Jm. Hammond et al., EXPRESSION OF THE POTYVIRUS COAT PROTEIN-MEDIATED BY RECOMBINANT VACCINIA VIRUS AND ASSEMBLY OF POTYVIRUS-LIKE PARTICLES IN MAMMALIAN-CELLS, Archives of virology, 143(7), 1998, pp. 1433-1439
The coat protein of the potyvirus, Johnsongrass mosaic virus (JGMV), w
as expressed using a recombinant vaccinia virus (VV) system. Ultra-thi
n section electron microscopy demonstrated that the coat protein assem
bled into potyvirus-like particles (PVLPs) in recombinant VV infected
cells. Infection of cells with two additional VV recombinants expressi
ng coat protein plus N-terminal and N- and C-terminal extensions also
resulted in the formation of PVLPs. These results suggest that the abi
lity 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 su
ch a vaccine strategy would also benefit from the proven advantages of
poxviruses as vaccines such as stability in a freeze dried form, resi
stance to environmental factors and the potential for oral administrat
ion.