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Naturally processed T cell–activating peptides of the major birch pollen allergen  Sonja Mutschlechner, PhD, Matthias Egger, PhD, Peter Briza, PhD, Michael.

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Presentation on theme: "Naturally processed T cell–activating peptides of the major birch pollen allergen  Sonja Mutschlechner, PhD, Matthias Egger, PhD, Peter Briza, PhD, Michael."— Presentation transcript:

1 Naturally processed T cell–activating peptides of the major birch pollen allergen 
Sonja Mutschlechner, PhD, Matthias Egger, PhD, Peter Briza, PhD, Michael Wallner, PhD, Peter Lackner, PhD, Anette Karle, PhD, Anne B. Vogt, PhD, Gottfried F. Fischer, MD, Barbara Bohle, PhD, Fatima Ferreira, PhD  Journal of Allergy and Clinical Immunology  Volume 125, Issue 3, Pages e2 (March 2010) DOI: /j.jaci Copyright © 2010 American Academy of Allergy, Asthma & Immunology Terms and Conditions

2 Fig 1 Time kinetics of endolysosomal processing of Bet v 1. After 0.5 to 24 hours of incubation of Bet v 1 with endolysosomal proteases isolated from DCs, generated peptides were sequenced by mass spectrometry. Frequently recognized T-cell epitopes are framed in the amino acid sequence of Bet v 1, shown on top. Journal of Allergy and Clinical Immunology  , e2DOI: ( /j.jaci ) Copyright © 2010 American Academy of Allergy, Asthma & Immunology Terms and Conditions

3 Fig 2 Optimizing the period for allergen pulsing of DCs. DCs from an individual with birch pollen allergy were incubated with Bet v 1 (5 μg/0.5 × 106 cells) for 6, 11, 24, and 48 hours, respectively, and used to stimulate a Bet v 1–specific T-cell clone. T-cell proliferation (SI) is shown. Journal of Allergy and Clinical Immunology  , e2DOI: ( /j.jaci ) Copyright © 2010 American Academy of Allergy, Asthma & Immunology Terms and Conditions

4 Fig 3 Naturally processed Bet v 1–derived peptides. Peptides eluted from purified HLA-DR:peptide complexes isolated from DCs of 4 patients with Bet v 1 allergy were sequenced by mass spectrometry. A, Amino acid sequence of Bet v 1. Frequently recognized T-cell epitopes are framed. B, HLA-DR–eluted peptides are shown in black; 12mer peptides inducing proliferative responses in Bet v 1–specific TCLs are shown in gray. Journal of Allergy and Clinical Immunology  , e2DOI: ( /j.jaci ) Copyright © 2010 American Academy of Allergy, Asthma & Immunology Terms and Conditions

5 Fig 4 T cell–activating properties of naturally processed Bet v 1–derived peptides. Bet v 1–reactive TCCs were stimulated with 2.5 μmol/L of the epitope-containing 12mer peptide (black bars), an 18mer peptide representing the HLA-DR–eluted peptides (white bars), and Bet v 1 (gray bars). TCC218 was stimulated with FKYNYSVIEGGP and FKYNYSVIEGGPIGDTLE. TCC266, TCC334, TCC14VR, and TCC4R were stimulated with TLLRAVESYLLA and GETLLRAVESYLLAHSDA. A, Proliferative responses (SI) are shown. B, Cytokines (pg/mL) were measured by ELISA. Journal of Allergy and Clinical Immunology  , e2DOI: ( /j.jaci ) Copyright © 2010 American Academy of Allergy, Asthma & Immunology Terms and Conditions

6 Fig 5 Structural determinants of the immunodominant T-cell epitope Bet v (TLLRAVESYLLA). A, Zigzags in the aa sequence of Bet v 1 represent α-helices, arrows indicate β-sheets, and bars represent loops. Structure assignments were taken from Protein Data Bank file 1BV1. B, The loop (green) flanking the C-terminal α-helix (golden) containing Bet v is shown in the 3-dimensional structure. C, Surface representation of the loop (green) flanking the C-terminal α-helix (golden) containing Bet v Peptide C-N atoms in the loop region are yellow and blue. The arrow indicates the only solvent-accessible peptide bond. Molecular graphics in B and C were created with UCSF Chimera (PMID: ). Journal of Allergy and Clinical Immunology  , e2DOI: ( /j.jaci ) Copyright © 2010 American Academy of Allergy, Asthma & Immunology Terms and Conditions

7 Time kinetics of endolysosomal processing of Bet v 1. A, After 0
Time kinetics of endolysosomal processing of Bet v 1. A, After 0.5 to 24 hours of incubation of Bet v 1 with endolysosomal proteases, 10 μL of the digestion reactions corresponding to 2.5 μg Bet v 1 were analyzed by SDS-PAGE and Coomassie staining. M, Marker (kd); B, Bet v 1 in digestion buffer without microsomal fractions. B, Grayscaled and inverted bands corresponding to intact Bet v 1 were quantified as integrated measures of intensity and size using the software Adobe Photoshop CS3. Protein degradation is shown as function of time. Journal of Allergy and Clinical Immunology  , e2DOI: ( /j.jaci ) Copyright © 2010 American Academy of Allergy, Asthma & Immunology Terms and Conditions

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