We have determined the sequence of the gE and gI genes of canine herpesvirus (CHV), DFD-6 strain. The gE ORF codes for a 522 a.a. polypeptide with a signal sequence at the amino-terminus and a trans-membrane domain at the carboxy-terminus. The gI ORF codes for a 259 a.a. polypeptide with a signal sequence but no trans-membrane domain. Comparison with another line of CHV indicated that the DFD-6 gI gene underwent a frame-shift mutation which caused the loss of the trans-membrane domain. Antibodies against the gE and gI polypeptides detected a 94 kDa gE and a broad band of gI (55-62 kDa) in DFD-6 infected cells, respectively. The precursor of DFD-6 gE is modified to the mature form by N-linked glycosylation only in the presence of gI. Together with the fact that the gI- mutant of DFD-6 produced smaller plaques, it is suggested that the truncated DFD-6 gI is functional. The precursor of DFD-6 gI is modified to the mature form by N-linked glycosylation only in the presence of gE.