Screening for peptides of anti-rotavirus by phage-displayed technique / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 403-408, 2007.
Article
in Chinese
| WPRIM
| ID: wpr-328015
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Antiviral Agents
/
Peptides
/
Pharmacology
/
Viral Plaque Assay
/
Protein Binding
/
Neutralization Tests
/
Molecular Sequence Data
/
Cell Line
/
Cell Survival
/
Chemistry
Type of study:
Diagnostic study
/
Screening study
Limits:
Animals
/
Humans
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2007
Type:
Article
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