Expression of rotavirus VP2 produces empty corelike particles

Autor: Annie Charpilienne, Jean Cohen, S E Crawford, M Labbé, Mary K. Estes
Přispěvatelé: ProdInra, Migration, Unité de recherche Virologie et Immunologie Moléculaires (VIM (UR 0892)), Institut National de la Recherche Agronomique (INRA)
Rok vydání: 1991
Předmět:
Rotavirus
viruses
Gene Expression
Moths
Recombinant virus
medicine.disease_cause
law.invention
chemistry.chemical_compound
Virus-like particle
law
Gene expression
Morphogenesis
Polyhedrin
Cells
Cultured
ComputingMilieux_MISCELLANEOUS
[SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology
0303 health sciences
virus diseases
INSECTE
Capsid
[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
Recombinant DNA
Baculoviridae
Research Article
Molecular Sequence Data
Immunology
Biology
Transfection
Microbiology
03 medical and health sciences
Virology
Centrifugation
Density Gradient
medicine
Animals
RNA
Double-Stranded
030304 developmental biology
MORPHOGENESE
Base Sequence
030306 microbiology
Virion
DNA
Molecular biology
Solubility
chemistry
Insect Science
Capsid Proteins
Zdroj: Journal of Virology
Journal of Virology, American Society for Microbiology, 1991, 65 (6), pp.2946-2952
ISSN: 1098-5514
0022-538X
DOI: 10.1128/jvi.65.6.2946-2952.1991
Popis: The complete VP2 gene of bovine rotavirus strain RF has been inserted into the baculovirus transfer vector pVL941 under the control of the polyhedrin promoter. Cotransfection of Spodoptera frugiperda 9 cells with wild-type baculovirus DNA and transfer vector DNA led to the formation of recombinant baculoviruses which contain bovine rotavirus gene 2. Infection of S. frugiperda cells with this recombinant virus resulted in the production of a protein similar in size and antigenic properties to the authentic rotavirus VP2. The protein binds double-stranded RNA and DNA in an overlay protein blot assay. Expressed VP2 assembles in the cytoplasm of infected cells in corelike particles 45 nm in diameter. These corelike particles were purified by sucrose gradient centrifugation and found to be devoid of nucleic acid. Coexpression of VP2 and VP6 from heterologous rotavirus strains (bovine and simian) resulted in the formation of single-shelled particles. These results definitively show the existence of an innermost protein shell in rotavirus which is formed independently of other rotavirus proteins. These results have implications for schemes of rotavirus morphogenesis.
Databáze: OpenAIRE
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