Functional fine-mapping and molecular modeling of a conserved loop epitope of the measles virus hemagglutinin protein.

@article{Ptz2003FunctionalFA,
  title={Functional fine-mapping and molecular modeling of a conserved loop epitope of the measles virus hemagglutinin protein.},
  author={Mike M P{\"u}tz and Johan Hoebeke and Wim Ammerlaan and Serge Schneider and Claude P. Muller},
  journal={European journal of biochemistry},
  year={2003},
  volume={270 7},
  pages={1515-27}
}
Neutralizing and protective monoclonal antibodies (mAbs) were used to fine-map the highly conserved hemagglutinin noose epitope (H379-410, HNE) of the measles virus. Short peptides mimicking this epitope were previously shown to induce virus-neutralizing antibodies [El Kasmi et al. (2000) J. Gen. Virol.81, 729-735]. The epitope contains three cysteine residues, two of which (Cys386 and Cys394) form a disulfide bridge critical for antibody binding. Substitution and truncation analogues revealed… CONTINUE READING

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