Resolution and identification of major peanut allergens using a combination of fluorescence two-dimensional differential gel electrophoresis, Western blotting and Q-TOF mass spectrometry

Chassaigne, Hubert; Tregoat, Virginie; Nørgaard, Jørgen; Maleki, Soheila J.; Hengel, Arjon J. van

doi:10.1016/j.jprot.2009.02.002

Cited by 57 publications

(37 citation statements)

References 36 publications

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“…From the six peptides that were characterised in the potential fenugreek 7S vicilin-like protein, three (FEITPEK; RNFLAGEEDNVISQIQRPVKEL and isoform RNFLAGEEDNVISQVERPVKEL) were homologous to known IgE-binding epitopes in the major peanut allergen Ara h 1 [26, 32]. The determination of two fenugreek isoformic peptides in the C-terminal sequence segment, which has been shown to be especially stable and was used as biomarker in the quantitative MS analysis of peanut in foods [33], may indicate the presence of two distinct “Tri f 1”-isoforms.…”

Section: Discussionmentioning

confidence: 99%

Characterization of potential allergens in fenugreek (Trigonella foenum-graecum) using patient sera and MS-based proteomic analysis

Fæste

Christians

Egaas

et al. 2010

Journal of Proteomics

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Section: Discussionmentioning

confidence: 99%

Characterization of potential allergens in fenugreek (Trigonella foenum-graecum) using patient sera and MS-based proteomic analysis

Fæste

Christians

Egaas

et al. 2010

Journal of Proteomics

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“…The peanut seed storage proteins Ara h 1 (vicilin), Ara h 2 (conglutin) and Ara h 3 (glycinin) are all major allergens and seem to be responsible for primary sensitization to peanut in susceptible individuals [14,15]. IgE antibodies to the peanut storage proteins have been suggested as risk markers for severe allergic reactions in peanut-sensitized individuals [16].…”

Section: Introductionmentioning

confidence: 99%

Evaluation of IgE Antibodies to Recombinant Peanut Allergens in Patients with Reported Reactions to Peanut

Movérare¹,

Ahlstedt

Bengtsson

et al. 2011

Int Arch Allergy Immunol

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Background: Peanut may cause severe reactions in allergic individuals. The objective was to evaluate IgE antibodies to various recombinant (r) peanut and birch pollen allergens in relation to IgE levels to whole peanut extract and severe allergic reactions to peanut. Methods: Seventy-four Swedish peanut-allergic patients (age: 14–61 years) reported previous peanut exposure and associated symptoms using a questionnaire. Their IgE reactivity to peanut, birch pollen and individual allergen components was analyzed using ImmunoCAP®. Results: Of the 48 subjects sensitized to Ara h 1, 2 or 3, 60% had peanut-specific IgE levels >15 kU_A/l, while 100% of the subjects without detectable IgE to these allergens had low peanut-specific IgE levels (<10 kU_A/l). The levels of IgE to rAra h 8, rBet v 1 and birch pollen were highly correlated (r_S = 0.94, p < 0.0001). Fifty-eight patients reported adverse reactions after accidental or deliberate peanut exposure (oral, inhalation or skin) of whom 41 had IgE to rAra h 1, 2 or 3. Symptoms of respiratory distress were associated with sensitization to Ara h 1, 2 or 3 (56 vs. 18%, p < 0.01). Two cases of anaphylaxis were reported among the individuals sensitized to Ara h 1–3. IgE to rAra h 8, rAra h 9, profilin or cross-reactive carbohydrate determinants were not associated with severe symptoms. Conclusions: The results indicate that IgE reactivity to Ara h 1, 2 and 3 is associated with severe reactions after exposure to peanut in Swedish patients.

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“…Ara h 3/4 is mainly proteolytically modified (truncation at multiple sites) with possible glycosylation. Proteolytic truncation was observed for the acidic subunit but not for the basic resulting in a series of polypeptides ranging from 13–45 kDa [16]. Ara h 1 and Ara h 3 were clearly identified through mass spectrometry in both samples (bands 1–4; 11 and 14; Table 3).…”

Section: Resultsmentioning

confidence: 99%

Current Challenges in Detecting Food Allergens by Shotgun and Targeted Proteomic Approaches: A Case Study on Traces of Peanut Allergens in Baked Cookies

2012

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There is a need for selective and sensitive methods to detect the presence of food allergens at trace levels in highly processed food products. In this work, a combination of non-targeted and targeted proteomics approaches are used to illustrate the difficulties encountered in the detection of the major peanut allergens Ara h 1, Ara h 2 and Ara h 3 from a representative processed food matrix. Shotgun proteomics was employed for selection of the proteotypic peptides for targeted approaches via selective reaction monitoring. Peanut presence through detection of the proteotypic Ara h 3/4 peptides AHVQVVDSNGNR (m/z 432.5, 3+) and SPDIYNPQAGSLK (m/z 695.4, 2+) was confirmed and the developed method was able to detect peanut presence at trace levels (≥10 μg peanut g−1 matrix) in baked cookies.

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Resolution and identification of major peanut allergens using a combination of fluorescence two-dimensional differential gel electrophoresis, Western blotting and Q-TOF mass spectrometry

Cited by 57 publications

References 36 publications

Characterization of potential allergens in fenugreek (Trigonella foenum-graecum) using patient sera and MS-based proteomic analysis

Characterization of potential allergens in fenugreek (Trigonella foenum-graecum) using patient sera and MS-based proteomic analysis

Evaluation of IgE Antibodies to Recombinant Peanut Allergens in Patients with Reported Reactions to Peanut

Current Challenges in Detecting Food Allergens by Shotgun and Targeted Proteomic Approaches: A Case Study on Traces of Peanut Allergens in Baked Cookies

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