Preparation and Characterization of Monoclonal Antibodies Directed against Five Structural Components of Human Respiratory Syncytial Virus Subgroup B
1 Department of Virology, National Bacteriological Laboratory, S-105 21 Stockholm, 2 Department of Virology, Karolinska Institute, S-105 21 Stockholm, Sweden and 3 Department of Medicine, Marshall University School of Medicine and Veterans Administration Medical Center, Huntington, West Virginia, U....
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| Veröffentlicht in: | Journal of general virology 1987-12, Vol.68 (12), p.3125-3135 |
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| creator | Orvell, Claes Norrby, Erling Mufson, Maurice A |
| description | 1 Department of Virology, National Bacteriological Laboratory, S-105 21 Stockholm,
2 Department of Virology, Karolinska Institute, S-105 21 Stockholm, Sweden
and 3 Department of Medicine, Marshall University School of Medicine and Veterans Administration Medical Center, Huntington, West Virginia, U.S.A.
Mouse hybridomas producing antibodies against the structural proteins of strain WV4843, a subgroup B strain of respiratory syncytial (RS) virus, were produced by fusion of Sp2/0 myeloma cells with spleen cells from BALB/c mice immunized with purified preparations of the virus. After immunoprecipitation tests with [ 35 S]methionine-labelled extracellular virions, 35 clones found to produce antibodies against the fusion (F) protein, six against the membrane (M) protein, 21 against the nucleocapsid (NP) and eight against the phospho- (P) protein were further characterized. Immunoprecipitation with [ 3 H]glucosamine-labelled intracellular virus polypeptides detected nine hybridoma cell lines producing antibodies against the large glyco- (G) protein of the virus. By competitive binding ELISA tests with monoclonal antibodies against each of the structural components, a minimum of two, 24, four, 15 and three epitopes were detected on the G, F, M, NP and P proteins, respectively. Eleven monoclonal antibodies directed against nine epitopes of the F protein could neutralize the infectivity of the virus. In contrast, none of the nine monoclonal antibodies against G could neutralize the infectivity of the virus. In order to find out more about the antigenic relationship between human and bovine RS virus strains all monoclonal antibodies were reacted with subgroup A RS virus and also with three different strains of bovine RS virus and one strain of caprine RS virus in immunofluorescence, ELISA and immunoprecipitation tests. In addition, 31 previously developed monoclonal antibodies against subgroup A virus were reacted with the bovine and caprine strains. The numbers of monoclonal antibodies of subgroup B specific for the B type of the two human subgroups were 9/9, 3/35, 0/6, 0/21, 0/8, for the G, F, M, NP and P proteins, respectively. No antigenic variations were found between the three bovine strains and the caprine strain. They did not react with the nine monoclonal antibodies against the G protein of subgroup B, nor did they react with nine monoclonal antibodies against subgroup A. Most but not all of the monoclonal antibodies against the other structural proteins o |
| doi_str_mv | 10.1099/0022-1317-68-12-3125 |
| format | Article |
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2 Department of Virology, Karolinska Institute, S-105 21 Stockholm, Sweden
and 3 Department of Medicine, Marshall University School of Medicine and Veterans Administration Medical Center, Huntington, West Virginia, U.S.A.
