Characterization of structural proteins of hirame rhabdovirus, HRV
Structural proteins of hirame rhabdovirus (HRV) were analyzed by SDS-polyacrylamide gel electrophoresis, western blotting, 2-dimensional gel electrophoresis, and Triton X-100 treatment. Purified HRV virions were composed of: polymerase (L), glycoprotein (G), nucleoprotein (N), and 2 matrix proteins...
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Veröffentlicht in: | Diseases of aquatic organisms 1991-05, Vol.10 (3), p.167-172 |
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creator | NISHIZAWA, T YOSHIMIZU, M WINTON, J AHNE, W KIMURA, T |
description | Structural proteins of hirame rhabdovirus (HRV) were analyzed by SDS-polyacrylamide gel electrophoresis, western blotting, 2-dimensional gel electrophoresis, and Triton X-100 treatment. Purified HRV virions were composed of: polymerase (L), glycoprotein (G), nucleoprotein (N), and 2 matrix proteins (M1 and M2). Based upon their relative mobilities, the estimated molecular weights of the proteins were: L, 156 KDa; G, 68 KDa; N, 46.4 KDa; M1, 26.4 KDa; and M2, 19.9 KDa. The electrophoretic pattern formed by the structural proteins of HRV was clearly different from that formed by pike fry rhabdovirus, spring viremia of carp virus, eel virus of America, and eel virus European X which belong to the Vesiculovirus genus; however, it resembled the pattern formed by structural proteins of viral hemorrhagic septicemia virus (VHSV) and infectious hematopoietic necrosis virus (IHNV) which are members of the Lyssavirus genus. Among HRV, IHNV, and VHSV, differences were observed in the relative mobilities of the G, N, M1, and M2 proteins. |
doi_str_mv | 10.3354/dao010167 |
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Purified HRV virions were composed of: polymerase (L), glycoprotein (G), nucleoprotein (N), and 2 matrix proteins (M1 and M2). Based upon their relative mobilities, the estimated molecular weights of the proteins were: L, 156 KDa; G, 68 KDa; N, 46.4 KDa; M1, 26.4 KDa; and M2, 19.9 KDa. The electrophoretic pattern formed by the structural proteins of HRV was clearly different from that formed by pike fry rhabdovirus, spring viremia of carp virus, eel virus of America, and eel virus European X which belong to the Vesiculovirus genus; however, it resembled the pattern formed by structural proteins of viral hemorrhagic septicemia virus (VHSV) and infectious hematopoietic necrosis virus (IHNV) which are members of the Lyssavirus genus. Among HRV, IHNV, and VHSV, differences were observed in the relative mobilities of the G, N, M1, and M2 proteins.</description><identifier>ISSN: 0177-5103</identifier><identifier>EISSN: 1616-1580</identifier><identifier>DOI: 10.3354/dao010167</identifier><identifier>CODEN: DAOREO</identifier><language>eng</language><publisher>Oldendorf: Inter-Research</publisher><subject>biochemical composition ; Biological and medical sciences ; electrophoresis ; fish diseases ; Fundamental and applied biological sciences. 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Purified HRV virions were composed of: polymerase (L), glycoprotein (G), nucleoprotein (N), and 2 matrix proteins (M1 and M2). Based upon their relative mobilities, the estimated molecular weights of the proteins were: L, 156 KDa; G, 68 KDa; N, 46.4 KDa; M1, 26.4 KDa; and M2, 19.9 KDa. The electrophoretic pattern formed by the structural proteins of HRV was clearly different from that formed by pike fry rhabdovirus, spring viremia of carp virus, eel virus of America, and eel virus European X which belong to the Vesiculovirus genus; however, it resembled the pattern formed by structural proteins of viral hemorrhagic septicemia virus (VHSV) and infectious hematopoietic necrosis virus (IHNV) which are members of the Lyssavirus genus. Among HRV, IHNV, and VHSV, differences were observed in the relative mobilities of the G, N, M1, and M2 proteins.