Spectrin-like proteins in the paraflagellar rod structure of Trypanosoma brucei
A polyclonal, monospecific rabbit antibody to human erythrocyte spectrins cross-reacted with two sets of proteins (a doublet of 180/200K and a triplet of 67-66-65K; K = 10(3) Mr) in the parasitic protozoon Trypanosoma brucei brucei. Except for the 66K protein, the cross-reacting proteins are localiz...
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| Veröffentlicht in: | Journal of cell science 1988-06, Vol.90 (2), p.307-315 |
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| container_title | Journal of cell science |
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| creator | Schneider, A Lutz, H.U Marugg, R Gehr, P Seebeck, T |
| description | A polyclonal, monospecific rabbit antibody to human erythrocyte spectrins cross-reacted with two sets of proteins (a doublet of 180/200K and a triplet of 67-66-65K; K = 10(3) Mr) in the parasitic protozoon Trypanosoma brucei brucei. Except for the 66K protein, the cross-reacting proteins are localized in the flagellum, on the basis of evidence from cell fractionation and immunofluorescence microscopy. Immunogold labelling and electron micrographs further revealed that the spectrin-like proteins are confined to the paraflagellar rod structure. The spectrin-like proteins with apparent molecular weights of 180 and 200 share homology with spectrin band 1, since V8-protease from Staphylococcus aureus generated similarly sized, antigenic peptides from these proteins. The results indicate homology between the cross-reacting proteins and human red cell spectrin. |
| doi_str_mv | 10.1242/jcs.90.2.307 |
| format | Article |
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Except for the 66K protein, the cross-reacting proteins are localized in the flagellum, on the basis of evidence from cell fractionation and immunofluorescence microscopy. Immunogold labelling and electron micrographs further revealed that the spectrin-like proteins are confined to the paraflagellar rod structure. The spectrin-like proteins with apparent molecular weights of 180 and 200 share homology with spectrin band 1, since V8-protease from Staphylococcus aureus generated similarly sized, antigenic peptides from these proteins. The results indicate homology between the cross-reacting proteins and human red cell spectrin.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.90.2.307</identifier><identifier>PMID: 3073166</identifier><identifier>CODEN: JNCSAI</identifier><language>eng</language><publisher>Cambridge: Company of Biologists</publisher><subject>Animals ; antibodies ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; electron microscopy ; Fluorescent Antibody Technique ; Fundamental and applied biological sciences. Psychology ; Human protozoal diseases ; Immunoblotting ; immunochemistry ; Infectious diseases ; Medical sciences ; Parasitic diseases ; polypeptides ; proteins ; Protozoa ; Protozoal diseases ; Spectrin - analysis ; Tropical medicine ; Trypanosoma brucei ; Trypanosoma brucei brucei - analysis ; Trypanosomiasis</subject><ispartof>Journal of cell science, 1988-06, Vol.90 (2), p.307-315</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c373t-3b6de91b75e456814a18460e1050c6f53be2ea28105f393f1bc21c1d3eb4b3453</citedby><cites>FETCH-LOGICAL-c373t-3b6de91b75e456814a18460e1050c6f53be2ea28105f393f1bc21c1d3eb4b3453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3678,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7787966$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3073166$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schneider, A</creatorcontrib><creatorcontrib>Lutz, H.U</creatorcontrib><creatorcontrib>Marugg, R</creatorcontrib><creatorcontrib>Gehr, P</creatorcontrib><creatorcontrib>Seebeck, T</creatorcontrib><title>Spectrin-like proteins in the paraflagellar rod structure of Trypanosoma brucei</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>A polyclonal, monospecific rabbit antibody to human erythrocyte spectrins cross-reacted with two sets of proteins (a doublet of 180/200K and a triplet of 67-66-65K; K = 10(3) Mr) in the parasitic protozoon Trypanosoma brucei brucei. Except for the 66K protein, the cross-reacting proteins are localized in the flagellum, on the basis of evidence from cell fractionation and immunofluorescence microscopy. Immunogold labelling and electron micrographs further revealed that the spectrin-like proteins are confined to the paraflagellar rod structure. The spectrin-like proteins with apparent molecular weights of 180 and 200 share homology with spectrin band 1, since V8-protease from Staphylococcus aureus generated similarly sized, antigenic peptides from these proteins. The results indicate homology between the cross-reacting proteins and human red cell spectrin.