Three mouse monoclonal antibodies (mAb) specific to E2 antigen of human hepatitis G virus (HGV) were used to bio-panning of a phage displayed random peptide library of 15 amino acid residues. After 3 rounds of screening, the ratio of output to input increased to 1.1 × 10-3 and the false positive rate reduced to 0.2% , which means the enrichment was effective. At the third round of screening, 15 plage clones were selected for the use in binding and competitive inhibition tests. Thirteen of them could specifically react with the mAb M6. The inhibition rates of phage 10 clones out of 15 were over 60% . From the deduced insert sequence in the coat protein Ⅷ, the core sequence NPLWP was found in 6 phage clones which are homologeous to the amino acids 301-305 of HGV E2 .The sera from the mice immunized with the phage clone C2 containing motif sequence were found positive for anti-HGV, These indicate the possibility that NPLWP motif in the short peptide is the mimic of HGV E2 epitope that can be recognized b Three mouse monoclonal antibodies (mAb) specific to E2 antigen of human hepatitis G virus (HGV) were used to bio-panning of a phage displayed random peptide library of 15 amino acid residues. After 3 rounds of screening, the ratio of output to input increased to 1.1 × 10 -3 and the false positive rate reduced to 0.2%, which means the enrichment was effective. At the third round of screening, 15 plage clones were selected for the use in binding and competitive inhibition tests. Thirteen of them could could specifically react with the mAb M6. The inhibition rates of phage 10 clones out of 15 were over 60%. From the deduced insert sequence in the coat protein VIII, the core sequence NPLWP was found in 6 phage clones which are homologeous to the amino acids 301-305 of HGV E2. The sera from the mice immunized with the phage clone C2 containing motif sequence were found positive for anti-HGV, These indicate the possibility that NPLWP motif in the short peptide is the mimic of HGV E2 epitope that can be recognized b