Identification by serological proteome analysis of paramyosin as prominent allergen in dust mite allergy

Conti, Antonio; Burastero, Giulia; Suli, C.; Banerjee, Srinita; Vrtala, Susanne; Alessio, Massimo; Burastero, Samuele E.

doi:10.1016/j.jprot.2017.06.024

Cited by 9 publications

(6 citation statements)

References 29 publications

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“…Der f 2 was shown to be the most frequently sensitized allergen among HDM‐sensitized respiratory allergy and atopic dermatitis patients in a Korean study, wherein the combination of group 1 and 2 major allergens improved diagnostic sensitivity [35 ]. In a serological proteome analysis study, a group 11 HDM allergen was found to contain an HDM allergic serum IgE‐recognized allergen component [36 ]. Interestingly, sensitization to Der p 10 was shown to result from seafood‐cockroach cross‐reactivity in a study with participants from coastal southern China [37 ].…”

Section: Discussionmentioning

confidence: 99%

Identification of immunodominant IgE binding epitopes of Der p 24, a major allergen of Dermatophagoides pteronyssinus

Cai

Chen

Zhang

et al. 2019

Clin Transl Allergy

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Background The identification of house dust mite (HDM) allergens and epitopes is important for allergy diagnosis and treatment. We sought to identify the Dermatophagoides pteronyssinus group 24 allergen (Der p 24) and to identify its immunodominant IgE epitope(s). Methods Der p 24 cDNA was cloned and expressed in a pET expression system. The IgE binding activity of purified recombinant (r)Der p 24 was evaluated by western blotting. Truncated Der p 24 proteins and overlapping synthetic polypeptides were subjected to IgE binding assays. Balb/c mice were immunized to investigate IgE epitope induction of IgE production. IgE binding of the 32 N-terminal residues of Der p 24 was compared to other Der p epitopes in enzyme-linked immunosorbent assays and dot blot assays. Human skin prick tests (SPTs) were performed. Results We cloned and expressed Der p 24 cDNA (GenBank accession no. KP893174.1). HDM allergic sera bound rDer p 24 in vitro and 5/10 HDM allergic patients (50%) had positive SPT reactions to rDer p 24. The immunodominant IgE epitope of Der p 24 was localized to the N-terminal 32-residue region, which produced a high specific IgE antibody titer in vivo and promoted mast cell β-hexosaminidase release. The IgE binding activity this N-terminal epitope of Der p 24 was stronger than that of Der p 1 or Der p 2 IgE epitopes. Conclusions We identified Der p 24 as a major HDM allergen with strong IgE binding activity via an immunodominant IgE epitope in the N-terminal 32-residue region, which triggers IgE production in vivo. The identified Der p 24 epitope may support HDM allergy diagnosis and treatment.

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Section: Discussionmentioning

confidence: 99%

Identification of immunodominant IgE binding epitopes of Der p 24, a major allergen of Dermatophagoides pteronyssinus

Cai

Chen

Zhang

et al. 2019

Clin Transl Allergy

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“…However, some clinical researchers pointed out that TM is not a major cross-reactive allergen in HDM and snail cross-reactive allergies, or even involved in snail allergy, and that other non-TM allergens may play a dominant role in the cross-reactivity between HDM and molluscs . Like the TM, PM is a protein associated with muscular contraction described in diverse invertebrates and is also a major allergen in molluscs and mites (such as Rap v 2, Der f 11 and Der p 11). , As a high MW allergen, PM has been suggested to play an important role in allergic asthma caused by dust mites . Interestingly, in this work, multiple IgE-binding components involved in cross-reactivity between D.…”

Section: Discussionmentioning

confidence: 67%

“…43 Like the TM, PM is a protein associated with muscular contraction described in diverse invertebrates and is also a major allergen in molluscs and mites (such as Rap v 2, Der f 11 and Der p 11). 20,44 As a high MW allergen, PM has been suggested to play an important role in allergic asthma caused by dust mites. 45 Interestingly, in this work, multiple IgE-binding components involved in cross-reactivity between D. farinae and mollusc species, as well as PMs were recognized and confirmed by mass spectrometry in the D. farinae extract and inhibition ELISA assay, suggesting that the PM might be a cross-reactive allergen implicated in mite−mollusc crossreactivity.…”

