The antigen-binding site of an N-propionylated polysialic acid-specific antibody protective against group B meningococci is consistent with extended epitopes.

@article{Johal2013TheAS,
  title={The antigen-binding site of an N-propionylated polysialic acid-specific antibody protective against group B meningococci is consistent with extended epitopes.},
  author={Asha R. Johal and Harold C. Jarrell and James A. Letts and Nam Huan Khieu and Roxanne C Landry and Wojciech Jachymek and Qingling Yang and Harold J. Jennings and Jean Robert Brisson and Stephen V Evans},
  journal={Glycobiology},
  year={2013},
  volume={23 8},
  pages={
          946-54
        },
  url={https://api.semanticscholar.org/CorpusID:9755772}
}
The model of extended NPrPSA decasaccharide bound to 13D9 derived from docking studies is consistent with saturation transfer difference nuclear magnetic resonance experiments, providing further evidence that extended epitopes have the ability to break immune tolerance associated with the polysialic acid capsule of these pathogens.

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