</description><subject>biochemical composition</subject><subject>Biological and medical sciences</subject><subject>electrophoresis</subject><subject>fish diseases</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hemorrhagic septicemia virus</subject><subject>hirame rhabdovirus</subject><subject>infectious hematopoietic necrosis virus</subject><subject>Lyssavirus</subject><subject>Marine</subject><subject>Microbiology</subject><subject>proteins</subject><subject>Rhabdoviridae</subject><subject>rhabdovirus</subject><subject>structural proteins</subject><subject>Virology</subject><subject>viruses</subject><issn>0177-5103</issn><issn>1616-1580</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNo9kE1Lw0AYhBdRsFYP_oMcRBCM7rtfyR61qBUKgqjX8GY_6Eqa1N1EqL_elJaeBoZnhmEIuQR6x7kU9xY7ChRUcUQmoEDlIEt6TCYUiiKXQPkpOUvpm1JgWsKEPM6WGNH0LoY_7EPXZp3PUh8H0w8Rm2wdu96FNm3tZYi4cllcYm273xCHdJvN37_OyYnHJrmLvU7J5_PTx2yeL95eXmcPi9wIzvq8oNxTb6RliiteFgBUIgUwljlUhS4E495xgFrXpdGWlTUvhbCaWSydtXxKrne946afwaW-WoVkXNNg67ohVSC1YEzpEbzZgSZ2KUXnq3UMK4ybCmi1fak6vDSyV_tSTAYbH7E1IR0CkgsxTuP_lMBmdw</recordid><startdate>19910508</startdate><enddate>19910508</enddate><creator>NISHIZAWA, T</creator><creator>YOSHIMIZU, M</creator><creator>WINTON, J</creator><creator>AHNE, W</creator><creator>KIMURA, T</creator><general>Inter-Research</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TN</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H94</scope><scope>H95</scope><scope>H97</scope><scope>H98</scope><scope>L.G</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>19910508</creationdate><title>Characterization of structural proteins of hirame rhabdovirus, HRV</title><author>NISHIZAWA, T ; YOSHIMIZU, M ; WINTON, J ; AHNE, W ; KIMURA, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c432t-703f0fc5d26363871105a011cd2ea6797423fe311b9b8c9d28b3844d92da8edd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>biochemical composition</topic><topic>Biological and medical sciences</topic><topic>electrophoresis</topic><topic>fish diseases</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hemorrhagic septicemia virus</topic><topic>hirame rhabdovirus</topic><topic>infectious hematopoietic necrosis virus</topic><topic>Lyssavirus</topic><topic>Marine</topic><topic>Microbiology</topic><topic>proteins</topic><topic>Rhabdoviridae</topic><topic>rhabdovirus</topic><topic>structural proteins</topic><topic>Virology</topic><topic>viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>NISHIZAWA, T</creatorcontrib><creatorcontrib>YOSHIMIZU, M</creatorcontrib><creatorcontrib>WINTON, J</creatorcontrib><creatorcontrib>AHNE, W</creatorcontrib><creatorcontrib>KIMURA, T</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Oceanic Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Aquaculture Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Diseases of aquatic organisms</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>NISHIZAWA, T</au><au>YOSHIMIZU, M</au><au>WINTON, J</au><au>AHNE, W</au><au>KIMURA, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of structural proteins of hirame rhabdovirus, HRV</atitle><jtitle>Diseases of aquatic organisms</jtitle><date>1991-05-08</date><risdate>1991</risdate><volume>10</volume><issue>3</issue><spage>167</spage><epage>172</epage><pages>167-172</pages><issn>0177-5103</issn><eissn>1616-1580</eissn><coden>DAOREO</coden><abstract>Structural proteins of hirame rhabdovirus (HRV) were analyzed by SDS-polyacrylamide gel electrophoresis, western blotting, 2-dimensional gel electrophoresis, and Triton X-100 treatment. Purified HRV virions were composed of: polymerase (L), glycoprotein (G), nucleoprotein (N), and 2 matrix proteins (M1 and M2). Based upon their relative mobilities, the estimated molecular weights of the proteins were: L, 156 KDa; G, 68 KDa; N, 46.4 KDa; M1, 26.4 KDa; and M2, 19.9 KDa. The electrophoretic pattern formed by the structural proteins of HRV was clearly different from that formed by pike fry rhabdovirus, spring viremia of carp virus, eel virus of America, and eel virus European X which belong to the Vesiculovirus genus; however, it resembled the pattern formed by structural proteins of viral hemorrhagic septicemia virus (VHSV) and infectious hematopoietic necrosis virus (IHNV) which are members of the Lyssavirus genus. Among HRV, IHNV, and VHSV, differences were observed in the relative mobilities of the G, N, M1, and M2 proteins.</abstract><cop>Oldendorf</cop><pub>Inter-Research</pub><doi>10.3354/dao010167</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | biochemical composition Biological and medical sciences electrophoresis fish diseases Fundamental and applied biological sciences. Psychology hemorrhagic septicemia virus hirame rhabdovirus infectious hematopoietic necrosis virus Lyssavirus Marine Microbiology proteins Rhabdoviridae rhabdovirus structural proteins Virology viruses |
title | Characterization of structural proteins of hirame rhabdovirus, HRV |
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