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Characterization of structural proteins of hirame rhabdovirus, HRV

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Title: Characterization of structural proteins of hirame rhabdovirus, HRV
Authors: Nishizawa, Toyohiko Browse this author →KAKEN DB
Yoshimizu, Mamoru Browse this author →KAKEN DB
Winton, James Browse this author
Ahne, Winfried Browse this author
Kimura, Takahisa Browse this author →KAKEN DB
Issue Date: 8-May-1991
Publisher: Inter-Research
Journal Title: Diseases of Aquatic Organisms
Volume: 10
Start Page: 167
End Page: 172
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. Western blot analysis revealed that the G, N, and M2 proteins of HRV shared antigenic determinants with IHNV and VHSV, but not with any of the 4 fish vesiculoviruses tested. Cross-reactions between the M1 proteins of HRV, IHNV, or VHSV were not detected in this assay. Two-dimensional gel electrophoresis was used to show that HRV differed from IHNV or VHSV in the isoelectric point (pI) of the M1 and M2 proteins. In this system, 2 forms of the M1 protein of HRV and IHNV were observed. These subspecies of M1 had the same relative mobility but different pI values. Treatment of purified virions with 2% Triton X-100 in Tris buffer containing NaCl removed the G, M1, and M2 proteins of IHNV, but HRV virions were more stable under these conditions.
Rights: Copyright © 1991 Inter-Research
Relation: http://www.int-res.com/articles/dao/10/d010p167.pdf
Type: article
URI: http://hdl.handle.net/2115/38545
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 吉水 守

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