Quantitation of Tamm-Horsfall Protein Binding to Uropathogenic Escherichia coli and Lectins
In quantitative experiments using ELISA, binding of Tamm-Horsfall protein (THP) to uropathogenic Escherichia coli was studied with monoclonal antibody to THP. Adherence to E. coli bearing type 1 fimbriae was proportional to THP concentration and size of the bacterial inoculum. Type 1 fimbriae-bearin...
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| Veröffentlicht in: | The Journal of infectious diseases 1990-12, Vol.162 (6), p.1335-1340 |
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| creator | Reinhart, Harald H. Obedeanu, Nora Sobel, Jack D. |
| description | In quantitative experiments using ELISA, binding of Tamm-Horsfall protein (THP) to uropathogenic Escherichia coli was studied with monoclonal antibody to THP. Adherence to E. coli bearing type 1 fimbriae was proportional to THP concentration and size of the bacterial inoculum. Type 1 fimbriae-bearing E. coli bound 50 times more THP than did non-type 1-fimbriated or P-fimbriated strains. Concanavalin A and wheat germ agglutinin bound THP in a dosedependent fashion, whereas pokeweed mitogen and Vicia villosa B4 isolectin did not. Addition of mannose and N-acetylglucosamine reduced adherence of THP to concanavalin A and wheat germ agglutinin by 50%-80%-Sugar inhibition studies suggested that the fimbrial receptor site for THP has lectin-like properties and that THP binds to fimbriae via its mannose side chains. This quantitative assay is useful for studying the interaction between THP, uroepithelial cells, and bacteria in vitro. |
| doi_str_mv | 10.1093/infdis/162.6.1335 |
| format | Article |
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Adherence to E. coli bearing type 1 fimbriae was proportional to THP concentration and size of the bacterial inoculum. Type 1 fimbriae-bearing E. coli bound 50 times more THP than did non-type 1-fimbriated or P-fimbriated strains. Concanavalin A and wheat germ agglutinin bound THP in a dosedependent fashion, whereas pokeweed mitogen and Vicia villosa B4 isolectin did not. Addition of mannose and N-acetylglucosamine reduced adherence of THP to concanavalin A and wheat germ agglutinin by 50%-80%-Sugar inhibition studies suggested that the fimbrial receptor site for THP has lectin-like properties and that THP binds to fimbriae via its mannose side chains. This quantitative assay is useful for studying the interaction between THP, uroepithelial cells, and bacteria in vitro.</description><identifier>ISSN: 0022-1899</identifier><identifier>EISSN: 1537-6613</identifier><identifier>DOI: 10.1093/infdis/162.6.1335</identifier><identifier>PMID: 1977810</identifier><identifier>CODEN: JIDIAQ</identifier><language>eng</language><publisher>Chicago, IL: University of Chicago Press</publisher><subject>Agglutination ; Agglutination Tests ; Bacteria ; Bacterial Adhesion - drug effects ; Bacteriology ; Biological and medical sciences ; Carbohydrates - pharmacology ; Concanavalin A - metabolism ; Enzyme-Linked Immunosorbent Assay ; Erythrocytes ; Escherichia coli ; Escherichia coli - drug effects ; Escherichia coli - metabolism ; Escherichia coli - ultrastructure ; Escherichia coli Infections - microbiology ; Fimbriae ; Fimbriae, Bacterial - metabolism ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Humans ; Lectins ; Lectins - metabolism ; Major Articles ; Microbiology ; Motility, taxis ; Mucoproteins - metabolism ; Receptors ; Sugars ; Urinary Tract Infections - microbiology ; Urine ; Uromodulin ; Wheat Germ Agglutinins - metabolism</subject><ispartof>The Journal of infectious diseases, 1990-12, Vol.162 (6), p.1335-1340</ispartof><rights>Copyright 1990 The University of Chicago</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30127908$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30127908$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5344316$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1977810$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reinhart, Harald H.</creatorcontrib><creatorcontrib>Obedeanu, Nora</creatorcontrib><creatorcontrib>Sobel, Jack D.</creatorcontrib><title>Quantitation of Tamm-Horsfall Protein Binding to Uropathogenic Escherichia coli and Lectins</title><title>The Journal of infectious diseases</title><addtitle>J Infect Dis</addtitle><description>In quantitative experiments using ELISA, binding of Tamm-Horsfall protein (THP) to uropathogenic Escherichia coli was studied with monoclonal antibody to THP. Adherence to E. coli bearing type 1 fimbriae was proportional to THP concentration and size of the bacterial inoculum. Type 1 fimbriae-bearing E. coli bound 50 times more THP than did non-type 1-fimbriated or P-fimbriated strains. Concanavalin A and wheat germ agglutinin bound THP in a dosedependent fashion, whereas pokeweed mitogen and Vicia villosa B4 isolectin did not. Addition of mannose and N-acetylglucosamine reduced adherence of THP to concanavalin A and wheat germ agglutinin by 50%-80%-Sugar inhibition studies suggested that the fimbrial receptor site for THP has lectin-like properties and that THP binds to fimbriae via its mannose side chains. This quantitative assay is useful for studying the interaction between THP, uroepithelial cells, and bacteria in vitro.