Characterization of the allergic T-cell response to Pru p 3, the nonspecific lipid transfer protein in peach

Schulten, Véronique; Radakovics, Astrid; Hartz, Christina; Mari, Adriano; Vázquez-Cortés, Sonia; Fernández‐Rivas, Montserrat; Lauer, Iris; Jahn‐Schmid, Beatrice; Eiwegger, Thomas; Scheurer, Stephan; Bohle, Barbara

doi:10.1016/j.jaci.2009.02.010

Cited by 35 publications

(39 citation statements)

References 51 publications

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“…We believe that, even if biased by a limited overlap, the epitopes that we have identified are of interest given the reproducibility of our findings. In addition, our results are consistent with those of 2 recently published studies where Pru p 3 65–80 was identified as the major Th2 immunogenic peptide [15,16]. In the Spanish study, TCL recognition after amino acid 75 is low [15].…”

Section: Discussionsupporting

confidence: 92%

“…Pru p 3 is a major peach allergen recognized by serum IgE antibodies in many peach-allergic individuals [7]. While there are reports in the literature on the existence of peach-specific B-cell epitopes [13], data on peach-specific T-cell epitopes have only recently emerged [15,16]. Moreover, allergenic Pru p 3 homologues are present in several foods, and cross-reactivity among various fruit and vegetable allergens belonging to different botanical families has been demonstrated [32,33,34,35].…”

Section: Discussionmentioning

confidence: 99%

“…The regions of Pru p 3 bound by IgE antibodies have been previously identified [13], and recombinant Pru p 3 has been produced [14]. However, few primary data have been published that identify T-cell epitopes of Pru p 3 [15,16]. …”

Section: Introductionmentioning

confidence: 99%

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Characterization of the T-Cell Epitopes of the Major Peach Allergen Pru p 3

Pastorello

Monza

Pravettoni

et al. 2010

Int Arch Allergy Immunol

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Background: Pru p 3 is the major peach allergen recognized by more than 90% of peach-allergic individuals of the Mediterranean area. Identification of the dominant Pru p 3 T-cell epitopes can improve our understanding of the immune responses against this protein and could be helpful in the development of hypoallergenic immunotherapy. For this purpose, we examined the phenotypes, specificities and cytokine secretion profiles of proliferating T cells in response to Pru p 3 in peach-allergic individuals. Methods: Peripheral blood mononuclear cells from 15 peach-allergic patients were incubated with Pru p 3. The proliferation of antigen-specific T-cell lines (TCLs) was assessed by tritiated methylthymidine incorporation. T-cell epitopes were identified by analyzing the reactivity of TCLs against 8 overlapping peptides spanning the entire length of Pru p 3. We characterized the phenotype of Pru-p-3-specific TCLs by flow cytometry and analyzed their production of interleukin (IL) 4 and γ-interferon (IFN-γ) by ELISA. Results: Ninety-two Pru-p-3-specific TCLs were isolated (stimulation index ≧5). These TCLs proliferated mainly in response to Pru p 3_12–27 and Pru p 3_57–72. Pru-p-3-specific TCLs were mainly CD4+ (81%) and expressed cell surface CD30. In addition, TCLs produced high levels of IL-4 and low levels of IFN-γ, indicating a Th2 phenotype. Conclusions: Two immunodominant T-cell-reactive regions of Pru p 3 were identified: Pru p 3_12–27 and Pru p 3_57–72. These peptides showed a differential ability to elicit a Th2 response. Taken together, our results provide a better understanding of the immunological T-cell reactivity against Pru p 3.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

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Characterization of the T-Cell Epitopes of the Major Peach Allergen Pru p 3

Pastorello

Monza

Pravettoni

et al. 2010

Int Arch Allergy Immunol

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“…As observed previously, TCC constitutively expressed both integrins independently from their activation status 16. However, Bet v 1‐nonreactive TCC showed a slightly higher surface expression of integrin β7 and a significantly lower expression of integrin β1 (CD29, P = 0.032, Mann–Whitney U ‐test) than Bet v 1‐cross‐reactive Dau c 1‐specific TCC.…”

Section: Resultssupporting

confidence: 77%

“…To gain insight into the possible priming sites of Dau c 1‐specific T cells, we compared the expression of the integrins β7 and β1 on the surface of Dau c 1‐specific TCC cross‐reactive and nonreactive with Bet v 1. The gut‐homing factor integrin α4β7 binds to the key intestinal mucosal addressin cell adhesion molecule‐1 (MAdCAM‐1) 14 and has been shown to be expressed on milk allergen‐specific T cells and peanut‐specific TCC 15, 16. In contrast, the α4β1‐integrin (very late antigen‐4) has been implicated in the recruitment of T cells to extraintestinal sites of inflammation, such as lungs and skin 17.…”

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confidence: 99%

Characterization of the T-cell response to Dau c 1, the Bet v 1-homolog in carrot

Zulehner

Nagl

Briza

et al. 2016

Allergy

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BackgroundIn contrast to other Bet v 1‐related food allergens, the major carrot allergen, Dau c 1, has been suggested to induce food allergy independently from Bet v 1. As T cells are crucial in the sensitization process, we sought to characterize the T‐cell response to Dau c 1 and its cross‐reactivity with Bet v 1.MethodsDau c 1‐specific T‐cell lines (TCL) and clones (TCC) established from PBMC of birch pollen‐allergic patients with carrot allergy were analyzed for reactivity to Bet v 1, epitope specificity, allergen‐induced cytokine secretion, and expression of integrins α4β7 and α4β1, critical for gut and lung homing, respectively. mRNA expression of GATA3 and Tbet was analyzed in sorted CD3+ CD4+ CFSE low cells proliferating upon stimulation of PBMC with Dau c 1 or Bet v 1. Dau c 1 was incubated with endolysosomal proteases, and the resulting fragments were identified by mass spectrometry.ResultsAmong 14 distinct T‐cell‐activating regions, Dau c 1139–153 was recognized by 55% of the patients. Only 6 of 15 (40%) Dau c 1‐specific TCL and 9 of 21 (43%) TCC reacted with Bet v 1. Bet v 1‐nonreactive TCC were mainly Th1‐like and showed a higher expression of the integrin β7 and a significantly lower expression of the integrin β1 than Bet v 1‐positive TCC. A Th1‐like response was also detected in Dau c 1‐reactive CD3+ CD4+ CFSE low cells. Full‐length Dau c 1 was still detectable after 48 h of endolysosomal degradation. Proteolytic fragments of Dau c 1 matched its T‐cell‐activating regions.ConclusionDau c 1 displays several characteristics of sensitizing allergens, namely a major T‐cell‐activating region, low susceptibility to endolysosomal degradation, and induction of a Bet v 1‐independent T‐cell response. These cellular insights confirm that the major carrot allergen has a special status among Bet v 1‐related food allergens.

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