K. Maeda et al., CHARACTERIZATION OF CANINE HERPESVIRUS GLYCOPROTEIN-D (HEMAGGLUTININ), Journal of veterinary medical science, 59(11), 1997, pp. 1003-1009
Glycoprotein D (go) of canine herpesvirus (CHV) YP2 strain was express
ed in COS-7 and insect (Spodoptera frugiperda; Sf9) cells. The gDs exp
ressed in COS-7 and Sf9 cells reacted with a panel of monoclonal antib
odies (MAbs) against CHV go (hemagglutinin) and an MAb 25C9 against fe
line herpesvirus type 1 (FHV-1) go by indirect immunofluorescence assa
y, and possessed a molecular weight (MW) of approximately 51-55 and 41
-46 kilodalton (kDa), respectively, when examined by immunoblot analys
is. After treatment with tunicamycin, the MW of the go expressed in Sf
9 cells became approximately 37 kDa. By hemadsorption (HAD) tests usin
g canine or (RBC), COS-7 cells expressing CHV go adsorbed only canine
RBC, but not feline RBC, whereas control COS-7 cells expressing FHV-1
go adsorbed feline RBC, but not canine RBC. By hemagglutination (HA) t
ests, lysates of Sf9 cells expressing CHV go agglutinated canine RBC,
but not feline RBC. These HA and HAD activities were inhibited by HA-i
nhibition MAbs against CHV go. Control lysates of Sf9 cells expressing
FHV-1 go agglutinated only feline RBC. Serum from mice inoculated wit
h lysates of Sf9 cells expressing CHV gD possessed a high titer of vir
us-neutralizing activities against CHV infection. These results indica
ted that CHV go is structurally similar to FHV-1 go, but is functional
ly different from FHV-1 gD.