Babesia bovis : identification of immunodominant merozoite surface proteins in soluble culture-derived exoantigen
Babesia bovis merozoite proteins presenting as exoantigens in in vitro culture supernatants have been characterized. Bovine antisera to B. bovis exoantigens were used to immunoprecipitate [35S]-methionine metabolically labeled or lactoperoxidase-catalyzed radioiodinated B. bovis merozoite proteins....
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| Veröffentlicht in: | Parasitology research (1987) 1997, Vol.83 (8), p.776-780 |
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| container_title | Parasitology research (1987) |
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| creator | JOHNSON, W. C PERRYMAN, L. E GOFF, W. L |
| description | Babesia bovis merozoite proteins presenting as exoantigens in in vitro culture supernatants have been characterized. Bovine antisera to B. bovis exoantigens were used to immunoprecipitate [35S]-methionine metabolically labeled or lactoperoxidase-catalyzed radioiodinated B. bovis merozoite proteins. A total of 24 metabolically labeled proteins ranging in molecular weight from 24,000 to 225,000 Da and 9 radioiodinated proteins with molecular weights varying between 24,000 and 225,000 Da were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Monoclonal antibodies to B. bovis merozoite surface proteins were also used to immunoprecipitate metabolically labeled exoantigens directly from in vitro culture supernatants. These results demonstrate epitopes from at least nine merozoite surface proteins present in the exoantigen fraction, among which are the recently characterized major surface antigens 1 and 2, rhoptry-associated protein 1, and spherical body protein 2. |
| doi_str_mv | 10.1007/s004360050338 |
| format | Article |
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These results demonstrate epitopes from at least nine merozoite surface proteins present in the exoantigen fraction, among which are the recently characterized major surface antigens 1 and 2, rhoptry-associated protein 1, and spherical body protein 2.</description><identifier>ISSN: 0932-0113</identifier><identifier>EISSN: 1432-1955</identifier><identifier>DOI: 10.1007/s004360050338</identifier><identifier>PMID: 9342742</identifier><identifier>CODEN: PARREZ</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Animals ; Antibodies, Protozoan - blood ; Antibodies, Protozoan - immunology ; Antigens, Protozoan - chemistry ; Antigens, Protozoan - immunology ; Antigens, Surface - chemistry ; Antigens, Surface - immunology ; Babesia bovis - immunology ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; Cattle ; Fluorescent Antibody Technique, Indirect ; Fundamental and applied biological sciences. 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C</creatorcontrib><creatorcontrib>PERRYMAN, L. E</creatorcontrib><creatorcontrib>GOFF, W. L</creatorcontrib><title>Babesia bovis : identification of immunodominant merozoite surface proteins in soluble culture-derived exoantigen</title><title>Parasitology research (1987)</title><addtitle>Parasitol Res</addtitle><description>Babesia bovis merozoite proteins presenting as exoantigens in in vitro culture supernatants have been characterized. Bovine antisera to B. bovis exoantigens were used to immunoprecipitate [35S]-methionine metabolically labeled or lactoperoxidase-catalyzed radioiodinated B. bovis merozoite proteins. A total of 24 metabolically labeled proteins ranging in molecular weight from 24,000 to 225,000 Da and 9 radioiodinated proteins with molecular weights varying between 24,000 and 225,000 Da were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Monoclonal antibodies to B. bovis merozoite surface proteins were also used to immunoprecipitate metabolically labeled exoantigens directly from in vitro culture supernatants. These results demonstrate epitopes from at least nine merozoite surface proteins present in the exoantigen fraction, among which are the recently characterized major surface antigens 1 and 2, rhoptry-associated protein 1, and spherical body protein 2.