The amino-terminal residue of glycoprotein B is critical for neutralization of bovine herpesvirus 1

• Published in: Virus Research Vol. 115; no. 2; pp. 105 - 111
• Main Authors: Okazaki, Katsunori, Fujii, Sanae, Takada, Ayato, Kida, Hiroshi
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2006; Elsevier BV
• Subjects: Amino Acid Sequence; Amino Acid Substitution; Animals; Antibodies, Viral; Antibodies, Viral - immunology; BHV1; Bovine herpesvirus 1; Cattle; Cell Line; DNA, Viral; DNA, Viral - chemistry; DNA, Viral - genetics; Epitope Mapping; Epitopes; Epitopes - chemistry; Epitopes - immunology; Herpesvirus 1, Bovine; Herpesvirus 1, Bovine - genetics; Herpesvirus 1, Bovine - growth & development; Herpesvirus 1, Bovine - immunology; Immunohistochemistry; Molecular Sequence Data; Monoclonal antibody; Mutation; Mutation, Missense; Neutralization; Neutralization Tests; Sequence Deletion; Viral Envelope Proteins; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - genetics; Viral Envelope Proteins - immunology; Viral Plaque Assay; Viral Proteins; gB; Monoclonal antibody; BHV1; Neutralization
• ISSN: 0168-1702; 1872-7492
• DOI: 10.1016/j.virusres.2005.07.008

In order to address the neutralization epitope on bovine herpesvirus 1 (BHV1) glycoprotein B (gB), a panel of monoclonal antibodies (MAbs), a series of truncation forms of the glycoprotein and an MAb-escape mutant were used in this study. Immunocytochemistry on the truncations using MAbs against the glycoprotein revealed that the neutralization epitopes recognized by the MAbs lay between residues 1 and 52 of mature gB. Comparison of the sequences among the mutant, parent, and revertant viruses demonstrated that the amino-terminal residue of mature gB of the escape mutant was changed from Arg to Gln. These findings indicate that the amino-terminal residue of gB is critical for neutralization of BHV1.