Characterization of rabies virus glycoprotein expressed by recombinant baculovirus

• Published in: Virus research Vol. 25; no. 1-2; p. 1
• Main Authors: Tuchiya, K. (Nippon Inst. for Biological Science, Ome, Tokyo (Japan)), Matsuura, Y, Kawai, A, Ishihama, A, Ueda, S
• Format: Journal Article
• Language: English
• Published: Netherlands 01.09.1992
• Subjects: ADN; Animals; BACULOVIRIDAE; Baculoviridae - genetics; Base Sequence; Cells, Cultured; Cloning, Molecular; DNA; DNA, Viral - genetics; EXPRESION GENICA; EXPRESSION DES GENES; GENE; GENE EXPRESSION; GENES; Genetic Vectors; GLICOPROTEINAS; GLYCOPROTEINE; GLYCOPROTEINS; Glycoproteins - chemistry; Glycoproteins - genetics; Glycosylation; IMMUNOLOGICAL TECHNIQUES; Molecular Sequence Data; RABIES VIRUS; Rabies virus - genetics; Recombinant Proteins - genetics; SPODOPTERA FRUGIPERDA; TECHNIQUE IMMUNOLOGIQUE; TECNICAS INMUNOLOGICAS; Viral Fusion Proteins - chemistry; Viral Fusion Proteins - genetics; VIRUS DE LA RABIA; VIRUS DE LA RAGE
• ISSN: 0168-1702; 1872-7492
• DOI: 10.1016/0168-1702(92)90095-Q

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.