Molecular and structural analysis of a continuous birch profilin epitope defined by a monoclonal antibody.

@article{Wiedemann1996MolecularAS,
  title={Molecular and structural analysis of a continuous birch profilin epitope defined by a monoclonal antibody.},
  author={Philipp Wiedemann and Klaus Giehl and Steve C. Almo and Alexander A. Fedorov and Mark E. Girvin and Peter J. Steinberger and Mogens R{\"u}diger and Martina Ortner and Manfred J. Sippl and Christiane Dolecek and D. Kraft and Bm Jockusch and Rudolf Valenta},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 47},
  pages={
          29915-21
        }
}
The interaction of a mouse monoclonal antibody (4A6) and birch profilin, a structurally well conserved actin- and phosphoinositide-binding protein and cross-reactive allergen, was characterized. In contrast to serum IgE from allergic patients, which shows cross-reactivity with most plants, monoclonal antibody 4A6 selectively reacted with tree pollen profilins. Using synthetic overlapping peptides, a continuous hexapeptide epitope was identified. The exchange of a single amino acid (Gln-47… CONTINUE READING

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