Fine mapping of a continuous epitope on VP7 of bluetongue virus using overlapping synthetic peptides and a random epitope library

Virology. 1994 Jan;198(1):346-9. doi: 10.1006/viro.1994.1039.

Abstract

Two complementary techniques have been used to delineate an epitope on VP7 of bluetongue virus. Two MAbs (F10 and D11), both of which bound within a region spanning amino acids 255 to 274 in the 349 amino acid protein, were used to probe overlapping synthetic peptides covering this region. A pentapeptide, QYPAL, and a hexapeptide, QY-PALT (amino acids 259-264), preferentially bound both MAbs. MAb F10 also reacted with a heptapeptide (TAEIFNV) immediately adjacent to QYPALT. The MAbs were also used to affinity-purify fusion phages from a random hexapeptide library. All phage peptides selected were similar to QYPALT. Comparison of the peptides suggested that residues Q and P at positions 1 and 3 were critical for recognition. Some affinity-purified phages displayed the hexapeptide QYPSLL, which is similar to a sequence in VP7 of another orbivirus, epizootic hemorrhagic disease virus. This finding allowed a potentially cross-reactive site to be identified.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Antigens, Viral / analysis*
  • Antigens, Viral / immunology
  • Bluetongue virus / chemistry
  • Bluetongue virus / immunology*
  • Capsid / analysis
  • Capsid / immunology*
  • Capsid Proteins*
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes / analysis*
  • Epitopes / immunology
  • Molecular Sequence Data
  • Peptide Fragments / analysis
  • Peptide Fragments / genetics
  • Peptide Fragments / immunology
  • Peptide Mapping

Substances

  • Antigens, Viral
  • Capsid Proteins
  • Epitopes
  • Peptide Fragments
  • VP7 protein, Rotavirus