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 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.
CSIRO, Australian Animal Health Laboratory, Geelong, Victoria, Australia.
J M
JM
Hammond
K W
KW
Sproat
T G
TG
Wise
A D
AD
Hyatt
M N
MN
Jagadish
B E
BE
Coupar
D000818:Animals; D002213:Capsid / Q000235:genetics* / Q000648:ultrastructure; D002460:Cell Line; D015870:Gene Expression; D005822:Genetic Vectors; D007181:Inclusion Bodies, Viral / Q000648:ultrastructure; D008854:Microscopy, Electron; D017800:Potyvirus / Q000235:genetics* / Q000276:immunology / Q000502:physiology*; D011994:Recombinant Proteins / Q000235:genetics / Q000648:ultrastructure; D011995:Recombination, Genetic; D014616:Vaccinia virus / Q000235:genetics* / Q000276:immunology; D014765:Viral Vaccines / Q000235:genetics / Q000276:immunology; D014779:Virus Replication
D011994:Recombinant Proteins; D014765:Viral Vaccines