</description><subject>Animals</subject><subject>antibodies</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>electron microscopy</subject><subject>Fluorescent Antibody Technique</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Human protozoal diseases</subject><subject>Immunoblotting</subject><subject>immunochemistry</subject><subject>Infectious diseases</subject><subject>Medical sciences</subject><subject>Parasitic diseases</subject><subject>polypeptides</subject><subject>proteins</subject><subject>Protozoa</subject><subject>Protozoal diseases</subject><subject>Spectrin - analysis</subject><subject>Tropical medicine</subject><subject>Trypanosoma brucei</subject><subject>Trypanosoma brucei brucei - analysis</subject><subject>Trypanosomiasis</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMtLw0AQxhdRaq3evIo5iCcT95Fks0cpvqDQQ9vzstnM1tS83E0O_e_d2CAMDDPz45uPD6FbgiNCY_p80C4SOKIRw_wMzUnMeSgI4-dojjEloUgYu0RXzh0wxpwKPkMzjzKSpnO03nSge1s2YVV-Q9DZtoeycUHZBP2Xn5VVplJ7qCplA9sWgevtoPvBQtCaYGuPnWpa19YqyP0eymt0YVTl4GbqC7R7e90uP8LV-v1z-bIKNeOsD1meFiBIzhOIkzQjsSJZnGIgOME6NQnLgYKimZ8NE8yQXFOiScEgj3MWJ2yBHk-63vHPAK6Xden0aLOBdnCSZzzxysKDTydQ29Y5C0Z2tqyVPUqC5Zif9PlJgSWVYygLdDfpDnkNxT88BebvD9NdOa0qY1WjS_ePcf9X_GH3J8yoVqq99chuQzFhmMRjpewXoUyBhw</recordid><startdate>19880601</startdate><enddate>19880601</enddate><creator>Schneider, A</creator><creator>Lutz, H.U</creator><creator>Marugg, R</creator><creator>Gehr, P</creator><creator>Seebeck, T</creator><general>Company of Biologists</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>19880601</creationdate><title>Spectrin-like proteins in the paraflagellar rod structure of Trypanosoma brucei</title><author>Schneider, A ; Lutz, H.U ; Marugg, R ; Gehr, P ; Seebeck, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c373t-3b6de91b75e456814a18460e1050c6f53be2ea28105f393f1bc21c1d3eb4b3453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Animals</topic><topic>antibodies</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>electron microscopy</topic><topic>Fluorescent Antibody Technique</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Human protozoal diseases</topic><topic>Immunoblotting</topic><topic>immunochemistry</topic><topic>Infectious diseases</topic><topic>Medical sciences</topic><topic>Parasitic diseases</topic><topic>polypeptides</topic><topic>proteins</topic><topic>Protozoa</topic><topic>Protozoal diseases</topic><topic>Spectrin - analysis</topic><topic>Tropical medicine</topic><topic>Trypanosoma brucei</topic><topic>Trypanosoma brucei brucei - analysis</topic><topic>Trypanosomiasis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schneider, A</creatorcontrib><creatorcontrib>Lutz, H.U</creatorcontrib><creatorcontrib>Marugg, R</creatorcontrib><creatorcontrib>Gehr, P</creatorcontrib><creatorcontrib>Seebeck, T</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>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schneider, A</au><au>Lutz, H.U</au><au>Marugg, R</au><au>Gehr, P</au><au>Seebeck, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spectrin-like proteins in the paraflagellar rod structure of Trypanosoma brucei</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>1988-06-01</date><risdate>1988</risdate><volume>90</volume><issue>2</issue><spage>307</spage><epage>315</epage><pages>307-315</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><coden>JNCSAI</coden><abstract>A polyclonal, monospecific rabbit antibody to human erythrocyte spectrins cross-reacted with two sets of proteins (a doublet of 180/200K and a triplet of 67-66-65K; K = 10(3) Mr) in the parasitic protozoon Trypanosoma brucei brucei. Except for the 66K protein, the cross-reacting proteins are localized in the flagellum, on the basis of evidence from cell fractionation and immunofluorescence microscopy. Immunogold labelling and electron micrographs further revealed that the spectrin-like proteins are confined to the paraflagellar rod structure. The spectrin-like proteins with apparent molecular weights of 180 and 200 share homology with spectrin band 1, since V8-protease from Staphylococcus aureus generated similarly sized, antigenic peptides from these proteins. The results indicate homology between the cross-reacting proteins and human red cell spectrin.</abstract><cop>Cambridge</cop><pub>Company of Biologists</pub><pmid>3073166</pmid><doi>10.1242/jcs.90.2.307</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of cell science, 1988-06, Vol.90 (2), p.307-315 |
| issn | 0021-9533 1477-9137 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Company of Biologists |
| subjects | Animals antibodies Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences electron microscopy Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology Human protozoal diseases Immunoblotting immunochemistry Infectious diseases Medical sciences Parasitic diseases polypeptides proteins Protozoa Protozoal diseases Spectrin - analysis Tropical medicine Trypanosoma brucei Trypanosoma brucei brucei - analysis Trypanosomiasis |
| title | Spectrin-like proteins in the paraflagellar rod structure of Trypanosoma brucei |
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