Recovery and characterization of a chimeric rinderpest virus with the glycoproteins of peste-des-petits-ruminants virus: Homologous F and H proteins are required for virus viability
Sc. Das et al., Recovery and characterization of a chimeric rinderpest virus with the glycoproteins of peste-des-petits-ruminants virus: Homologous F and H proteins are required for virus viability, J VIROLOGY, 74(19), 2000, pp. 9039-9047
Rinderpest (RP) and peste-des-petits-ruminants (PPR) are two important dise
ases of domestic ruminants. To improve on currently available vaccines agai
nst PPR, we have created cDNA copies of the RP virus genome in which either
the fusion (F) or hemagglutinin (H) gene, or both, was replaced with the c
orresponding gene from PPR virus. It was necessary to develop a modified re
scue system in which the T7 RNA polymerase was provided by a recombinant fo
wlpox virus and the entire rescue procedure took place in Vero cells before
we could obtain live virus from these chimeric constructs. No virus was re
covered when only one of the glycoprotein genes was changed, but a chimeric
virus containing both F and H genes from PPR virus was reproducibly rescue
d from cDNA, indicating that a virus-specific functional interaction takes
place between the F and H proteins. The rescued virus expressing the PPR gl
ycoproteins grew more slowly in tissue culture than either parental virus a
nd formed abnormally large syncytia. Goats infected with the chimera showed
no adverse reaction, as assessed by clinical signs, temperature, leukocyte
count, virus isolation, and serology, and were protected from subsequent c
hallenge with wild-type PPR virus.