Epitope Specificities of the Groups Y and W-135 Polysaccharides of Neisseria meningitides.

• Author(s) / Creator(s)

  • Fusco P. C.
  • Bundle, D. R.
  • Ling, C.-C.
  • Michon, F.
  • Moore, S. L.
  • Uitz, C.

• Previous studies have identified the length dependency of several polysaccharide (PS) protective epitopes. We have investigated whether meningococcal polysaccharides Y and W-135 possess such epitopes. Oligosaccharides (OSs) consisting of one or more disaccharide repeating units (RU) were derived from the capsular PSs of group Y and W-135 meningococci (GYMP and GWMP, respectively) by mild acid hydrolysis. The relative affinities of anticapsular antibodies binding to derivative OSs of different chain lengths were measured in inhibition enzyme-linked immunosorbent assays. As OS size increased from two to three RU, there was a notable increase in binding inhibition of rabbit anti-group Y antiserum. This pattern of antibody binding inhibition was also observed for rabbit antiserum to group W-135, though the inhibition increase was much more pronounced. In the cases of both OS species, the concentration of inhibiting antigen required to achieve 50% inhibition of rabbit immunoglobulin binding increased progressively as the inhibiting disaccharide chain length increased from 1 RU through greater than 50 RU. These data suggest that antibodies directed against both of these meningococcal PSs recognize conformational epitopes only fully expressed in higher-molecularweight forms of these antigens.

• Date created

  2007

• Subjects / Keywords

  • Bacterial immunology
  • Polysaccharides
  • Antigens
  • Epitopes

• Type of Item

  Article (Published)

• DOI

  https://doi.org/10.7939/R39K45W8M

• License

  © 2007 American Society for Microbiology. This version of this article is open access and can be downloaded and shared. The original author(s) and source must be cited.