Screening for Peptides of Antirotavirus by Phage-displayed Technique

In this study, a 15-mer phage display peptide library was used to pan against human rotavirus immobilized on solid phase. Four different peptides that could specifically bind with rotavirus particles were selected. The results of plaque reduction neutralization test and MTT analysis indicated that three of the peptides can inhibit rotavirus infecting in vitro. A peptide for which the sequence is QSNPIHIITNTRNHP showed the best efficiency-93% neutralization infectivity. Two other peptides, A and B, showed 40% and 50% neutralization infectivity, respectively. The results of amino sequence analysis indicate the three peptides containing two conserved motifs: SNPIHII and NIP. No putative trypsin hydrolysis site was found in C peptide, however, four and three potential sites were found in A and B peptides, respectively. Using trypsin inhibitor, both A and B peptides showed the similar antiviral effect as C peptide. It suggests that the intactness of the two conserved motifs play an important role in counteracting virus infection. According to the results of this study, peptide C is the potential candidate to be exploited as an antiviral peptide drug.