Abstract
The purified C subunit of the recombinant porcine aminopeptidase N (rpAPN-C) protein was used as an immobilized target to screen potential ligands against rpAPN-C from a 12-mer phage display random peptide library. After five rounds of biopanning, five phage clones showed specific binding affinities to rpAPN-C. In 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyl tetrazolium bromide (MTT) assays, the phage clone PM1, which contained the HDAISWTHYHPW peptide sequence, had a protective effect against TGEV infection in swine testis cells. Therefore, the HDAISWTHYHPW peptide sequence has a potential use as a small molecular therapeutic agent against TGEV infection.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites / genetics
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CD13 Antigens / genetics*
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Cell Surface Display Techniques
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Enzyme-Linked Immunosorbent Assay / veterinary
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Gastroenteritis, Transmissible, of Swine / drug therapy*
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Male
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Molecular Sequence Data
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Oligopeptides / genetics
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Oligopeptides / therapeutic use*
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Peptide Library
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Protein Subunits / genetics
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Protein Subunits / metabolism*
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Swine
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Testis / virology*
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Tetrazolium Salts
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Thiazoles
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Transmissible gastroenteritis virus / metabolism*
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Transmissible gastroenteritis virus / physiology
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Virus Internalization
Substances
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Oligopeptides
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Peptide Library
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Protein Subunits
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Tetrazolium Salts
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Thiazoles
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CD13 Antigens
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thiazolyl blue