Keywords

Rotavirus, Phage Display, Antiviral Peptides, Plaque Inhibition

Abstract

Four polypeptides that specifically bind to rotavirus particles were screened from a phage random display pentapeptide library. The plaque reduction inhibition experiment and MTT assay showed that three of the polypeptides had an inhibitory effect on virus-infected cultured cells. Among them, the C peptide with the sequence QSNPIHIITNTRNHP had a significant inhibitory effect, with an inhibitory effect of 93%. The other two polypeptides A and B inhibited virus infection. The effects are 40% and 50% respectively. After polypeptide sequence analysis, it was found that these three pentadecapeptides have two conserved sequences, namely the 2nd to 8th amino acid residues SNPIHII and the 12th to 15th amino acid residues NIP. Trypsin hydrolysis site analysis showed that C peptide had no cleavage sites, while A peptide and B peptide had 3 and 4 potential hydrolysis sites respectively. Inhibiting trypsin activity in virus infection fluid, it was found that two peptides A and B can also significantly inhibit virus infection in vitro. This shows that the integrity of the two conserved sequences of the screened polypeptides plays an important role in antiviral infection. C-peptide has potential as an oral drug for the treatment of rotavirus infections.

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Original research done by YAO Ning, YAO Lun-Guang, ZHANG Xiang-Man, GUO Tai-Lin, KAN Yun-Chao, Yao Ning, Yao Lun-guang, Zhang Xiangman, Guo Tailin, Kan Yunchao

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