Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3431412 | Virus Research | 2006 | 7 Pages |
Abstract
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.
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Authors
Katsunori Okazaki, Sanae Fujii, Ayato Takada, Hiroshi Kida,