Mouse hybridomas producing antibodies against the structural proteins of strain WV4843, a subgroup B strain of respiratory syncytial (RS) virus, were produced by fusion of Sp2/0 myeloma cells with spleen cells from BALB/c mice immunized with purified preparations of the virus. After immunoprecipitation tests with [ 35 S]methionine-labelled extracellular virions, 35 clones found to produce antibodies against the fusion (F) protein, six against the membrane (M) protein, 21 against the nucleocapsid (NP) and eight against the phospho- (P) protein were further characterized. Immunoprecipitation with [ 3 H]glucosamine-labelled intracellular virus polypeptides detected nine hybridoma cell lines producing antibodies against the large glyco- (G) protein of the virus. By competitive binding ELISA tests with monoclonal antibodies against each of the structural components, a minimum of two, 24, four, 15 and three epitopes were detected on the G, F, M, NP and P proteins, respectively. Eleven monoclonal antibodies directed against nine epitopes of the F protein could neutralize the infectivity of the virus. In contrast, none of the nine monoclonal antibodies against G could neutralize the infectivity of the virus. In order to find out more about the antigenic relationship between human and bovine RS virus strains all monoclonal antibodies were reacted with subgroup A RS virus and also with three different strains of bovine RS virus and one strain of caprine RS virus in immunofluorescence, ELISA and immunoprecipitation tests. In addition, 31 previously developed monoclonal antibodies against subgroup A virus were reacted with the bovine and caprine strains. The numbers of monoclonal antibodies of subgroup B specific for the B type of the two human subgroups were 9/9, 3/35, 0/6, 0/21, 0/8, for the G, F, M, NP and P proteins, respectively. No antigenic variations were found between the three bovine strains and the caprine strain. They did not react with the nine monoclonal antibodies against the G protein of subgroup B, nor did they react with nine monoclonal antibodies against subgroup A. Most but not all of the monoclonal antibodies against the other structural proteins of the two human RS virus subgroups reacted with the four strains. All 11 monoclonal antibodies against the F protein of subgroup B that could neutralize the infectivity of subgroup B also reacted with the bovine strains and neutralized their infectivity. It is concluded that although the bovine strains share many epitopes with the two human subgroups, they are antigenically distinct from the human viruses.
Keywords: respiratory syncytial virus, structural proteins, monoclonal antibodies
Received 23 April 1987;
accepted 29 July 1987.</description><identifier>ISSN: 0022-1317</identifier><identifier>EISSN: 1465-2099</identifier><identifier>DOI: 10.1099/0022-1317-68-12-3125</identifier><identifier>PMID: 2447224</identifier><identifier>CODEN: JGVIAY</identifier><language>eng</language><publisher>Reading: Soc General Microbiol</publisher><subject>Antibodies, Monoclonal - immunology ; Antibodies, Viral - immunology ; Antibody Specificity ; Antigens, Viral - immunology ; Biological and medical sciences ; Capsid - immunology ; Epitopes ; Fundamental and applied biological sciences. Psychology ; Microbiology ; respiratory syncytial virus ; Respiratory Syncytial Viruses - immunology ; Techniques used in virology ; Viral Core Proteins - immunology ; Viral Fusion Proteins - immunology ; Viral Matrix Proteins - immunology ; Viral Proteins - immunology ; Virology</subject><ispartof>Journal of general virology, 1987-12, Vol.68 (12), p.3125-3135</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3575-3c27a891eca3045b3df7de9d652c7a469a964359f0d6c2618dfc76054339d9b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,3735,3736,27911,27912</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7567385$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2447224$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Orvell, Claes</creatorcontrib><creatorcontrib>Norrby, Erling</creatorcontrib><creatorcontrib>Mufson, Maurice A</creatorcontrib><title>Preparation and Characterization of Monoclonal Antibodies Directed against Five Structural Components of Human Respiratory Syncytial Virus Subgroup B</title><title>Journal of general virology</title><addtitle>J Gen Virol</addtitle><description>1 Department of Virology, National Bacteriological Laboratory, S-105 21 Stockholm,
2 Department of Virology, Karolinska Institute, S-105 21 Stockholm, Sweden
and 3 Department of Medicine, Marshall University School of Medicine and Veterans Administration Medical Center, Huntington, West Virginia, U.S.A.
