Protein changes in bovine lymphoblastoid cells induced by infection with the intracellular parasite Theileria parva
Protein and glycoprotein changes induced in bovine lymphoblasts by infection with Theileria parva were analyzed by high-resolution two-dimensional gel electrophoresis. Uninfected and infected cloned bovine T and B lymphoblasts were biosynthetically labeled with [ 35S]methionine and their two-dimensi...
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Veröffentlicht in: | Molecular and biochemical parasitology 1989-12, Vol.37 (2), p.159-169 |
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container_title | Molecular and biochemical parasitology |
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creator | Sugimoto, Chihiro Mutharia, Lucy M. Conrad, Patricia A. Dolan, Thomas T. Brown, Wendy C. Goddeeris, Bruno M. Pearson, Terry W. |
description | Protein and glycoprotein changes induced in bovine lymphoblasts by infection with
Theileria parva were analyzed by high-resolution two-dimensional gel electrophoresis. Uninfected and infected cloned bovine T and B lymphoblasts were biosynthetically labeled with [
35S]methionine and their two-dimensional autoradiographic patterns were compared with each other and with the pattern obtained using purified labeled schizonts. Ten proteins were found in infected cells which were not present in uninfected cells, and seven of these were detected in preparations of purified schizonts. Four glycoproteins were detected on the surface of infected cells labeled with [
3H]borohydride while a major glycoprotein present on uninfected cells disappeared or was reduced in infected cells. Other minor changes in protein and glycoprotein patterns were also observed. |
doi_str_mv | 10.1016/0166-6851(89)90148-5 |
format | Article |
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Theileria parva were analyzed by high-resolution two-dimensional gel electrophoresis. Uninfected and infected cloned bovine T and B lymphoblasts were biosynthetically labeled with [
35S]methionine and their two-dimensional autoradiographic patterns were compared with each other and with the pattern obtained using purified labeled schizonts. Ten proteins were found in infected cells which were not present in uninfected cells, and seven of these were detected in preparations of purified schizonts. Four glycoproteins were detected on the surface of infected cells labeled with [
3H]borohydride while a major glycoprotein present on uninfected cells disappeared or was reduced in infected cells. Other minor changes in protein and glycoprotein patterns were also observed.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/0166-6851(89)90148-5</identifier><identifier>PMID: 2514355</identifier><identifier>CODEN: MBIPDP</identifier><language>eng</language><publisher>Shannon: Elsevier B.V</publisher><subject>Animals ; Apicomplexa - metabolism ; Apicomplexa - physiology ; B-Lymphocytes - analysis ; B-Lymphocytes - parasitology ; Biological and medical sciences ; Cattle ; Cell Line ; cells ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; glycoproteins ; Life cycle. Host-agent relationship. Pathogenesis ; lymphoblasts ; Membrane Glycoproteins - analysis ; Membrane Proteins - analysis ; Methionine - analysis ; proteins ; Protozoa ; Protozoan Proteins - analysis ; Schizont ; Surface glycoprotein ; Surface protein ; T lymphoblast ; T-Lymphocytes - analysis ; T-Lymphocytes - parasitology ; Theileria parva ; Theileriasis - parasitology ; Two-dimensional gel electrophoresis</subject><ispartof>Molecular and biochemical parasitology, 1989-12, Vol.37 (2), p.159-169</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-fbf32f7f779f1d1eff525f8a7bf694ce896725ab6efa8618b41f2dc3d541ca1b3</citedby><cites>FETCH-LOGICAL-c441t-fbf32f7f779f1d1eff525f8a7bf694ce896725ab6efa8618b41f2dc3d541ca1b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0166-6851(89)90148-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6675012$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2514355$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sugimoto, Chihiro</creatorcontrib><creatorcontrib>Mutharia, Lucy M.