[Analysis on patial amino acid sequence of a novel glycoprotein binding to antiherpes simplex virus monoclonal antibody CHA9].

Aim: To acquire the characteristic amino acid sequence of a novel glycoprotein of herpes simplex virus (HSV), so as to localize gene encoding the novel glycoprotein accurately.
Methods: A 12-mer phage peptide library was screened for 3 rounds by using biotinylated mAb CHA9 against new glycoprotein g30k of HSV-2. Positive phage clones were detected by ELISA. 10 positive clones were selected randomly for sequencing. Sequence alignment and hydrophobic cluster analysis were carried out.
Results: Most of the sequences of 10 positive phage clones were highly homologous with a core-PH/KHXHXGS-. Phages containing this motif could react specifically with the mAb CHA9 and not cross-react with other IgG. Hydrophobic cluster analysis showed that the peptide was likely to form an epitope.
Conclusion: We obtained a characteristic short peptide which shows some characters of g30K amino acid sequence. It provides valuable clue for prediction of the open reading frame of g30K gene and will be useful to explore biological characteristics of the new glycoprotein.