J Gen Virol
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Journal of General Virology, Vol 79, 623-628, Copyright © 1998 by Society for General Microbiology

ARTICLES

Assembly of Amsacta moorei entomopoxvirus spheroidin into spheroids following synthesis in insect cells using a baculovirus vector

SA Marlow, LE Wilson, AM Lawrie, N Wilkinson and LA King
School of Biological and Molecular Sciences, Gipsy Lane Campus, Oxford Brookes University, UK.

The gene encoding the major occlusion body protein, spheroidin, of Amsacta moorei entomopoxvirus (AmEPV) was introduced into a baculovirus vector under control of the polyhedrin gene promoter. A recombinant virus produced large, ovoid occlusion body-like structures in both Spodoptera frugiperda and Trichoplusia ni cells. These structures resembled the spheroids found in AmEPV-infected Lymantria dispar cells, except they were devoid of virus particles and were not surrounded by a membrane- or envelope-like structure. These results were confirmed by immunofluoresence microscopy and Western blotting using a specific antipeptide antibody to spheroidin, and suggest that the supramolecular assembly of spheroids is not dependent on other EPV-encoded gene products. Transmission electron microscopy and subcellular fractionation experiments revealed that the spheroid-like structures were assembled in both the nucleus and cytoplasm of the recombinant virus-infected cells. This contrasts with the solely cytoplasmic localization found in AmEPV-infected cells.




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Copyright © 1998 by the Society for General Microbiology.