Section: ■ Discussionmentioning

confidence: 99%

Immunological Cross-Reactivity Involving Mollusc Species and Mite–Mollusc and Cross-Reactive Allergen PM Are Risk Factors of Mollusc Allergy

Xue

Gao

et al. 2022

J. Agric. Food Chem.

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Marine molluscs are seafood consumed worldwide and could cause food allergies, while investigation on their sensitizing components and cross-reactivity seems to be rare. Furthermore, allergy to mites may result in anaphylaxis in molluscallergic individuals owing to their cross-reactivity. The aim of the study was to identify cross-reactive allergens and investigate the cross-reactivity between different mollusc groups and mite−mollusc. The extracted mollusc and dust mite proteins were separated by SDS-PAGE, and IgE-binding components were recognized by immunoblotting with sera from patients sensitized to mollusc and mite. Cross-reactivity of different mollusc groups and mite−mollusc was assessed using ELISA and inhibition ELISA. The results of the immune detection, ELISA, and inhibition ELISA indicated that different mollusc groups and mite−mollusc showed varying degrees of cross-reactivity. The most frequently recognized cross-reactive protein was paramyosin from different mollusc groups and dust mite, while cross-reactive allergen paramyosin in the mite extract was identified and evaluated by MS and Allermatch, respectively. Inhibition ELISA studies also revealed that paramyosin played an important role in molluscan and mite−molluscan cross-reactivity. These findings contribute to a better understanding of the cross-reactivity involving mollusc species and mite− mollusc, which can be used to assist in the diagnosis and treatment of mite-and mollusc-allergic disorders.

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“…Paramyosin, a prominent allergen in dust mite allergies, was initially determined by in vivo (prick test) and in vitro (serum specific IgE) tests ( 99 ). The allergen was then analysed by 2-D gel electrophoresis combined with immunoblotting and MS.…”

Section: Methods For the Detection And Analysis Of Allergensmentioning

confidence: 99%

Review of New Trends in the Analysis of Allergenic Residues in Foods and Cosmetic Products

Tuzimski

Petruczynik

2020

Journal of AOAC INTERNATIONAL

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Background Allergies represent an important health problem in industrialized countries. Allergen sensitization is an important risk factor for the development of allergic diseases; thus, the identification of an individual’s allergen sensitization is essential for the diagnosis and treatment of diseases. Objective This review compares different modern methods applied for the analysis of allergens in various matrices (from 2015 to the end of September 2019). Conclusions Immunological methods are still most frequently used for detection of allergens. These methods are sensitive, but the lack of specificity and cross-reaction of some antibodies can still be a relevant source of errors. DNA-based methods are fast and reliable for determination of protein allergens, but the epitopes of protein allergens with posttranslational modifications and their changes, originated during various processing, cannot be identified through the use of this method. Methods based on application of biosensors are very rapid and easy to use, and can be readily implemented as screening methods to monitor allergens. Recent developments of new high-resolution MS instruments are encouraging and enable development in the analysis of allergens. Fast, very sensitive, reliable, and accurate detection and quantification of allergens in complex samples can be used in the near future. Mass spectrometry coupled with LC, GC, or electrophoretic methods bring additional advances in allergen analysis. The use of LC-MS or LC-MS/MS for the quantitative detection of allergens in various matrices is at present gaining acceptance as a protein-based confirmatory technique over the routinely performed enzyme-linked immunosorbent assays.

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Identification by serological proteome analysis of paramyosin as prominent allergen in dust mite allergy

Cited by 9 publications

References 29 publications

Identification of immunodominant IgE binding epitopes of Der p 24, a major allergen of Dermatophagoides pteronyssinus

Identification of immunodominant IgE binding epitopes of Der p 24, a major allergen of Dermatophagoides pteronyssinus

Immunological Cross-Reactivity Involving Mollusc Species and Mite–Mollusc and Cross-Reactive Allergen PM Are Risk Factors of Mollusc Allergy

Review of New Trends in the Analysis of Allergenic Residues in Foods and Cosmetic Products

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