Analysis of the structure and allergenicity of recombinant pro- and mature Der p 1 and Der f 1: Major conformational IgE epitopes blocked by prodomains

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Analysis of the structure and allergenicity of recombinant pro- and mature Der p 1 and Der f 1: Major conformational IgE epitopes blocked by prodomains Toshiro Takai, PhD, Takeshi Kato, BS, Hiroshi Yasueda, PhD, Ko Okumura, MD, PhD, Hideoki Ogawa, MD, PhD Journal of Allergy and Clinical Immunology Volume 115, Issue 3, Pages 555-563 (March 2005) DOI: 10.1016/j.jaci.2004.11.024 Copyright © 2005 American Academy of Allergy, Asthma and Immunology Terms and Conditions

Fig 1 Molecular sizes and secondary structures of purified recombinant proforms and mature forms and natural types of Der p 1 (A, C, and E) and Der f 1 (B, D, and F). Fig 1, A-D, Gel-filtration analysis. The fractions shown as 1 through 8 in Fig 1, A and B, were subjected to SDS-PAGE (15% to 25%) under nonreducing conditions and silver stained and are shown in Fig 1, C and D, respectively. Fig 1, E and F, CD spectra. Journal of Allergy and Clinical Immunology 2005 115, 555-563DOI: (10.1016/j.jaci.2004.11.024) Copyright © 2005 American Academy of Allergy, Asthma and Immunology Terms and Conditions

Fig 2 Comparison of direct IgE-binding capacity among recombinant and natural Der p 1 and Der f 1. The serum dilution was 1:8. The concentration of allergens in the immobilization step was 50 nM. Journal of Allergy and Clinical Immunology 2005 115, 555-563DOI: (10.1016/j.jaci.2004.11.024) Copyright © 2005 American Academy of Allergy, Asthma and Immunology Terms and Conditions

Fig 3 Inhibition of IgE binding to immobilized natural Der p 1 and Der f 1 by means of soluble recombinant proforms and mature forms and natural types. The concentration of the natural allergens in the immobilization step was 50 nM. A, The serum dilution was 1:8 for sera 1 through 4 and 7, 1:4 for serum 5, and 1:100 for serum 6. Dp1, Der p 1; Df1, Der f 1. B and C, The serum dilution was 1:8. Journal of Allergy and Clinical Immunology 2005 115, 555-563DOI: (10.1016/j.jaci.2004.11.024) Copyright © 2005 American Academy of Allergy, Asthma and Immunology Terms and Conditions

Fig 4 Histamine release from basophils stimulated with recombinant proforms and mature forms and natural types of Der p 1 (A) and Der f 1 (B). Spontaneous histamine release for volunteers 1, 2, and 3 were 19%, 27%, and 7% in Fig 4, A, and 19%, 30%, and 4% in Fig 4, B, respectively. The results shown are representative of 2 or 3 independent experiments. Journal of Allergy and Clinical Immunology 2005 115, 555-563DOI: (10.1016/j.jaci.2004.11.024) Copyright © 2005 American Academy of Allergy, Asthma and Immunology Terms and Conditions

Fig 5 Homology modeling of the tertiary structure of pro-Der f 1. A, Front view. B, View from the right side of Fig 5, A. The prosegment, mature portion, and the N-glycosylation site Asn53 are shown in blue, red, and green, respectively. The catalytic center, Cys35, is shown as a space-filling model in yellow. These figures were produced by using the RasMol program.32 Journal of Allergy and Clinical Immunology 2005 115, 555-563DOI: (10.1016/j.jaci.2004.11.024) Copyright © 2005 American Academy of Allergy, Asthma and Immunology Terms and Conditions