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Monoclonal antibodies to Mycoplasma gallisepticum membrane proteins
Monoclonal antibodies (MAbs) were prepared to study the immunogenesis of Mycoplasma gallisepticum. Balb/c mice were immunized with M. gallisepticum immunostimulating complexes and the supernatant of heterokaryotes screened with M. gallisepticum and closely related M. synoviae as antigens in indirect...
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| Published in: | Avian diseases 1993-07, Vol.37 (3), p.689-696 |
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| Main Authors: | , , , |
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| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c324t-99485b76740221883868566061d98e30df6fdd307271e8089096c47151464d763 |
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| container_end_page | 696 |
| container_issue | 3 |
| container_start_page | 689 |
| container_title | Avian diseases |
| container_volume | 37 |
| creator | Czifra, G Tuboly, T Sundquist, B.G Stipkovits, L |
| description | Monoclonal antibodies (MAbs) were prepared to study the immunogenesis of Mycoplasma gallisepticum. Balb/c mice were immunized with M. gallisepticum immunostimulating complexes and the supernatant of heterokaryotes screened with M. gallisepticum and closely related M. synoviae as antigens in indirect enzyme-linked immunosorbent assay. All selected MAbs proved to be M. gallisepticum species-specific when they were tested against 10 different avian Mycoplasma species. After immunoblotting analysis, five polypeptides were identified with estimated molecular weights of 110,000, 66,000, 64,000, 56,000, and 50,000. Cell membrane localization of the recognized polypeptides was studied by immunoelectron microscopy. None of the MAbs inhibited the hemagglutinating activity of freshly prepared M. gallisepticum. However, one MAb (B3) specific for p56 agglutinated the stained M. gallisepticum antigen in the slide agglutination test. Results seemed to correlate with published information on the protein composition and agglutinating activity of Mycoplasma gallisepticum |
| doi_str_mv | 10.2307/1592016 |
| format | article |
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Balb/c mice were immunized with M. gallisepticum immunostimulating complexes and the supernatant of heterokaryotes screened with M. gallisepticum and closely related M. synoviae as antigens in indirect enzyme-linked immunosorbent assay. All selected MAbs proved to be M. gallisepticum species-specific when they were tested against 10 different avian Mycoplasma species. After immunoblotting analysis, five polypeptides were identified with estimated molecular weights of 110,000, 66,000, 64,000, 56,000, and 50,000. Cell membrane localization of the recognized polypeptides was studied by immunoelectron microscopy. None of the MAbs inhibited the hemagglutinating activity of freshly prepared M. gallisepticum. However, one MAb (B3) specific for p56 agglutinated the stained M. gallisepticum antigen in the slide agglutination test. Results seemed to correlate with published information on the protein composition and agglutinating activity of Mycoplasma gallisepticum</description><identifier>ISSN: 0005-2086</identifier><identifier>EISSN: 1938-4351</identifier><identifier>DOI: 10.2307/1592016</identifier><identifier>PMID: 8257358</identifier><language>eng</language><publisher>United States: American Association of Avian Pathologists, Inc</publisher><subject>Animals ; Antibodies ; Antibodies, Bacterial ; Antibodies, Monoclonal ; ANTICORPS MONOCLONAL ; ANTICUERPOS MONOCLONALES ; ANTIGENE ; ANTIGENOS ; Antigens ; Bacterial Proteins - chemistry ; Bacterial Proteins - immunology ; Bacterial Proteins - isolation & purification ; Cellulose nitrate ; Chickens ; Enzyme linked immunosorbent assay ; Immunization ; Immuno stimulating complex ; Immunoblotting ; IMMUNOSTIMULATION ; INMUNOESTIMULACION ; ISCOMs - immunology ; MEMBRANAS CELULARES ; MEMBRANE CELLULAIRE ; Membrane Proteins - chemistry ; Membrane Proteins - immunology ; Membrane Proteins - isolation & purification ; Mice ; Mice, Inbred BALB C ; Molecular Weight ; Mycoplasma ; Mycoplasma - immunology ; MYCOPLASMA GALLISEPTICUM ; RATON ; SOURIS ; Species Specificity</subject><ispartof>Avian diseases, 1993-07, Vol.37 (3), p.689-696</ispartof><rights>Copyright 1993 The American Association of Avian Pathologists, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c324t-99485b76740221883868566061d98e30df6fdd307271e8089096c47151464d763</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/1592016$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/1592016$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,58238,58471</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8257358$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Czifra, G</creatorcontrib><creatorcontrib>Tuboly, T</creatorcontrib><creatorcontrib>Sundquist, B.G</creatorcontrib><creatorcontrib>Stipkovits, L</creatorcontrib><title>Monoclonal antibodies to Mycoplasma gallisepticum membrane proteins</title><title>Avian diseases</title><addtitle>Avian Dis</addtitle><description>Monoclonal antibodies (MAbs) were prepared to study the immunogenesis of Mycoplasma gallisepticum. Balb/c mice were immunized with M. gallisepticum immunostimulating complexes and the supernatant of heterokaryotes screened with M. gallisepticum and closely related M. synoviae as antigens in indirect enzyme-linked immunosorbent assay. All selected MAbs proved to be M. gallisepticum species-specific when they were tested against 10 different avian Mycoplasma species. After immunoblotting analysis, five polypeptides were identified with estimated molecular weights of 110,000, 66,000, 64,000, 56,000, and 50,000. Cell membrane localization of the recognized polypeptides was studied by immunoelectron microscopy. None of the MAbs inhibited the hemagglutinating activity of freshly prepared M. gallisepticum. However, one MAb (B3) specific for p56 agglutinated the stained M. gallisepticum antigen in the slide agglutination test. Results seemed to correlate with published information on the protein composition and agglutinating activity of Mycoplasma gallisepticum</description><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Bacterial</subject><subject>Antibodies, Monoclonal</subject><subject>ANTICORPS MONOCLONAL</subject><subject>ANTICUERPOS MONOCLONALES</subject><subject>ANTIGENE</subject><subject>ANTIGENOS</subject><subject>Antigens</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - immunology</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Cellulose nitrate</subject><subject>Chickens</subject><subject>Enzyme linked immunosorbent assay</subject><subject>Immunization</subject><subject>Immuno stimulating complex</subject><subject>Immunoblotting</subject><subject>IMMUNOSTIMULATION</subject><subject>INMUNOESTIMULACION</subject><subject>ISCOMs - immunology</subject><subject>MEMBRANAS CELULARES</subject><subject>MEMBRANE CELLULAIRE</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - immunology</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Molecular Weight</subject><subject>Mycoplasma</subject><subject>Mycoplasma - immunology</subject><subject>MYCOPLASMA GALLISEPTICUM</subject><subject>RATON</subject><subject>SOURIS</subject><subject>Species Specificity</subject><issn>0005-2086</issn><issn>1938-4351</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><recordid>eNp9kD1LxEAQhhdRzvMUe0FIIVpFZ7PfpRx-wR0WevWySTbHyiYbs0lx_95IgqXVFO_DMzMvQpcY7jMC4gEzlQHmR2iJFZEpJQwfoyUAsDQDyU_RWYxfAFgoDgu0kBkThMklWm9DEwofGuMT0_QuD6WzMelDsj0UofUm1ibZG-9dtG3viqFOalvnnWls0naht66J5-ikMj7ai3mu0O756XP9mm7eX97Wj5u0IBntU6WoZLnggkKWYSmJ5JJxDhyXSloCZcWrshyfyQS2EqQCxQsqMMOU01JwskK3k3dc_D3Y2OvaxcJ6Px4ThqgFBwVcsBG8m8CiCzF2ttJt52rTHTQG_VuXnusayetZOeS1Lf-4uZ8xv5nyr9iH7h_N1YRVJmiz71zUuw_FMAjKyQ9xFXWS</recordid><startdate>19930701</startdate><enddate>19930701</enddate><creator>Czifra, G</creator><creator>Tuboly, T</creator><creator>Sundquist, B.G</creator><creator>Stipkovits, L</creator><general>American Association of Avian Pathologists, Inc</general><scope>FBQ</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>19930701</creationdate><title>Monoclonal antibodies to Mycoplasma gallisepticum membrane proteins</title><author>Czifra, G ; Tuboly, T ; Sundquist, B.G ; Stipkovits, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c324t-99485b76740221883868566061d98e30df6fdd307271e8089096c47151464d763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Bacterial</topic><topic>Antibodies, Monoclonal</topic><topic>ANTICORPS MONOCLONAL</topic><topic>ANTICUERPOS MONOCLONALES</topic><topic>ANTIGENE</topic><topic>ANTIGENOS</topic><topic>Antigens</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - immunology</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Cellulose nitrate</topic><topic>Chickens</topic><topic>Enzyme linked immunosorbent assay</topic><topic>Immunization</topic><topic>Immuno stimulating complex</topic><topic>Immunoblotting</topic><topic>IMMUNOSTIMULATION</topic><topic>INMUNOESTIMULACION</topic><topic>ISCOMs - immunology</topic><topic>MEMBRANAS CELULARES</topic><topic>MEMBRANE CELLULAIRE</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - immunology</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Molecular Weight</topic><topic>Mycoplasma</topic><topic>Mycoplasma - immunology</topic><topic>MYCOPLASMA GALLISEPTICUM</topic><topic>RATON</topic><topic>SOURIS</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Czifra, G</creatorcontrib><creatorcontrib>Tuboly, T</creatorcontrib><creatorcontrib>Sundquist, B.G</creatorcontrib><creatorcontrib>Stipkovits, L</creatorcontrib><collection>AGRIS</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>Avian diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Czifra, G</au><au>Tuboly, T</au><au>Sundquist, B.G</au><au>Stipkovits, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoclonal antibodies to Mycoplasma gallisepticum membrane proteins</atitle><jtitle>Avian diseases</jtitle><addtitle>Avian Dis</addtitle><date>1993-07-01</date><risdate>1993</risdate><volume>37</volume><issue>3</issue><spage>689</spage><epage>696</epage><pages>689-696</pages><issn>0005-2086</issn><eissn>1938-4351</eissn><abstract>Monoclonal antibodies (MAbs) were prepared to study the immunogenesis of Mycoplasma gallisepticum. Balb/c mice were immunized with M. gallisepticum immunostimulating complexes and the supernatant of heterokaryotes screened with M. gallisepticum and closely related M. synoviae as antigens in indirect enzyme-linked immunosorbent assay. All selected MAbs proved to be M. gallisepticum species-specific when they were tested against 10 different avian Mycoplasma species. After immunoblotting analysis, five polypeptides were identified with estimated molecular weights of 110,000, 66,000, 64,000, 56,000, and 50,000. Cell membrane localization of the recognized polypeptides was studied by immunoelectron microscopy. None of the MAbs inhibited the hemagglutinating activity of freshly prepared M. gallisepticum. However, one MAb (B3) specific for p56 agglutinated the stained M. gallisepticum antigen in the slide agglutination test. Results seemed to correlate with published information on the protein composition and agglutinating activity of Mycoplasma gallisepticum</abstract><cop>United States</cop><pub>American Association of Avian Pathologists, Inc</pub><pmid>8257358</pmid><doi>10.2307/1592016</doi><tpages>8</tpages></addata></record> |
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| ispartof | Avian diseases, 1993-07, Vol.37 (3), p.689-696 |
| issn | 0005-2086 1938-4351 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76090675 |
| source | JSTOR Archival Journals and Primary Sources Collection |
| subjects | Animals Antibodies Antibodies, Bacterial Antibodies, Monoclonal ANTICORPS MONOCLONAL ANTICUERPOS MONOCLONALES ANTIGENE ANTIGENOS Antigens Bacterial Proteins - chemistry Bacterial Proteins - immunology Bacterial Proteins - isolation & purification Cellulose nitrate Chickens Enzyme linked immunosorbent assay Immunization Immuno stimulating complex Immunoblotting IMMUNOSTIMULATION INMUNOESTIMULACION ISCOMs - immunology MEMBRANAS CELULARES MEMBRANE CELLULAIRE Membrane Proteins - chemistry Membrane Proteins - immunology Membrane Proteins - isolation & purification Mice Mice, Inbred BALB C Molecular Weight Mycoplasma Mycoplasma - immunology MYCOPLASMA GALLISEPTICUM RATON SOURIS Species Specificity |
| title | Monoclonal antibodies to Mycoplasma gallisepticum membrane proteins |
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