The major conformational IgE-binding epitopes of hevein (Hev b6.02) are identified by a novel chimera-based allergen epitope mapping strategy.

@article{Karisola2002TheMC,
  title={The major conformational IgE-binding epitopes of hevein (Hev b6.02) are identified by a novel chimera-based allergen epitope mapping strategy.},
  author={Piia Karisola and Harri Alenius and Jari Mikkola and Nisse Erkki Juhani Kalkkinen and J. P. Helin and Olli T. Pentik{\"a}inen and Susanna Repo and Timo Reunala and Kristiina Turjanmaa and Mark S Johnson and Timo Palosuo and Markku S. Kulomaa},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 25},
  pages={
          22656-61
        }
}
A novel approach to localize and reconstruct conformational IgE-binding epitope regions of hevein (Hev b6.02), a major natural rubber latex allergen, is described. An antimicrobial protein (AMP) from the amaranth Amaranthus caudatus was used as an immunologically non-IgE-binding adaptor molecule to which terminal or central parts of hevein were fused. Hevein and AMP share a structurally identical core region but have different N-terminal and C-terminal regions. Only 1 of 16 hevein-allergic… CONTINUE READING

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