Mouse hybridomas producing antibodies against the structural proteins of strain WV4843, a subgroup B strain of respiratory syncytial (RS) virus, were produced by fusion of Sp2/0 myeloma cells with spleen cells from BALB/c mice immunized with purified preparations of the virus. After immunoprecipitation tests with [ 35 S]methionine-labelled extracellular virions, 35 clones found to produce antibodies against the fusion (F) protein, six against the membrane (M) protein, 21 against the nucleocapsid (NP) and eight against the phospho- (P) protein were further characterized. Immunoprecipitation with [ 3 H]glucosamine-labelled intracellular virus polypeptides detected nine hybridoma cell lines producing antibodies against the large glyco- (G) protein of the virus. By competitive binding ELISA tests with monoclonal antibodies against each of the structural components, a minimum of two, 24, four, 15 and three epitopes were detected on the G, F, M, NP and P proteins, respectively. Eleven monoclonal antibodies directed against nine epitopes of the F protein could neutralize the infectivity of the virus. In contrast, none of the nine monoclonal antibodies against G could neutralize the infectivity of the virus. In order to find out more about the antigenic relationship between human and bovine RS virus strains all monoclonal antibodies were reacted with subgroup A RS virus and also with three different strains of bovine RS virus and one strain of caprine RS virus in immunofluorescence, ELISA and immunoprecipitation tests. In addition, 31 previously developed monoclonal antibodies against subgroup A virus were reacted with the bovine and caprine strains. The numbers of monoclonal antibodies of subgroup B specific for the B type of the two human subgroups were 9/9, 3/35, 0/6, 0/21, 0/8, for the G, F, M, NP and P proteins, respectively. No antigenic variations were found between the three bovine strains and the caprine strain. They did not react with the nine monoclonal antibodies against the G protein of subgroup B, nor did they react with nine monoclonal antibodies against subgroup A. Most but not all of the monoclonal antibodies against the other structural proteins of the two human RS virus subgroups reacted with the four strains. All 11 monoclonal antibodies against the F protein of subgroup B that could neutralize the infectivity of subgroup B also reacted with the bovine strains and neutralized their infectivity. It is concluded that although the bovine strains share many epitopes with the two human subgroups, they are antigenically distinct from the human viruses.
Keywords: respiratory syncytial virus, structural proteins, monoclonal antibodies
Received 23 April 1987;
accepted 29 July 1987.</description><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Viral - immunology</subject><subject>Antibody Specificity</subject><subject>Antigens, Viral - immunology</subject><subject>Biological and medical sciences</subject><subject>Capsid - immunology</subject><subject>Epitopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>respiratory syncytial virus</subject><subject>Respiratory Syncytial Viruses - immunology</subject><subject>Techniques used in virology</subject><subject>Viral Core Proteins - immunology</subject><subject>Viral Fusion Proteins - immunology</subject><subject>Viral Matrix Proteins - immunology</subject><subject>Viral Proteins - immunology</subject><subject>Virology</subject><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQhyNEVZbCG4DkA0LikOL_jo9lobRSEYituFqO7ewaJXawk6LlPXhfHO1qxa2nkWe--Y2lr6peIXiJoJTvIcS4RgSJmjc1wjVBmD2pVohyVuMCPK1WJ-RZ9TznnxAiSpk4r84xpQJjuqr-fktu1ElPPgaggwXrXXmZySX_59CMHfgSQzR9DLoHV2HybbTeZfDRJ1dAC_RW-5AncO0fHNhMaTbTnAq7jsMYgwtTXkJu5kEH8N3l0ZdzMe3BZh_MfvKF_OHTnMFmbrcpziP48KI663Sf3ctjvajurz_dr2_qu6-fb9dXd7UhTLCaGCx0I5EzmkDKWmI7YZ20nGEjNOVSS04Jkx203GCOGtsZwSGjhEgrW3JRvT3Ejin-ml2e1OCzcX2vg4tzVkI0DZGIPQoi2nCEyQLSA2hSzDm5To3JDzrtFYJqsaYWJWpRonijEFaLtbL2-pg_t4Ozp6WjpjJ_c5zrbHTfJR2MzydMMC5Is8S8O2A7v939LnrU1oXBl7-0PqoHn_47-Q8-RrAY</recordid><startdate>198712</startdate><enddate>198712</enddate><creator>Orvell, Claes</creator><creator>Norrby, Erling</creator><creator>Mufson, Maurice A</creator><general>Soc General Microbiol</general><general>Society for General Microbiology</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>7T5</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>198712</creationdate><title>Preparation and Characterization of Monoclonal Antibodies Directed against Five Structural Components of Human Respiratory Syncytial Virus Subgroup B</title><author>Orvell, Claes ; Norrby, Erling ; Mufson, Maurice A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3575-3c27a891eca3045b3df7de9d652c7a469a964359f0d6c2618dfc76054339d9b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Viral - immunology</topic><topic>Antibody Specificity</topic><topic>Antigens, Viral - immunology</topic><topic>Biological and medical sciences</topic><topic>Capsid - immunology</topic><topic>Epitopes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>respiratory syncytial virus</topic><topic>Respiratory Syncytial Viruses - immunology</topic><topic>Techniques used in virology</topic><topic>Viral Core Proteins - immunology</topic><topic>Viral Fusion Proteins - immunology</topic><topic>Viral Matrix Proteins - immunology</topic><topic>Viral Proteins - immunology</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Orvell, Claes</creatorcontrib><creatorcontrib>Norrby, Erling</creatorcontrib><creatorcontrib>Mufson, Maurice A</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>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of general virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Orvell, Claes</au><au>Norrby, Erling</au><au>Mufson, Maurice A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and Characterization of Monoclonal Antibodies Directed against Five Structural Components of Human Respiratory Syncytial Virus Subgroup B</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>1987-12</date><risdate>1987</risdate><volume>68</volume><issue>12</issue><spage>3125</spage><epage>3135</epage><pages>3125-3135</pages><issn>0022-1317</issn><eissn>1465-2099</eissn><coden>JGVIAY</coden><abstract>1 Department of Virology, National Bacteriological Laboratory, S-105 21 Stockholm,
2 Department of Virology, Karolinska Institute, S-105 21 Stockholm, Sweden
and 3 Department of Medicine, Marshall University School of Medicine and Veterans Administration Medical Center, Huntington, West Virginia, U.S.A.
