description><identifier>ISSN: 0343-8651</identifier><identifier>EISSN: 1432-0991</identifier><identifier>DOI: 10.1007/bf01568531</identifier><identifier>CODEN: CUMIDD</identifier><language>eng</language><publisher>New York, NY: Springer</publisher><subject>Bacteriology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Streptococcus pyogenes</subject><ispartof>Current microbiology, 1988-01, Vol.16 (4), p.209-216</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=7818188$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>TYLENSKA, S. K</creatorcontrib><creatorcontrib>FISCHETTI, V. A</creatorcontrib><creatorcontrib>GIBBONS, R. J</creatorcontrib><title>Binding selectivity of Streptococcus pyogenes and M-protein to epithelial cells differs from that of lipoteichoic acid</title><title>Current microbiology</title><description>The ability of M-protein-positive (M super(+)) and M-protein-negative (M super(-)) strains (including an M super(-) mutant lacking the structural gene for M-protein) of Streptococcus pyogenes) to attach to human pharyngeal, and tongue epithelial cells was compared. M super(+) strains of S. pyogenes) attached in higher numbers to human pharyngeal epithelial cells than to human buccal or tongue cells. M super(-) strains did not exhibit high-level binding to any type of epithelial cell. Adhesion of an M super(+) and an M super(-) strain of S. pyogenes) was low to all types of rat epithelial cells. The differences in the surface components between human pharyngeal and buccal epithelial cells were confirmed by studies utilizing radiolabeled lectins. Ulex europaeus lectin with a specificity for fucosyl residues, and Triticum vulgaris lectin with a specificity for N-acetyl glucosamine and N-acetyl neuraminic acid residues, bound in higher amounts to human pharyngeal cells than to buccal cells.</description><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Streptococcus pyogenes</subject><issn>0343-8651</issn><issn>1432-0991</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><recordid>eNotTz1PwzAUtBBIlMLCL_CA2ALPcZw4I1R8SUUMwBy9OM-tkRuH2K3Uf08qejfccne6Y-xawJ0AqO5bC0KVWklxwmaikHkGdS1O2QxkITNdKnHOLmL8ARB5DWLGdo-u71y_4pE8meR2Lu15sPwzjTSkYIIx28iHfVhRT5Fj3_H3bBhDItfzFDgNLq3JO_TckPeRd85aGiO3Y9jwtMZ0aPNuOCTMOjjD0bjukp1Z9JGujjpn389PX4vXbPnx8rZ4WGZ9XuQpMy0qVBImtLLMi9oAktEWyJainc6CakEUHXSdRZ0bSbIqKm0EKYGlRDlnt_-90-TfLcXUbFw8DMWewjY2oqhVrkBPxpujEaNBb0fsjYvNMLoNjvum0mKiln_2rW1J</recordid><startdate>19880101</startdate><enddate>19880101</enddate><creator>TYLENSKA, S. K</creator><creator>FISCHETTI, V. A</creator><creator>GIBBONS, R. J</creator><general>Springer</general><scope>IQODW</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>19880101</creationdate><title>Binding selectivity of Streptococcus pyogenes and M-protein to epithelial cells differs from that of lipoteichoic acid</title><author>TYLENSKA, S. K ; FISCHETTI, V. A ; GIBBONS, R. J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-n242t-cba5a530000b36249c0aec8f0ef61bbf005b014d0ddfa82c3e37478c1e51a63a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Streptococcus pyogenes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TYLENSKA, S. K</creatorcontrib><creatorcontrib>FISCHETTI, V. A</creatorcontrib><creatorcontrib>GIBBONS, R. J</creatorcontrib><collection>Pascal-Francis</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Current microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>TYLENSKA, S. K</au><au>FISCHETTI, V. A</au><au>GIBBONS, R. J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding selectivity of Streptococcus pyogenes and M-protein to epithelial cells differs from that of lipoteichoic acid</atitle><jtitle>Current microbiology</jtitle><date>1988-01-01</date><risdate>1988</risdate><volume>16</volume><issue>4</issue><spage>209</spage><epage>216</epage><pages>209-216</pages><issn>0343-8651</issn><eissn>1432-0991</eissn><coden>CUMIDD</coden><abstract>The ability of M-protein-positive (M super(+)) and M-protein-negative (M super(-)) strains (including an M super(-) mutant lacking the structural gene for M-protein) of Streptococcus pyogenes) to attach to human pharyngeal, and tongue epithelial cells was compared. M super(+) strains of S. pyogenes) attached in higher numbers to human pharyngeal epithelial cells than to human buccal or tongue cells. M super(-) strains did not exhibit high-level binding to any type of epithelial cell. Adhesion of an M super(+) and an M super(-) strain of S. pyogenes) was low to all types of rat epithelial cells. The differences in the surface components between human pharyngeal and buccal epithelial cells were confirmed by studies utilizing radiolabeled lectins. Ulex europaeus lectin with a specificity for fucosyl residues, and Triticum vulgaris lectin with a specificity for N-acetyl glucosamine and N-acetyl neuraminic acid residues, bound in higher amounts to human pharyngeal cells than to buccal cells.</abstract><cop>New York, NY</cop><pub>Springer</pub><doi>10.1007/bf01568531</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0343-8651
ispartof Current microbiology, 1988-01, Vol.16 (4), p.209-216
issn 0343-8651
1432-0991
language eng
recordid cdi_proquest_miscellaneous_14952508
source SpringerLink Journals - AutoHoldings
subjects Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Microbiology
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Streptococcus pyogenes
title Binding selectivity of Streptococcus pyogenes and M-protein to epithelial cells differs from that of lipoteichoic acid
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-11T03%3A12%3A07IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Binding%20selectivity%20of%20Streptococcus%20pyogenes%20and%20M-protein%20to%20epithelial%20cells%20differs%20from%20that%20of%20lipoteichoic%20acid&rft.jtitle=Current%20microbiology&rft.au=TYLENSKA,%20S.%20K&rft.date=1988-01-01&rft.volume=16&rft.issue=4&rft.spage=209&rft.epage=216&rft.pages=209-216&rft.issn=0343-8651&rft.eissn=1432-0991&rft.coden=CUMIDD&rft_id=info:doi/10.1007/bf01568531&rft_dat=%3Cproquest_pasca%3E14952508%3C/proquest_pasca%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14952508&rft_id=info:pmid/&rfr_iscdi=true