Are dust mite allergens more abundant and/or more stable than other  Dermatophagoides pteronyssinus  proteins?

Ogburn, Ryenne N.; Randall, Thomas A.; Xu, Yingrong; Roberts, Julia H.; Mebrahtu, Betelihem; Karnuta, Jaret M.; Rider, S. Dean; Kissling, Grace E.; London, Robert E.; Pomés, Anna; Arlian, Larry G.; Fitzgerald, Michael C.; Mueller, Geoffrey A.

doi:10.1016/j.jaci.2016.08.016

Cited by 18 publications

(43 citation statements)

References 17 publications

(9 reference statements)

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“…Perhaps the best‐known example is the house dust mite allergen, Der p 1, a proteolytic enzyme capable of cleaving CD23 (FcεRII, the low‐affinity IgE receptor) and CD25 (IL‐2 receptor α‐chain) expressed on the surface of some B cells, resulting in dysregulation of the immune response and induced production of IgE . The allergenicity of these proteins is not limited to their enzymatic activity, however, and both relative abundance and stability have been cited as of equal importance . Pyruvate kinases, enolases and aldolases have been shown to be abundant but heat‐labile proteins in fish and shrimp …”

Section: Discussionmentioning

confidence: 99%

“…36 The allergenicity of these proteins is not limited to their enzymatic activity, however, and both relative abundance and stability have been cited as of equal importance. 37,38 Pyruvate kinases, enolases and aldolases have been shown to be abundant but heat-labile proteins in fish 22 and shrimp. 21 The objective of this work was to identify whether cross-reactive IgE-binding proteins were present in C and fish, which could explain the frequency of sensitizations to these foods.…”

Section: Discussionmentioning

confidence: 99%

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Serum IgE cross‐reactivity between fish and chicken meats in dogs

Bexley

Kingswell

Olivry

2018

Veterinary Dermatology

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Background In humans, a cross‐reactive clinical allergy has been reported between three chicken and fish meat proteins: beta‐enolase, aldolase A and parvalbumin. Objective To evaluate if IgE cross‐reactivity between chicken and fish also existed in the dog. Animals Sera from dogs with suspected allergic skin disease and with IgE against chicken and fish. Methods and materials Sera were analysed by ELISA and immunoblotting with chicken, white fish (haddock and cod) and salmon extracts. Reciprocal inhibition ELISAs and inhibition immunoblots were then performed. Protein sequencing of bands identified on multiple extracts was determined by mass spectrometry. Results Out of 53 archived canine sera tested by ELISA against chicken, white fish or salmon, 15 (28%), 12 (23%) and 26 (49%), respectively, had elevated IgE against one, two or all three of these extracts. Seven of the triple‐reactive sera were subjected to reciprocal inhibition ELISAs. A >50% inhibition was found between chicken–fish, chicken–salmon and fish–salmon in seven, four and five of seven dogs, respectively. Immunoblotting identified multiple IgE‐binding proteins of identical molecular weights in the three extracts; these were partially to fully cross‐reactive by inhibition immunoblotting. Mass spectrometry identified nine cross‐reactive proteins as: pyruvate kinase, creatine kinase, alpha‐actin, glyceraldehyde‐3‐phosphate dehydrogenase, beta‐enolase, aldolase, malate dehydrogenase, lactate dehydrogenase and triose‐phosphate isomerase 1. All of these have been reported previously as fish, shellfish and/or chicken allergens for humans. Conclusions and clinical importance Whether any of these newly identified IgE cross‐reactive chicken–fish allergens is the cause of clinical allergy needs to be determined in dogs reacting to at least two of these common food sources.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Serum IgE cross‐reactivity between fish and chicken meats in dogs

Bexley

Kingswell

Olivry

2018

Veterinary Dermatology

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“…Correlation between protein abundance and RNA-Seq data has been established, with some post-transcriptional cellular processes affecting this interpretation [63]. A study on European HDM allergen transcript levels using RNA-Seq data concluded that allergens have a higher level of abundance than nonallergens [64]; and their results were found to be to relatively similar to homologues identified in american HDM from a different study [65]. In particular, these dust mite allergen studies indicate that there is substantial correlation between RNA-Seq dependent abundance levels and a protein's allergen status.…”

Section: Discussionmentioning

confidence: 99%

Novel allergen discovery through comprehensivede novotranscriptomic analyses of 5 shrimp species

