Screening for peptides of anti-rotavirus by phage-displayed technique.
- Author:
Ning YAO
1
;
Lun-Guang YAO
;
Xiang-Man ZHANG
;
Tai-Lin GUO
;
Yun-Chao KAN
Author Information
1. Pharmacy College, Southwest Jiaotong University, Emeishan 614202, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Animals;
Antiviral Agents;
isolation & purification;
pharmacology;
Cell Line;
Cell Survival;
drug effects;
Dose-Response Relationship, Drug;
Drug Evaluation, Preclinical;
Humans;
Molecular Sequence Data;
Neutralization Tests;
Peptide Library;
Peptides;
chemistry;
immunology;
pharmacology;
Protein Binding;
Rotavirus;
drug effects;
growth & development;
immunology;
Sequence Analysis, Protein;
Viral Plaque Assay
- From:
Chinese Journal of Biotechnology
2007;23(3):403-408
- CountryChina
- Language:Chinese
-
Abstract:
In this study, a 15-mer phage display peptide library was employed to pan against human rotavirus immobilized on solid phase. 4 different peptides were selected and could bind with rotavirus particles specifically. Plaque reduction neutralization test and MTT analysis results indicated that 3 of the peptides can inhibit rotavirus infecting in vitro. A peptide which sequence is QSNPIHIITNTRNHP showed the best efficiency--93% neutralization infectivity. Two other peptides, A and B, showed 40% and 50% neutralization infectivity respectively. Amino sequence analysis results indicate the 3 peptides containing 2 conserved motifs: SNPIHII and NIP. No putative trypsin hydrolysis site was found in C peptide, however, 4 and 3 potential sites were found in A and B peptides respectively. Using trypsin inhibitor, both A and B peptides showed the similar antiviral effect as that of C peptide. It suggests that the intactness of the 2 conserved motifs play an important role in counteracting virus infection. According to the results of this study, peptide C is hopeful to be exploited as an antiviral peptide drug.
