Phage displayed 6-mer mimotopes with a consensus proline absent in the minimized linear wild-type epitope

Sabrina Deroo, Philippe Fournier, Dietmar Theisen, Nicolas H.C. Brons, Hans Deckmyn, Claude P. Muller*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

1 Citation (Scopus)

Abstract

Phage displayed random 6-mer libraries were screened with a monoclonal antibody specific for a minimized 'linear' 7-mer epitope of the measles virus hemagglutinin protein. No clone with the wild-type sequence was selected and most clones contained a sequence motif not found in the wild-type sequence. Two mimotopes (LYMPQLS, SEMPQLP) were synthesized which inhibited binding to the measles virus 95-135 times better than a wild-type peptide. Sequence comparison of proteins with known 3D-structure indicates that the epitope corresponds to an α-helix, while the best mimotopes have no predicted helix propensity. The proline is thought to be required for inducing a turn necessary for mimicking part of the α-helix. The higher intrinsic stability of such a mimotope may explain its improved binding and may be more suitable in immunogenicity experiments.

Original languageEnglish
Pages (from-to)159-162
Number of pages4
JournalLetters in Peptide Science
Volume5
Issue number2-3
DOIs
Publication statusPublished - 1998
Externally publishedYes

Keywords

  • Measles virus
  • Monoclonal antibody
  • Peptides
  • Phage display libraries

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