Identification and characterization of the glycoprotein E and I genes of canine herpesvirus

• Published in: Virus research Vol. 56; no. 1; pp. 77 - 92
• Main Authors: Nishikawa, Yoshifumi, Xuan, Xuenan, Otsuka, Haruki
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.07.1998
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Blotting, Western; Canine herpesvirus; Cell Line; DNA, Viral - analysis; Dogs; Female; Genes, Viral; Glycoproteins - chemistry; Glycoproteins - genetics; Herpesvirus 1, Canid - genetics; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - genetics; Mice; Molecular Sequence Data; Mutation; Open Reading Frames; Polymerase Chain Reaction; Rabbits; Sequence Alignment; Sequence Homology, Amino Acid; Vaccinia virus - genetics; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - genetics; Canine herpesvirus; gI; gE
• DOI: 10.1016/S0168-1702(98)00062-8
• ISSN: 0168-1702

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.