</description><subject>Agglutination</subject><subject>Agglutination Tests</subject><subject>Bacteria</subject><subject>Bacterial Adhesion - drug effects</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Carbohydrates - pharmacology</subject><subject>Concanavalin A - metabolism</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Erythrocytes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli - ultrastructure</subject><subject>Escherichia coli Infections - microbiology</subject><subject>Fimbriae</subject><subject>Fimbriae, Bacterial - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Humans</subject><subject>Lectins</subject><subject>Lectins - metabolism</subject><subject>Major Articles</subject><subject>Microbiology</subject><subject>Motility, taxis</subject><subject>Mucoproteins - metabolism</subject><subject>Receptors</subject><subject>Sugars</subject><subject>Urinary Tract Infections - microbiology</subject><subject>Urine</subject><subject>Uromodulin</subject><subject>Wheat Germ Agglutinins - metabolism</subject><issn>0022-1899</issn><issn>1537-6613</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFj81KAzEYRYMotVYfwIWQhdtp8yWZTGapUq1QUKFduSiZ_LQp06Qk6cK3t2Cpq7s4lwMHoXsgYyAtm_jgjM8TEHQsxsBYfYGGULOmEgLYJRoSQmkFsm2v0U3OW0IIZ6IZoAG0TSOBDNH310GF4osqPgYcHV6o3a6axZSd6nv8mWKxPuBnH4wPa1wiXqa4V2UT1zZ4jadZb2zyeuMV1rH3WAWD51YXH_ItujpKsr077QgtX6eLl1k1_3h7f3maV1uoZak0BeGssqIGygTjLUBXG6kNF1RZ3dVCMum4451pnGSmoWCklNByxlUHhI3Qw593f-h21qz2ye9U-lmdIo_88cRV1qp3SQXt8_lWM84ZiH_NNpeYzpgRoE1LJPsF6a9rjQ</recordid><startdate>19901201</startdate><enddate>19901201</enddate><creator>Reinhart, Harald H.</creator><creator>Obedeanu, Nora</creator><creator>Sobel, Jack D.</creator><general>University of Chicago Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>19901201</creationdate><title>Quantitation of Tamm-Horsfall Protein Binding to Uropathogenic Escherichia coli and Lectins</title><author>Reinhart, Harald H. ; Obedeanu, Nora ; Sobel, Jack D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j158t-c216feae65123634911b5d8cd462aecb56838f4f4bd7f83d721d88819434ab103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Agglutination</topic><topic>Agglutination Tests</topic><topic>Bacteria</topic><topic>Bacterial Adhesion - drug effects</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Carbohydrates - pharmacology</topic><topic>Concanavalin A - metabolism</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Erythrocytes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli - ultrastructure</topic><topic>Escherichia coli Infections - microbiology</topic><topic>Fimbriae</topic><topic>Fimbriae, Bacterial - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Humans</topic><topic>Lectins</topic><topic>Lectins - metabolism</topic><topic>Major Articles</topic><topic>Microbiology</topic><topic>Motility, taxis</topic><topic>Mucoproteins - metabolism</topic><topic>Receptors</topic><topic>Sugars</topic><topic>Urinary Tract Infections - microbiology</topic><topic>Urine</topic><topic>Uromodulin</topic><topic>Wheat Germ Agglutinins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reinhart, Harald H.</creatorcontrib><creatorcontrib>Obedeanu, Nora</creatorcontrib><creatorcontrib>Sobel, Jack D.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>The Journal of infectious diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reinhart, Harald H.</au><au>Obedeanu, Nora</au><au>Sobel, Jack D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitation of Tamm-Horsfall Protein Binding to Uropathogenic Escherichia coli and Lectins</atitle><jtitle>The Journal of infectious diseases</jtitle><addtitle>J Infect Dis</addtitle><date>1990-12-01</date><risdate>1990</risdate><volume>162</volume><issue>6</issue><spage>1335</spage><epage>1340</epage><pages>1335-1340</pages><issn>0022-1899</issn><eissn>1537-6613</eissn><coden>JIDIAQ</coden><abstract>In quantitative experiments using ELISA, binding of Tamm-Horsfall protein (THP) to uropathogenic Escherichia coli was studied with monoclonal antibody to THP. Adherence to E. coli bearing type 1 fimbriae was proportional to THP concentration and size of the bacterial inoculum. Type 1 fimbriae-bearing E. coli bound 50 times more THP than did non-type 1-fimbriated or P-fimbriated strains. Concanavalin A and wheat germ agglutinin bound THP in a dosedependent fashion, whereas pokeweed mitogen and Vicia villosa B4 isolectin did not. Addition of mannose and N-acetylglucosamine reduced adherence of THP to concanavalin A and wheat germ agglutinin by 50%-80%-Sugar inhibition studies suggested that the fimbrial receptor site for THP has lectin-like properties and that THP binds to fimbriae via its mannose side chains. This quantitative assay is useful for studying the interaction between THP, uroepithelial cells, and bacteria in vitro.</abstract><cop>Chicago, IL</cop><pub>University of Chicago Press</pub><pmid>1977810</pmid><doi>10.1093/infdis/162.6.1335</doi><tpages>6</tpages></addata></record> |
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| ispartof | The Journal of infectious diseases, 1990-12, Vol.162 (6), p.1335-1340 |
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| subjects | Agglutination Agglutination Tests Bacteria Bacterial Adhesion - drug effects Bacteriology Biological and medical sciences Carbohydrates - pharmacology Concanavalin A - metabolism Enzyme-Linked Immunosorbent Assay Erythrocytes Escherichia coli Escherichia coli - drug effects Escherichia coli - metabolism Escherichia coli - ultrastructure Escherichia coli Infections - microbiology Fimbriae Fimbriae, Bacterial - metabolism Fundamental and applied biological sciences. Psychology Glycoproteins Humans Lectins Lectins - metabolism Major Articles Microbiology Motility, taxis Mucoproteins - metabolism Receptors Sugars Urinary Tract Infections - microbiology Urine Uromodulin Wheat Germ Agglutinins - metabolism |
| title | Quantitation of Tamm-Horsfall Protein Binding to Uropathogenic Escherichia coli and Lectins |
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