Identification of cell membrane proteins linked to susceptibility to bovine viral diarrhoea virus infection
Three monoclonal antibodies directed against cell surface molecules of bovine cells inhibited subsequent infections with bovine viral diarrhoea virus (BVDV). They specifically blocked the infectivity of three non-cytopathogenic and three cytopathogenic BVDV strains. These results showed that an impo...
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| Veröffentlicht in: | Archives of virology 1995-01, Vol.140 (11), p.1997-2009 |
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| container_issue | 11 |
| container_start_page | 1997 |
| container_title | Archives of virology |
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| creator | Schelp, C Greiser-Wilke, I Wolf, G Beer, M Moennig, V Liess, B |
| description | Three monoclonal antibodies directed against cell surface molecules of bovine cells inhibited subsequent infections with bovine viral diarrhoea virus (BVDV). They specifically blocked the infectivity of three non-cytopathogenic and three cytopathogenic BVDV strains. These results showed that an important mechanism for virus uptake was inhibited. The ligand of the monoclonal antibody BVD/CA 17, which blocked infectivity most efficiently, was found on leukocytes from a wide range of domestic and wild even-toed ungulates using flow cytometric analysis. In contrast, the monoclonal antibodies BVD/CA 26 and BVD/CA 27 appeared to be specific for bovine cells. Immunoprecipitation of labelled bovine cell surface proteins showed that the three monoclonal antibodies bound to proteins with identical relative molecular masses (Mr). Proteins of an apparent Mr of 93 K and 60 K were precipitated from lysates of fetal bovine kidney cells irrespectively of the MAbs used. |
| doi_str_mv | 10.1007/BF01322688 |
| format | Article |
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They specifically blocked the infectivity of three non-cytopathogenic and three cytopathogenic BVDV strains. These results showed that an important mechanism for virus uptake was inhibited. The ligand of the monoclonal antibody BVD/CA 17, which blocked infectivity most efficiently, was found on leukocytes from a wide range of domestic and wild even-toed ungulates using flow cytometric analysis. In contrast, the monoclonal antibodies BVD/CA 26 and BVD/CA 27 appeared to be specific for bovine cells. Immunoprecipitation of labelled bovine cell surface proteins showed that the three monoclonal antibodies bound to proteins with identical relative molecular masses (Mr). Proteins of an apparent Mr of 93 K and 60 K were precipitated from lysates of fetal bovine kidney cells irrespectively of the MAbs used.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/BF01322688</identifier><identifier>PMID: 7503697</identifier><language>eng</language><publisher>Wien: Springer</publisher><subject>Animals ; Antibodies, Monoclonal - immunology ; Biological and medical sciences ; Bovine viral diarrhea virus ; Bovine Virus Diarrhea-Mucosal Disease - microbiology ; calves ; Cattle ; Cell Membrane - immunology ; Cells, Cultured ; cultured cells ; cytopathogenicity ; Diarrhea Viruses, Bovine Viral - immunology ; flow cytometry ; Fundamental and applied biological sciences. Psychology ; immunoblotting ; infection ; kidneys ; leukocytes ; Membrane Proteins - chemistry ; Membrane Proteins - immunology ; Microbiology ; Molecular Weight ; monoclonal antibodies ; pathogenicity ; Receptors, Virus - chemistry ; Receptors, Virus - immunology ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Species Specificity ; strain differences ; viral proteins ; Virology</subject><ispartof>Archives of virology, 1995-01, Vol.140 (11), p.1997-2009</ispartof><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c335t-b0b77f016aae42287f4a9607fea431bc0244b19efc0a046a7315bd10e90bab7d3</citedby><cites>FETCH-LOGICAL-c335t-b0b77f016aae42287f4a9607fea431bc0244b19efc0a046a7315bd10e90bab7d3</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=2936075$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7503697$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schelp, C</creatorcontrib><creatorcontrib>Greiser-Wilke, I</creatorcontrib><creatorcontrib>Wolf, G</creatorcontrib><creatorcontrib>Beer, M</creatorcontrib><creatorcontrib>Moennig, V</creatorcontrib><creatorcontrib>Liess, B</creatorcontrib><title>Identification of cell membrane proteins linked to susceptibility to bovine viral diarrhoea virus infection</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><description>Three monoclonal antibodies directed against cell surface molecules of bovine cells inhibited subsequent infections with bovine viral diarrhoea virus (BVDV). They specifically blocked the infectivity of three non-cytopathogenic and three cytopathogenic BVDV strains. These results showed that an important mechanism for virus uptake was inhibited. The ligand of the monoclonal antibody BVD/CA 17, which blocked infectivity most efficiently, was found on leukocytes from a wide range of domestic and wild even-toed ungulates using flow cytometric analysis. In contrast, the monoclonal antibodies BVD/CA 26 and BVD/CA 27 appeared to be specific for bovine cells. Immunoprecipitation of labelled bovine cell surface proteins showed that the three monoclonal antibodies bound to proteins with identical relative molecular masses (Mr). Proteins of an apparent Mr of 93 K and 60 K were precipitated from lysates of fetal bovine kidney cells irrespectively of the MAbs used.