</creatorcontrib><creatorcontrib>Conrad, Patricia A.</creatorcontrib><creatorcontrib>Dolan, Thomas T.</creatorcontrib><creatorcontrib>Brown, Wendy C.</creatorcontrib><creatorcontrib>Goddeeris, Bruno M.</creatorcontrib><creatorcontrib>Pearson, Terry W.</creatorcontrib><title>Protein changes in bovine lymphoblastoid cells induced by infection with the intracellular parasite Theileria parva</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>Protein and glycoprotein changes induced in bovine lymphoblasts by infection with
Theileria parva were analyzed by high-resolution two-dimensional gel electrophoresis. Uninfected and infected cloned bovine T and B lymphoblasts were biosynthetically labeled with [
35S]methionine and their two-dimensional autoradiographic patterns were compared with each other and with the pattern obtained using purified labeled schizonts. Ten proteins were found in infected cells which were not present in uninfected cells, and seven of these were detected in preparations of purified schizonts. Four glycoproteins were detected on the surface of infected cells labeled with [
3H]borohydride while a major glycoprotein present on uninfected cells disappeared or was reduced in infected cells. Other minor changes in protein and glycoprotein patterns were also observed.</description><subject>Animals</subject><subject>Apicomplexa - metabolism</subject><subject>Apicomplexa - physiology</subject><subject>B-Lymphocytes - analysis</subject><subject>B-Lymphocytes - parasitology</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cell Line</subject><subject>cells</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>glycoproteins</subject><subject>Life cycle. Host-agent relationship. Pathogenesis</subject><subject>lymphoblasts</subject><subject>Membrane Glycoproteins - analysis</subject><subject>Membrane Proteins - analysis</subject><subject>Methionine - analysis</subject><subject>proteins</subject><subject>Protozoa</subject><subject>Protozoan Proteins - analysis</subject><subject>Schizont</subject><subject>Surface glycoprotein</subject><subject>Surface protein</subject><subject>T lymphoblast</subject><subject>T-Lymphocytes - analysis</subject><subject>T-Lymphocytes - parasitology</subject><subject>Theileria parva</subject><subject>Theileriasis - parasitology</subject><subject>Two-dimensional gel electrophoresis</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2LFDEQhoMo67j6DxT7IKKH1iSdr74syOIXLCi4ew7V6cp2pKczJt0j8-9NO8Mc9RBS1PvUB_US8pzRd4wy9b48VSsj2RvTvm0pE6aWD8iGGc3rVnDzkGzOyGPyJOeflFKplbogF1wy0Ui5Ifl7ijOGqXIDTPeYqxJ2cR8mrMbDdjfEboQ8x9BXDsdxlfvFYV91hxJ6dHOIU_U7zEM1D1hSc4IVXEZI1Q4S5DBjdTtgGDEFWFN7eEoeeRgzPjv9l-Tu08fb6y_1zbfPX68_3NROCDbXvvMN99pr3XrWM_RecukN6M6rVjg0rdJcQqfQg1HMdIJ53ruml4I5YF1zSV4f--5S_LVgnu025HU7mDAu2epWsJZS_V-QSUU55byA4gi6FHNO6O0uhS2kg2XUrqbY9eJ2vbg1rf1ripWl7MWp_9JtsT8XnVwo-quTDtnB6BNMLuQzppSWlK3TXx4xD9HCfSrI3Q9OWUO5Mg2VrBBXRwLLWfcBk80u4FQMC6l4ZfsY_r3pH7sds_M</recordid><startdate>19891201</startdate><enddate>19891201</enddate><creator>Sugimoto, Chihiro</creator><creator>Mutharia, Lucy M.</creator><creator>Conrad, Patricia A.</creator><creator>Dolan, Thomas T.</creator><creator>Brown, Wendy C.</creator><creator>Goddeeris, Bruno M.</creator><creator>Pearson, Terry W.