A Novel Isoallergen Dau c 1.0401 in Carrot: Stability, Allergenicity, and Comparison with Other Isoallergens

Jacob, Thessa; Wangorsch, Andrea; Vogel, Lothar; Reuter, Andreas; Mahler, Vera; Wöhrl, Birgitta M.

doi:10.1002/mnfr.202001110

Cited by 3 publications

(17 citation statements)

References 24 publications

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“…Isolation and identification of mRNA was performed as previously described [ 15 ] using specific primers in the 3’‐ and 5’‐UTR region of the different Dau c 1 genes based on their hypothetical mRNA (Table S1, Supporting Information).…”

Section: Methodsmentioning

confidence: 99%

“…Sera from carrot‐allergic patients that were recently used to test their reactivity against nDau c 1 and to characterize the isoallergen Dau c 1.0401 were applied in this study. [ 15 ] The sera were obtained after written consent and approval of the ethics committee (Faculty of Medicine, Friedrich‐Alexander‐University of Erlangen‐Nuremberg, No. 3494).…”

Section: Methodsmentioning

confidence: 99%

“…3494). [ 15 ] Characterization of the sera and their use in the various assays described here was shown in Table S3, Supporting Information.…”

Section: Methodsmentioning

confidence: 99%

“…Mediator release assays (MRAs) and IgE immunoblots were essentially performed as previously described . [ 14,15,20,21 ] For immunoblotting 0.8 µg non‐reduced protein cm −1 was used for the SDS‐polyacrylamide gel electrophoresis (PAGE). Transfer of the putative allergens onto nitrocellulose membranes was controlled by Ponceau S staining (Figure S1A, Supporting Information).…”

Section: Methodsmentioning

confidence: 99%

“…We have previously reported that the qualitative composition of nDau c 1 is unexpected, with at least eight isoallergens or variants that have not been characterized yet. [ 14 ]…”

Section: Introductionmentioning

confidence: 99%

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Allergenicity and IgE Recognition of New Dau c 1 Allergens from Carrot

Hendrich

Wangorsch

Rödel

et al. 2022

Molecular Nutrition Food Res

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Scope Carrot (Daucus carota) allergy is caused by the major carrot allergen Dau c 1, which is a mixture of several isoallergens and variants with sequence identities of >67% or >90%, respectively. However, little is known about the qualitative and quantitative composition of natural Dau c 1. Methods and results Mass spectrometry of isolated natural Dau c 1 reveals the existence of several yet unknown Dau c 1‐like proteins. The study expresses four Dau c 1‐like proteins in Escherichia coli. Two of the purified proteins, designated Dau c 1.0501 and 1.0601, exhibit sequence identities to Dau c 1.0101 and 1.0401 between 54% and 87%. They possess allergenic potential and are accepted as new isoallergens. One protein, designated as Dau c 1‐like is >50% identical with the new isoallergens but exhibits no allergenicity. Sequence and structural comparisons of this protein with the known Dau c 1 isoallergens offer relevant clues about putative structural IgE epitopes. Conclusion Identification of new isoallergens and the identification of IgE epitopes may contribute to a more refined component resolved diagnosis and may lay ground for further epitope mapping and personalized targeted treatment approaches of carrot allergy in preclinical and clinical studies.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…3494). [ 15 ] Characterization of the sera and their use in the various assays described here was shown in Table S3, Supporting Information.…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…We have previously reported that the qualitative composition of nDau c 1 is unexpected, with at least eight isoallergens or variants that have not been characterized yet. [ 14 ]…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Allergenicity and IgE Recognition of New Dau c 1 Allergens from Carrot

Hendrich

Wangorsch

Rödel

et al. 2022

Molecular Nutrition Food Res

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Allergenicity and structural properties of new Cor a 1 isoallergens from hazel identified in different plant tissues

Hendrich,

Reuter,

Jacob

et al. 2024

Sci Rep

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The hazel allergen Cor a 1 is a PR-10 protein, closely related to the major birch pollen allergen Bet v 1. Hazel allergies are caused by cross-reactive IgE antibodies originally directed against Bet v 1. Despite the importance of PR-10 proteins in allergy development, their function and localization in the plant remain largely elusive. Therefore, the presence of Cor a 1 mRNA and proteins was investigated in different tissues, i.e., the female flower, immature and mature nuts, catkins, and pollen. Four yet unknown Cor a 1 isoallergens, i.e., Cor a 1.0501–1.0801, and one new Cor a 1.03 variant were discovered and characterized. Depending on the isoallergen, the occurrence and level of mRNA expression varied in different tissues, suggesting different functions. Interestingly, Cor a 1.04 previously thought to be only present in nuts, was also detected in catkins and pollen. The corresponding Cor a 1 genes were expressed in Escherichia coli. The purified proteins were analysed by CD and NMR spectroscopy. Immunoblots and ELISAs to determine their allergenic potential showed that the new proteins reacted positively with sera from patients allergic to birch, hazel and elder pollen and were recognized as novel isoallergens/variants by the WHO/IUIS Allergen Nomenclature Sub-Committee.

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Linear Epitope Binding Patterns of Grass Pollen-Specific Antibodies in Allergy and in Response to Allergen-Specific Immunotherapy

et al. 2022

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Allergic diseases affect many individuals world-wide and are dependent on the interaction between allergens and antibodies of the IgE isotype. Allergen-specific immunotherapy (AIT) can alter the development of the disease, e.g., through induction of allergen-specific IgG that block allergen-IgE interactions. The knowledge of epitopes recognized by allergy-causing and protective antibodies are limited. Therefore, we developed an allergome-wide peptide microarray, aiming to track linear epitope binding patterns in allergic diseases and during AIT. Here, we focused on immune responses to grass pollen allergens and found that such epitopes were commonly recognized before initiation of AIT and that AIT commonly resulted in increased antibody production against additional epitopes already after 1 year of treatment. The linear epitope binding patterns were highly individual, both for subjects subjected to and for individuals not subjected to AIT. Still, antibodies against some linear epitopes were commonly developed during AIT. For example, the two rigid domains found in grass pollen group 5 allergens have previously been associated to a diversity of discontinuous epitopes. Here, we present evidence that also the flexible linker, connecting these domains, contains regions of linear epitopes against which antibodies are developed during AIT. We also describe some commonly recognized linear epitopes on Phl p 2 and suggest how antibodies against these epitopes may contribute to or prevent allergy in relation to a well-defined stereotyped/public IgE response against the same allergen. Finally, we identify epitopes that induce cross-reactive antibodies, but also antibodies that exclusively bind one of two highly similar variants of a linear epitope. Our findings highlight the complexity of antibody recognition of linear epitopes, with respect to both the studied individuals and the examined allergens. We expect that many of the findings in this study can be generalized also to discontinuous epitopes and that allergen peptide microarrays provide an important tool for enhancing the understanding of allergen-specific antibodies in allergic disease and during AIT.

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A Novel Isoallergen Dau c 1.0401 in Carrot: Stability, Allergenicity, and Comparison with Other Isoallergens

Cited by 3 publications

References 24 publications

Allergenicity and IgE Recognition of New Dau c 1 Allergens from Carrot

Allergenicity and IgE Recognition of New Dau c 1 Allergens from Carrot

Allergenicity and structural properties of new Cor a 1 isoallergens from hazel identified in different plant tissues

Linear Epitope Binding Patterns of Grass Pollen-Specific Antibodies in Allergy and in Response to Allergen-Specific Immunotherapy

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