High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X-ray crystallography.

@article{Padavattan2009HighaffinityIR,
  title={High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X-ray crystallography.},
  author={Sivaraman Padavattan and Sabine Flicker and Tlilman Schirmer and Christoph Madritsch and Stefanie Randow and Gerald H. Reese and Stephan Vieths and Christian Lupinek and Christof Ebner and Rudolf Valenta and Zora Markovi{\'c}-Housley},
  journal={Journal of immunology},
  year={2009},
  volume={182 4},
  pages={
          2141-51
        }
}
We report the three-dimensional structure of the complex between the major respiratory grass pollen allergen Phl p 2 and its specific human IgE-derived Fab. The Phl p 2-specific human IgE Fab has been isolated from a combinatorial library constructed from lymphocytes of a pollen allergic patient. When the variable domains of the IgE Fab were grafted onto human IgG1, the resulting Ab (huMab2) inhibited strongly the binding of allergic patients' IgE to Phl p 2 as well as allergen-induced basophil… CONTINUE READING
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