Epitope identification and in silico prediction of the specificity of antibodies binding to the coat proteins of Potato Virus Y strains

H.J.H.G. Keller, H. Pomp, J. Bakker, A. Schots

Research output: Contribution to journalArticleAcademicpeer-review

10 Citations (Scopus)

Abstract

A phage library containing 2.7 × 10(9) randomly expressed peptides was used to determine the epitopes of three monoclonal antibodies that bind to the coat protein of Potato Virus Y. Construction of the consensus sequences for the peptides obtained after three selection rounds indicated that each antibody recognized a different epitope located within the first 50 N-terminal amino acids of the coat protein. The location of the epitopes was confirmed by heterologous expression of the N-terminal part of the coat protein in Escherichia coli, and, subsequently, by performing an immunological test with the three antibodies. The accuracy of the phage library was demonstrated by predicting in silico the cross-reactivity of the three antibodies with other potyvirus family members. ELISA and in silico predictions revealed the same results in almost every case. The potential of peptide phage libraries to optimize the use of antibodies in plant virology is discussed
Original languageEnglish
Pages (from-to)391-397
JournalEuropean Journal of Plant Pathology
Volume111
Issue number4
DOIs
Publication statusPublished - 2005

Keywords

  • monoclonal-antibodies
  • phage
  • transmissibility
  • potyviruses
  • infection
  • peptides
  • antigens
  • library
  • surface
  • plants

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