Epitope mapping of 7S cashew antigen in complex with antibody by solution‐phase H/D exchange monitored by FT‐ICR mass spectrometry

Guan, Xiaoyan; Noble, Kyle A.; Tao, Yeqing; Roux, Kenneth H.; Sathe, Shridhar K.; Young, Nicolas L.; Marshall, Alan G.

doi:10.1002/jms.3589

Cited by 20 publications

(18 citation statements)

References 51 publications

(79 reference statements)

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“…Using the same procedure to obtain a recombinant Ana o 1, Guan et al [66] demonstrated that two of the linear epitope-contributing peptide segments, which were previously reported by Wang et al [65], participate in a conformational epitope. Additionally, the authors also revealed three new peptide segments that are believed to function as independent linear epitopes when complexed with some antibodies and/or together, contributing to one or more conformational epitopes [66].…”

Section: Ana O 1-vicilinmentioning

confidence: 86%

Cashew Nut Allergy: Clinical Relevance and Allergen Characterisation

Mendes

Costa

Vicente

et al. 2016

Clinic Rev Allerg Immunol

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Cashew plant (Anacardium occidentale L.) is the most relevant species of the Anacardium genus. It presents high economic value since it is widely used in human nutrition and in several industrial applications. Cashew nut is a well-appreciated food (belongs to the tree nut group), being widely consumed as snacks and in processed foods by the majority of world's population. However, cashew nut is also classified as a potent allergenic food known to be responsible for triggering severe and systemic immune reactions (e.g. anaphylaxis) in sensitised/allergic individuals that often demand epinephrine treatment and hospitalisation. So far, three groups of allergenic proteins have been identified and characterised in cashew nut: Ana o 1 and Ana o 2 (cupin superfamily) and Ana o 3 (prolamin superfamily), which are all classified as major allergens. The prevalence of cashew nut allergy seems to be rising in industrialised countries with the increasing consumption of this nut. There is still no cure for cashew nut allergy, as well as for other food allergies; thus, the allergic patients are advised to eliminate it from their diets. Accordingly, when carefully choosing processed foods that are commercially available, the allergic consumers have to rely on proper food labelling. In this sense, the control of labelling compliance is much needed, which has prompted the development of proficient analytical methods for allergen analysis. In the recent years, significant research advances in cashew nut allergy have been accomplished, which are highlighted and discussed in this review.

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Section: Ana O 1-vicilinmentioning

confidence: 86%

Cashew Nut Allergy: Clinical Relevance and Allergen Characterisation

Mendes

Costa

Vicente

et al. 2016

Clinic Rev Allerg Immunol

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“…Linear epitopes, composed of a continuous amino acid sequence, have been detected by screening patient sera on sequential overlapping peptide libraries or allergen fragments. Conformational epitopes, composed of sterically closed amino acids upon folding, were characterized by phage display technique or mass spectrometry partly in combination with B‐cell epitope prediction web tools or software, although the use of these techniques still has to be proven in future studies …”

Section: Introductionmentioning

confidence: 99%

“…tools or software, although the use of these techniques still has to be proven in future studies. 6,[17][18][19][20][21] So far, it is impossible to discriminate between clinically relevant and irrelevant epitopes or combinations using current approaches and to use these differences as diagnostic or prognostic markers.…”

mentioning

confidence: 99%

Can alternative epitope mapping approaches increase the impact of B‐cell epitopes in food allergy diagnostics?

Ehlers

Blankestijn

Knulst

et al. 2018

Clin Experimental Allergy

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Summary In vitro allergy diagnostics are currently based on the detection of specific IgE binding on intact allergens or a mixture thereof. This approach has drawbacks as it may yield false‐negative and/or false‐positive results. Thus, we reviewed the impact of known B‐cell epitopes of food allergens to predict transience or persistence, tolerance or allergy and the severity of an allergic reaction and to examine new epitope mapping strategies meant to improve serum‐based allergy diagnostics. Recent epitope mapping approaches have been worthwhile in epitope identification and may increase the specificity of allergy diagnostics by using epitopes predominately recognized by allergic patients in some cases. However, these approaches did not lead to discrimination between clinically relevant and irrelevant epitopes so far, since the polyclonal serum IgE‐binding epitope spectrum seems to be too individual, independent of the disease status of the patients. New epitope mapping strategies are necessary to overcome these obstacles. The use of patient‐derived monoclonal antibodies instead of patient sera for functional characterization of clinically relevant and irrelevant epitope combinations, distinguished by their ability to induce degranulation, might be a promising approach to gain more insight into the allergic reaction and to improve serum‐based allergy diagnostics.

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“…Owing to its sequencing capability, MS is one “read-out” for many functional epitope-mapping approaches [2, 3]. Moreover, MS-based footprinting (e.g., HDX-MS) have successfully bridged high and low-resolution structural epitope mapping methods by reliably localizing the binding site at the peptide level [4–8]. …”

Section: Introductionmentioning

confidence: 99%

Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding

Huang

Salinas

Chen

et al. 2017

J. Am. Soc. Mass Spectrom.

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Plasmodium vivax Duffy Binding Protein (PvDBP) is a promising vaccine candidate for P. vivax malaria. Recently, we reported the epitopes on PvDBP region II (PvDBP-II) for three inhibitory monoclonal antibodies (2D10, 2H2, and 2C6). In this communication, we describe the combination of native mass spectrometry and ion mobility (IM) with collision induced unfolding (CIU) to study the conformation and stabilities of three malarial antigen-antibody complexes. These complexes, when collisionally activated, undergo conformational changes that depend on the location of the epitope. CIU patterns for PvDBP-II in complex with antibody 2D10 and 2H2 are highly similar, indicating comparable binding topology and stability. A different CIU fingerprint is observed for PvDBP-II/2C6, indicating that 2C6 binds to PvDBP-II on an epitope different from 2D10 and 2H2. This work supports the use of CIU as a means of classifying antigen-antibody complexes by their epitope maps in a high throughput screening workflow.

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Epitope mapping of 7S cashew antigen in complex with antibody by solution‐phase H/D exchange monitored by FT‐ICR mass spectrometry

Cited by 20 publications

References 51 publications

Cashew Nut Allergy: Clinical Relevance and Allergen Characterisation

Cashew Nut Allergy: Clinical Relevance and Allergen Characterisation

Can alternative epitope mapping approaches increase the impact of B‐cell epitopes in food allergy diagnostics?

Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding

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