Karnaneedi

Huerlimann

Johnston

et al. 2020

Preprint

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Shellfish allergy affects up to 2% of the world's population and persists for life in most patients. The diagnosis of a shellfish allergy, in particular shrimp, is however often challenging due to the similarity of allergenic proteins in other invertebrates. Despite the clinical importance, the complete allergen repertoire of allergy-causing shrimps remains unclear. Here we mine the complete transcriptome of five frequently consumed shrimp species to identify and compare allergens with all known allergen sources. The transcriptomes were assembled de novo from raw RNA-Seq data of the whiteleg shrimp (Litopenaeus vannamei), black tiger shrimp (Penaeus monodon), banana shrimp (Fenneropenaeus merguiensis), king shrimp (Melicertus latisulcatus), and endeavour shrimp (Metapenaeus endeavouri). Trinity was used to assemble the transcriptome, and Transrate and BUSCO applied to verify the assembly. Blast search with the two major allergen databases, WHO/IUIS Allergen Nomenclature and AllergenOnline, successfully identified all seven known crustacean allergens. Salmon was utilised to measure their relative abundance, demonstrating sarcoplasmic calcium-binding protein, arginine kinase and myosin light chain as highly abundant allergens. In addition, the analyses revealed up to 40 unreported allergens in different shrimp species, including heat shock protein (HSP), alpha-tubulin, chymotrypsin,cyclophilin, beta-enolase, aldolase A, and glyceraldehyde-3-phosphate dehydrogenase (G3PD). Multiple sequence alignment, conducted in Jalview 2.1 with Clustal Omega, demonstrated high homology with allergens from other invertebrates including mites and cockroaches. This first transcriptomic analyses of allergens in a major food source provides a valuable genomic resource for investigating shellfish allergens, comparing invertebrate allergens and developing improved diagnostics and novel immunotherapeutics for food allergy. EJ and AL conceptualized the research objectives. SK, RH, EJ, RN, AT, and AL designed the research methods. RH, NW, and DJ provided the shrimp samples, conducted the RNA extraction and funded the RNA sequencing. SK and RH carried out the de novo transcriptome assembly, transcriptome quality check, BLAST search and relative abundance estimation. SK and RN constructed the allergen reference database and the molecular phylogenetic tree of known shellfish allergens. SK, RN, EJ, TR, AT, SDK, and AL determined the relevant allergens identified within the shrimp transcriptomes and the downstream analyses of these potential allergens. SK, RN, TR, RH, and AL designed the figures and tables. SK and AL wrote the first draft. All authors contributed to manuscript editing and revision.

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“…Anecdotal evidence suggested that abundance and stability could be two such properties, but no rigorous statistical comparisons were available until a study of the dust mite Dermatophagoides pteronyssinus (Dp) combined transcriptomics with proteomics. 1 The Dp study measured transcription levels as a proxy for protein abundance and correlated the results with proteome-wide stability measurements using mass spectrometry. It was found that the mite allergens were as a population more stable and more highly expressed than Dp non-allergens.…”

mentioning

confidence: 99%

Are allergens more abundant and/or more stable than other proteins in pollens and dust?

Cabrera

Randall

Ogburn

et al. 2019

Allergy

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To the Editor, The human exposome contains millions of proteins, yet only a select few consistently become allergens. This has led to speculation that there are intrinsic factors which differentiate allergens from non-allergens. Anecdotal evidence suggested that abundance and stability could be two such properties, but no rigorous statistical comparisons were available until a study of the dust mite Dermatophagoides pteronyssinus (Dp) combined transcriptomics with proteomics. 1 The Dp study measured transcription levels as a proxy for protein abundance and correlated the results with proteome-wide stability measurements using mass spectrometry. It was found that the mite allergens were as a population more stable and more highly expressed than Dp non-allergens. Dp was a good model

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Are dust mite allergens more abundant and/or more stable than other Dermatophagoides pteronyssinus proteins?

Cited by 18 publications

References 17 publications

Serum IgE cross‐reactivity between fish and chicken meats in dogs

Serum IgE cross‐reactivity between fish and chicken meats in dogs

Novel allergen discovery through comprehensivede novotranscriptomic analyses of 5 shrimp species

Are allergens more abundant and/or more stable than other proteins in pollens and dust?

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