Screening and antiviral analysis of phages that display peptides with an affinity to subunit C of porcine aminopeptidase

Monoclon Antib Immunodiagn Immunother. 2013 Oct;32(5):326-9. doi: 10.1089/mab.2013.0038.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites / genetics
  • CD13 Antigens / genetics*
  • Cell Surface Display Techniques
  • Enzyme-Linked Immunosorbent Assay / veterinary
  • Gastroenteritis, Transmissible, of Swine / drug therapy*
  • Male
  • Molecular Sequence Data
  • Oligopeptides / genetics
  • Oligopeptides / therapeutic use*
  • Peptide Library
  • Protein Subunits / genetics
  • Protein Subunits / metabolism*
  • Swine
  • Testis / virology*
  • Tetrazolium Salts
  • Thiazoles
  • Transmissible gastroenteritis virus / metabolism*
  • Transmissible gastroenteritis virus / physiology
  • Virus Internalization

Substances

  • Oligopeptides
  • Peptide Library
  • Protein Subunits
  • Tetrazolium Salts
  • Thiazoles
  • CD13 Antigens
  • thiazolyl blue