In order to map antigenically important regions of glycoprotein B (gB) of p
seudorabies virus (PrV), a panel of recombinant fragments of gB expressed i
n E. coli and truncated fragments of gB generated by cleavage of purified n
ative gB with trypsin and cyanogen bromide was analysed by using 26 monoclo
nal antibodies directed against gB. Three continuous epitopes were localize
d in the vicinity of the N terminus of gB, between amino acids (aa) 59 and
126. One continuous epitope mapped between residues 214 and 279. The residu
es involved in the assembly of eight discontinuous epitopes were located be
tween aa 540 and 734. The constituents of two discontinuous epitopes were h
arboured in a segment encompassing aa 540-646. The clustering of continuous
epitopes at the extreme N terminus of PrV gB and the locations of residues
involved in the assembly of discontinuous epitopes of PrV gB are in good a
greement with data on epitope locations in gB homologues from other herpesv
iruses.