Antigenic properties of peptidic mimics for epitopes of the lipopolysaccharide from Brucella

J Mol Biol. 1999 Nov 19;294(1):181-91. doi: 10.1006/jmbi.1999.3248.

Abstract

The lipopolysaccharide (LPS) is up to now the only identified major virulence determinant of Brucella. This bacterium is responsible for brucellosis in animals and for Malta fever in humans. Several monoclonal antibodies (mAbs) directed against various LPS epitopes have been characterized. Two mAbs, named A15-6B3 and B66-2C8, directed against distinct LPS epitopes have been used to select peptides from 11 phage display libraries. The sequences of the selected peptides contain an overrepresentation of either proline or tryptophan residues when selected with either A15-6B3 or B66-2C8 mAbs, respectively. For the best binding peptides, competition with LPS for the binding to the mAb is detected, which suggests that the peptides bind to the paratope of the mAb. The phages selected from the libraries were used to immunise mice, and a weak antibody response directed against LPS has been observed. These data suggest that a subset of the selected peptides are mimotopes of the LPS epitopes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, Bacterial / immunology*
  • Brucella / immunology*
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes*
  • Lipopolysaccharides / immunology*
  • Mice
  • Mice, Inbred BALB C
  • Molecular Mimicry*
  • Molecular Sequence Data
  • Peptide Library
  • Peptides / immunology*
  • Proline / immunology
  • Selection, Genetic
  • Tryptophan / immunology
  • Vaccination

Substances

  • Antigens, Bacterial
  • Epitopes
  • Lipopolysaccharides
  • Peptide Library
  • Peptides
  • Tryptophan
  • Proline