</creator><general>Elsevier B.V</general><general>Elsevier Science</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>19891201</creationdate><title>Protein changes in bovine lymphoblastoid cells induced by infection with the intracellular parasite Theileria parva</title><author>Sugimoto, Chihiro ; Mutharia, Lucy M. ; Conrad, Patricia A. ; Dolan, Thomas T. ; Brown, Wendy C. ; Goddeeris, Bruno M. ; Pearson, Terry W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441t-fbf32f7f779f1d1eff525f8a7bf694ce896725ab6efa8618b41f2dc3d541ca1b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>Apicomplexa - metabolism</topic><topic>Apicomplexa - physiology</topic><topic>B-Lymphocytes - analysis</topic><topic>B-Lymphocytes - parasitology</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cell Line</topic><topic>cells</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>glycoproteins</topic><topic>Life cycle. Host-agent relationship. Pathogenesis</topic><topic>lymphoblasts</topic><topic>Membrane Glycoproteins - analysis</topic><topic>Membrane Proteins - analysis</topic><topic>Methionine - analysis</topic><topic>proteins</topic><topic>Protozoa</topic><topic>Protozoan Proteins - analysis</topic><topic>Schizont</topic><topic>Surface glycoprotein</topic><topic>Surface protein</topic><topic>T lymphoblast</topic><topic>T-Lymphocytes - analysis</topic><topic>T-Lymphocytes - parasitology</topic><topic>Theileria parva</topic><topic>Theileriasis - parasitology</topic><topic>Two-dimensional gel electrophoresis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sugimoto, Chihiro</creatorcontrib><creatorcontrib>Mutharia, Lucy M.</creatorcontrib><creatorcontrib>Conrad, Patricia A.</creatorcontrib><creatorcontrib>Dolan, Thomas T.</creatorcontrib><creatorcontrib>Brown, Wendy C.</creatorcontrib><creatorcontrib>Goddeeris, Bruno M.</creatorcontrib><creatorcontrib>Pearson, Terry W.</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sugimoto, Chihiro</au><au>Mutharia, Lucy M.</au><au>Conrad, Patricia A.</au><au>Dolan, Thomas T.</au><au>Brown, Wendy C.</au><au>Goddeeris, Bruno M.</au><au>Pearson, Terry W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein changes in bovine lymphoblastoid cells induced by infection with the intracellular parasite Theileria parva</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1989-12-01</date><risdate>1989</risdate><volume>37</volume><issue>2</issue><spage>159</spage><epage>169</epage><pages>159-169</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><coden>MBIPDP</coden><abstract>Protein and glycoprotein changes induced in bovine lymphoblasts by infection with
Theileria parva were analyzed by high-resolution two-dimensional gel electrophoresis. Uninfected and infected cloned bovine T and B lymphoblasts were biosynthetically labeled with [
35S]methionine and their two-dimensional autoradiographic patterns were compared with each other and with the pattern obtained using purified labeled schizonts. Ten proteins were found in infected cells which were not present in uninfected cells, and seven of these were detected in preparations of purified schizonts. Four glycoproteins were detected on the surface of infected cells labeled with [
3H]borohydride while a major glycoprotein present on uninfected cells disappeared or was reduced in infected cells. Other minor changes in protein and glycoprotein patterns were also observed.</abstract><cop>Shannon</cop><pub>Elsevier B.V</pub><pmid>2514355</pmid><doi>10.1016/0166-6851(89)90148-5</doi><tpages>11</tpages></addata></record> |
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subjects | Animals Apicomplexa - metabolism Apicomplexa - physiology B-Lymphocytes - analysis B-Lymphocytes - parasitology Biological and medical sciences Cattle Cell Line cells Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology glycoproteins Life cycle. Host-agent relationship. Pathogenesis lymphoblasts Membrane Glycoproteins - analysis Membrane Proteins - analysis Methionine - analysis proteins Protozoa Protozoan Proteins - analysis Schizont Surface glycoprotein Surface protein T lymphoblast T-Lymphocytes - analysis T-Lymphocytes - parasitology Theileria parva Theileriasis - parasitology Two-dimensional gel electrophoresis |
title | Protein changes in bovine lymphoblastoid cells induced by infection with the intracellular parasite Theileria parva |
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