Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein G_NS were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed G_NS protein was also located on the cell surface but did not exhibit fusogenic activity. The G_NS protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant G_NS but did not react with G protein antibodies. A His₆-tagged, soluble form of the G protein was expressed and purified by Ni²⁺–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen.