Expression of the potyvirus coat protein mediated by recombinant vaccinia virus and assembly of potyvirus-like particles in mammalian cells

The coat protein of the potyvirus, Johnsongrass mosaic virus (JGMV), was expressed using a recombinant vaccinia virus (VV) system. Ultra-thin section electron microscopy demonstrated that the coat protein assembled into potyvirus-like particles (PVLPs) in recombinant VV infected cells. Infection of...

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Bibliographic Details
Published in:Archives of virology 1998-01, Vol.143 (7), p.1433-1439
Main Authors: Hammond, J.M, Sproat, K.W, Wise, T.G, Hyatt, A.D, Jagadish, M.N, Coupar, B.E.H
Format: Article
Language:English
Subjects:
Animals
Antigens
Biological and medical sciences
Capsid - genetics
Capsid - ultrastructure
Cell Line
Coat protein
coat proteins
Electron microscopy
Environmental factors
Fundamental and applied biological sciences. Psychology
Gene Expression
Generalities. Techniques. Transmission, epidemiology, ecology. Antiviral substances, control
Genetic Vectors
Inclusion Bodies, Viral - ultrastructure
Johnsongrass mosaic virus
Mammalian cells
Microbiology
Microscopy, Electron
Oral administration
Phytopathology. Animal pests. Plant and forest protection
Plant virus diseases
Plant viruses
Plant viruses and viroids
Potyvirus
Potyvirus - genetics
Potyvirus - immunology
Potyvirus - physiology
Recombinant Proteins - genetics
Recombinant Proteins - ultrastructure
Recombinants
Recombination, Genetic
Techniques used in virology
vaccine development
Vaccines
Vaccinia virus - genetics
Vaccinia virus - immunology
Viral Vaccines - genetics
Viral Vaccines - immunology
Virology
Virus Replication
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Summary:The coat protein of the potyvirus, Johnsongrass mosaic virus (JGMV), was expressed using a recombinant vaccinia virus (VV) system. Ultra-thin section electron microscopy demonstrated that the coat protein assembled into potyvirus-like particles (PVLPs) in recombinant VV infected cells. Infection of cells with two additional VV recombinants expressing coat protein plus N-terminal and N- and C-terminal extensions also resulted in the formation of PVLPs. These results suggest that the ability of VV to express the potyvirus coat protein at sufficient levels to allow PVLP formation in vitro, could make VV a suitable vector for the delivery of PVLPs displaying vaccine antigens in vivo without the need for particle purification and/or inclusion of adjuvant. Use of such a vaccine strategy would also benefit from the proven advantages of poxviruses as vaccines such as stability in a freeze dried form, resistance to environmental factors and the potential for oral administration.
ISSN:0304-8608
1432-8798
DOI:10.1007/s007050050387