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Biological and medical sciences</subject><subject>Bovine viral diarrhea virus</subject><subject>Bovine Virus Diarrhea-Mucosal Disease - microbiology</subject><subject>calves</subject><subject>Cattle</subject><subject>Cell Membrane - immunology</subject><subject>Cells, Cultured</subject><subject>cultured cells</subject><subject>cytopathogenicity</subject><subject>Diarrhea Viruses, Bovine Viral - immunology</subject><subject>flow cytometry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>immunoblotting</subject><subject>infection</subject><subject>kidneys</subject><subject>leukocytes</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - immunology</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>monoclonal antibodies</subject><subject>pathogenicity</subject><subject>Receptors, Virus - chemistry</subject><subject>Receptors, Virus - immunology</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Species Specificity</subject><subject>strain differences</subject><subject>viral proteins</subject><subject>Virology</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM1v1DAQxS0EKkvLhTvCB8QBKe34I3FyLBWFSpV6gJ6jsTMG0yRe7KRS_3sc7aqcRjPz05t5j7F3As4FgLn4cg1CSdm07Qu2E1rJqjVd-5LtQIGu2gba1-xNzn8AykDVJ-zE1KCazuzYw81A8xJ8cLiEOPPouaNx5BNNNuFMfJ_iQmHOfAzzAw18iTyv2dF-CTaMYXnaJjY-hsI-hoQjHwKm9DsSbv2aeZg9uU38jL3yOGZ6e6yn7P7668-r79Xt3bebq8vbyilVL5UFa4wH0SCSlrI1XmPXgPGEWgnrQGptRUfeAYJu0ChR20EAdWDRmkGdsk8H3fL735Xy0k8hb66Kn7jm3hijpNJQwM8H0KWYcyLf71OYMD31Avot2f5_sgV-f1Rd7UTDM3qMsuw_HveYHY6-pOdCfsZkp4qHumAfDpjH2OOvVJD7H7JcAVELuT32DyppisA</recordid><startdate>19950101</startdate><enddate>19950101</enddate><creator>Schelp, C</creator><creator>Greiser-Wilke, I</creator><creator>Wolf, G</creator><creator>Beer, M</creator><creator>Moennig, V</creator><creator>Liess, B</creator><general>Springer</general><scope>FBQ</scope><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>7X8</scope></search><sort><creationdate>19950101</creationdate><title>Identification of cell membrane proteins linked to susceptibility to bovine viral diarrhoea virus infection</title><author>Schelp, C ; Greiser-Wilke, I ; Wolf, G ; Beer, M ; Moennig, V ; Liess, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c335t-b0b77f016aae42287f4a9607fea431bc0244b19efc0a046a7315bd10e90bab7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Biological and medical sciences</topic><topic>Bovine viral diarrhea virus</topic><topic>Bovine Virus Diarrhea-Mucosal Disease - microbiology</topic><topic>calves</topic><topic>Cattle</topic><topic>Cell Membrane - immunology</topic><topic>Cells, Cultured</topic><topic>cultured cells</topic><topic>cytopathogenicity</topic><topic>Diarrhea Viruses, Bovine Viral - immunology</topic><topic>flow cytometry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>immunoblotting</topic><topic>infection</topic><topic>kidneys</topic><topic>leukocytes</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - immunology</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>monoclonal antibodies</topic><topic>pathogenicity</topic><topic>Receptors, Virus - chemistry</topic><topic>Receptors, Virus - immunology</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Species Specificity</topic><topic>strain differences</topic><topic>viral proteins</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schelp, C</creatorcontrib><creatorcontrib>Greiser-Wilke, I</creatorcontrib><creatorcontrib>Wolf, G</creatorcontrib><creatorcontrib>Beer, M</creatorcontrib><creatorcontrib>Moennig, V</creatorcontrib><creatorcontrib>Liess, B</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><jtitle>Archives of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schelp, C</au><au>Greiser-Wilke, I</au><au>Wolf, G</au><au>Beer, M</au><au>Moennig, V</au><au>Liess, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of cell membrane proteins linked to susceptibility to bovine viral diarrhoea virus infection</atitle><jtitle>Archives of virology</jtitle><addtitle>Arch Virol</addtitle><date>1995-01-01</date><risdate>1995</risdate><volume>140</volume><issue>11</issue><spage>1997</spage><epage>2009</epage><pages>1997-2009</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>Three monoclonal antibodies directed against cell surface molecules of bovine cells inhibited subsequent infections with bovine viral diarrhoea virus (BVDV). They specifically blocked the infectivity of three non-cytopathogenic and three cytopathogenic BVDV strains. These results showed that an important mechanism for virus uptake was inhibited. The ligand of the monoclonal antibody BVD/CA 17, which blocked infectivity most efficiently, was found on leukocytes from a wide range of domestic and wild even-toed ungulates using flow cytometric analysis. In contrast, the monoclonal antibodies BVD/CA 26 and BVD/CA 27 appeared to be specific for bovine cells. Immunoprecipitation of labelled bovine cell surface proteins showed that the three monoclonal antibodies bound to proteins with identical relative molecular masses (Mr). Proteins of an apparent Mr of 93 K and 60 K were precipitated from lysates of fetal bovine kidney cells irrespectively of the MAbs used.</abstract><cop>Wien</cop><cop>New York, NY</cop><pub>Springer</pub><pmid>7503697</pmid><doi>10.1007/BF01322688</doi><tpages>13</tpages></addata></record> |
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| subjects | Animals Antibodies, Monoclonal - immunology Biological and medical sciences Bovine viral diarrhea virus Bovine Virus Diarrhea-Mucosal Disease - microbiology calves Cattle Cell Membrane - immunology Cells, Cultured cultured cells cytopathogenicity Diarrhea Viruses, Bovine Viral - immunology flow cytometry Fundamental and applied biological sciences. Psychology immunoblotting infection kidneys leukocytes Membrane Proteins - chemistry Membrane Proteins - immunology Microbiology Molecular Weight monoclonal antibodies pathogenicity Receptors, Virus - chemistry Receptors, Virus - immunology Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Species Specificity strain differences viral proteins Virology |
| title | Identification of cell membrane proteins linked to susceptibility to bovine viral diarrhoea virus infection |
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