Abstract：
:A cDNA of the glycoprotein (G protein) gene of rabies virus Nishigahara strain was cloned and inserted into a baculovirus genome under the control of the polyhedrin promoter. Infection of Spodoptera frugiperda cells with this recombinant virus produced a large quantity of new protein instead of the parental polyhedrin protein. By immunofluorescent and immunoblotting analyses, the recombinant protein was antigenically similar to the authentic G protein. Its molecular mass estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, however, was slightly smaller than that of the authentic one, and this observation was suggested to be due to the difference in glycosylation level between the two G proteins. The recombinant G protein expressed on the cell surface of the insect cells showed a fusion activity at low pH. The fusion activity was inhibited by antiserum against either whole virions or G protein of rabies virus.
journal_name
Virus Resjournal_title
Virus researchauthors
Tuchiya K,Matsuura Y,Kawai A,Ishihama A,Ueda Sdoi
10.1016/0168-1702(92)90095-qsubject
Has Abstractpub_date
1992-09-01 00:00:00pages
1-13issue
1-2eissn
0168-1702issn
1872-7492pii
0168-1702(92)90095-Qjournal_volume
25pub_type
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