Mouse hybridomas producing antibodies against the structural proteins of strain WV4843, a subgroup B strain of respiratory syncytial (RS) virus, were produced by fusion of Sp2/0 myeloma cells with spleen cells from BALB/c mice immunized with purified preparations of the virus. After immunoprecipitation tests with [ 35 S]methionine-labelled extracellular virions, 35 clones found to produce antibodies against the fusion (F) protein, six against the membrane (M) protein, 21 against the nucleocapsid (NP) and eight against the phospho- (P) protein were further characterized. Immunoprecipitation with [ 3 H]glucosamine-labelled intracellular virus polypeptides detected nine hybridoma cell lines producing antibodies against the large glyco- (G) protein of the virus. By competitive binding ELISA tests with monoclonal antibodies against each of the structural components, a minimum of two, 24, four, 15 and three epitopes were detected on the G, F, M, NP and P proteins, respectively. Eleven monoclonal antibodies directed against nine epitopes of the F protein could neutralize the infectivity of the virus. In contrast, none of the nine monoclonal antibodies against G could neutralize the infectivity of the virus. In order to find out more about the antigenic relationship between human and bovine RS virus strains all monoclonal antibodies were reacted with subgroup A RS virus and also with three different strains of bovine RS virus and one strain of caprine RS virus in immunofluorescence, ELISA and immunoprecipitation tests. In addition, 31 previously developed monoclonal antibodies against subgroup A virus were reacted with the bovine and caprine strains. The numbers of monoclonal antibodies of subgroup B specific for the B type of the two human subgroups were 9/9, 3/35, 0/6, 0/21, 0/8, for the G, F, M, NP and P proteins, respectively. No antigenic variations were found between the three bovine strains and the caprine strain. They did not react with the nine monoclonal antibodies against the G protein of subgroup B, nor did they react with nine monoclonal antibodies against subgroup A. Most but not all of the monoclonal antibodies against the other structural proteins of the two human RS virus subgroups reacted with the four strains. All 11 monoclonal antibodies against the F protein of subgroup B that could neutralize the infectivity of subgroup B also reacted with the bovine strains and neutralized their infectivity. It is concluded that although the bovine strains share many epitopes with the two human subgroups, they are antigenically distinct from the human viruses.
Keywords: respiratory syncytial virus, structural proteins, monoclonal antibodies
Received 23 April 1987;
accepted 29 July 1987.</abstract><cop>Reading</cop><pub>Soc General Microbiol</pub><pmid>2447224</pmid><doi>10.1099/0022-1317-68-12-3125</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Microbiology Society; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Antibodies, Monoclonal - immunology Antibodies, Viral - immunology Antibody Specificity Antigens, Viral - immunology Biological and medical sciences Capsid - immunology Epitopes Fundamental and applied biological sciences. Psychology Microbiology respiratory syncytial virus Respiratory Syncytial Viruses - immunology Techniques used in virology Viral Core Proteins - immunology Viral Fusion Proteins - immunology Viral Matrix Proteins - immunology Viral Proteins - immunology Virology |
| title | Preparation and Characterization of Monoclonal Antibodies Directed against Five Structural Components of Human Respiratory Syncytial Virus Subgroup B |
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