</description><subject>Animals</subject><subject>Antibodies, Protozoan - blood</subject><subject>Antibodies, Protozoan - immunology</subject><subject>Antigens, Protozoan - chemistry</subject><subject>Antigens, Protozoan - immunology</subject><subject>Antigens, Surface - chemistry</subject><subject>Antigens, Surface - immunology</subject><subject>Babesia bovis - immunology</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Fluorescent Antibody Technique, Indirect</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunodominant Epitopes - chemistry</subject><subject>Immunodominant Epitopes - immunology</subject><subject>Precipitin Tests</subject><subject>Protozoa</subject><subject>Solubility</subject><issn>0932-0113</issn><issn>1432-1955</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkEtLxDAUhYMoOj6WLoUsxF01z7Zxp-ILBDfuSx43EmmTmaQd1F9vZQbB1b1wvnu45yB0SsklJaS5KoQIXhMiCeftDlpQwVlFlZS7aEHUvBNK-QE6LOWDENrUQuyjfcUFawRboNWtNlCCxiatQ8HXODiIY_DB6jGkiJPHYRimmFwaQtRxxAPk9J3CCLhM2WsLeJnTCCEWHCIuqZ9MD9hO_ThlqBzksAaH4TPNx-Ed4jHa87ovcLKdR-jt4f7t7ql6eX18vrt5qSxv-Vg1TlglhfA1MMoaoxUIaUxLfWtVq6RTrGGacFPPwSkVwHktnBFKO01qz4_QxcZ2_m41QRm7IRQLfa8jpKl0jeKSScpmsNqANqdSMvhumcOg81dHSffbcPev4Zk_2xpPZgD3R28rnfXzra6L1b3POtpQ_jDWSk5kw38Al3-Efw</recordid><startdate>1997</startdate><enddate>1997</enddate><creator>JOHNSON, W. C</creator><creator>PERRYMAN, L. 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L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c383t-7d4c9544f6e2127ba9e45bb81f8c9895d9272a03b6503114e3364db49ada06f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Antibodies, Protozoan - blood</topic><topic>Antibodies, Protozoan - immunology</topic><topic>Antigens, Protozoan - chemistry</topic><topic>Antigens, Protozoan - immunology</topic><topic>Antigens, Surface - chemistry</topic><topic>Antigens, Surface - immunology</topic><topic>Babesia bovis - immunology</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Fluorescent Antibody Technique, Indirect</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunodominant Epitopes - chemistry</topic><topic>Immunodominant Epitopes - immunology</topic><topic>Precipitin Tests</topic><topic>Protozoa</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>JOHNSON, W. C</creatorcontrib><creatorcontrib>PERRYMAN, L. E</creatorcontrib><creatorcontrib>GOFF, W. L</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>MEDLINE - Academic</collection><jtitle>Parasitology research (1987)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>JOHNSON, W. C</au><au>PERRYMAN, L. E</au><au>GOFF, W. L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Babesia bovis : identification of immunodominant merozoite surface proteins in soluble culture-derived exoantigen</atitle><jtitle>Parasitology research (1987)</jtitle><addtitle>Parasitol Res</addtitle><date>1997</date><risdate>1997</risdate><volume>83</volume><issue>8</issue><spage>776</spage><epage>780</epage><pages>776-780</pages><issn>0932-0113</issn><eissn>1432-1955</eissn><coden>PARREZ</coden><abstract>Babesia bovis merozoite proteins presenting as exoantigens in in vitro culture supernatants have been characterized. Bovine antisera to B. bovis exoantigens were used to immunoprecipitate [35S]-methionine metabolically labeled or lactoperoxidase-catalyzed radioiodinated B. bovis merozoite proteins. A total of 24 metabolically labeled proteins ranging in molecular weight from 24,000 to 225,000 Da and 9 radioiodinated proteins with molecular weights varying between 24,000 and 225,000 Da were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Monoclonal antibodies to B. bovis merozoite surface proteins were also used to immunoprecipitate metabolically labeled exoantigens directly from in vitro culture supernatants. These results demonstrate epitopes from at least nine merozoite surface proteins present in the exoantigen fraction, among which are the recently characterized major surface antigens 1 and 2, rhoptry-associated protein 1, and spherical body protein 2.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>9342742</pmid><doi>10.1007/s004360050338</doi><tpages>5</tpages></addata></record> |
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| ispartof | Parasitology research (1987), 1997, Vol.83 (8), p.776-780 |
| issn | 0932-0113 1432-1955 |
| language | eng |
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| subjects | Animals Antibodies, Protozoan - blood Antibodies, Protozoan - immunology Antigens, Protozoan - chemistry Antigens, Protozoan - immunology Antigens, Surface - chemistry Antigens, Surface - immunology Babesia bovis - immunology Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Cattle Fluorescent Antibody Technique, Indirect Fundamental and applied biological sciences. Psychology Immunodominant Epitopes - chemistry Immunodominant Epitopes - immunology Precipitin Tests Protozoa Solubility |
| title | Babesia bovis : identification of immunodominant merozoite surface proteins in soluble culture-derived exoantigen |
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