Differential IgE binding to isoallergens from Asian seabass (Lates calcarifer) in children and adults

Sharp, Michael F.; Kamath, Sandip D.; Koeberl, Martina; Jerry, Dean R.; O’Hehir, Robyn E; Campbell, Dianne E.; Lopata, Andreas L.

doi:10.1016/j.molimm.2014.05.010

Cited by 22 publications

(14 citation statements)

References 31 publications

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“…Aalberse (22) reviewed potentially cross-reactive structures of known allergens and noted that proteins with >50% identity throughout the length of the protein compared to an allergen are likely cross-reactive. However, some recent studies (19, 23, 24) demonstrated that this predictive value is only useful to predict the allergenicity of new protein of unknown structure but is not accurate to predict cross-reactivity. This is of particular importance for invertebrate tropomyosin, which shares over 50% of amino acid identify with human tropomyosin.…”

Section: Introductionmentioning

confidence: 99%

Conservation Analysis of B-Cell Allergen Epitopes to Predict Clinical Cross-Reactivity Between Shellfish and Inhalant Invertebrate Allergens

et al. 2019

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Understanding and predicting an individual's clinical cross-reactivity to related allergens is a key to better management, treatment and progression of novel therapeutics for food allergy. In food allergy, clinical cross-reactivity is observed in patients reacting to unexpected allergen sources containing the same allergenic protein or antibody binding patches (epitopes), often resulting in severe allergic reactions. Shellfish allergy affects up to 2% of the world population and persists for life in most patients. The diagnosis of shellfish allergy is however often challenging due to reported clinical cross-reactivity to other invertebrates including mites and cockroaches. Prediction of cross-reactivity can be achieved utilizing an in-depth analysis of a few selected IgE-antibody binding epitopes. We combined available experimentally proven IgE-binding epitopes with informatics-based cross-reactivity prediction modeling to assist in the identification of clinical cross-reactive biomarkers on shellfish allergens. This knowledge can be translated into prevention and treatment of allergic diseases. To overcome the problem of predicting IgE cross-reactivity of shellfish allergens we developed an epitope conservation model using IgE binding epitopes available in the Immune Epitope Database and Analysis Resource (http://www.iedb.org/). We applied this method to a set of four different shrimp allergens, and successfully identified several non-cross-reactive as well as cross-reactive epitopes, which have been experimentally established to cross-react. Based on these findings we suggest that this method can be used for advanced component-resolved-diagnosis to identify patients sensitized to a specific shellfish group and distinguish from patients with extensive cross-reactivity to ingested and inhaled allergens from invertebrate sources.

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Section: Introductionmentioning

confidence: 99%

Conservation Analysis of B-Cell Allergen Epitopes to Predict Clinical Cross-Reactivity Between Shellfish and Inhalant Invertebrate Allergens

et al. 2019

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“…PV has been extensively studied in bony fish including in Atlantic cod (Gadus morhua) [28,29,[33][34][35][36][37], Alaska Pollack (Theragra chalcogramma) [38,39], common carp (Cyprinus carpio) [24,30,31,37,40], silver carp (Hypophthalmichthy molitrix) [41], Atlantic salmon (Salmo salar) [39,[42][43][44][45][46] and recently Asian seabass (Lates calcarifer) [47,48]. PV has been extensively studied in bony fish including in Atlantic cod (Gadus morhua) [28,29,[33][34][35][36][37], Alaska Pollack (Theragra chalcogramma) [38,39], common carp (Cyprinus carpio) [24,30,31,37,40], silver carp (Hypophthalmichthy molitrix) [41], Atlantic salmon (Salmo salar) [39,[42][43][44][45][46] and recently Asian seabass (Lates calcarifer) [47,48].…”

Section: Parvalbuminmentioning

confidence: 99%

“…In comparison, studies on PV from cartilaginous fish are limited to leopard shark [25], red stingray [26], Atlantic stingray [49] and thornback ray [50]. Some fish species seem also to express multiple isoforms of b-PV such as b1 and b2 seen in barramundi and isoforms 1 to 9 in zebrafish [47,51]. Some fish species seem also to express multiple isoforms of b-PV such as b1 and b2 seen in barramundi and isoforms 1 to 9 in zebrafish [47,51].…”

Section: Parvalbuminmentioning

confidence: 99%

“…Characterization. PV has been extensively studied in bony fish including in Atlantic cod (Gadus morhua) [28,29,[33][34][35][36][37], Alaska Pollack (Theragra chalcogramma) [38,39], common carp (Cyprinus carpio) [24,30,31,37,40], silver carp (Hypophthalmichthy molitrix) [41], Atlantic salmon (Salmo salar) [39,[42][43][44][45][46] and recently Asian seabass (Lates calcarifer) [47,48]. In comparison, studies on PV from cartilaginous fish are limited to leopard shark [25], red stingray [26], Atlantic stingray [49] and thornback ray [50].…”

Section: Parvalbuminmentioning

confidence: 99%

“…b-parvalbumin is more abundant in bony fish and appears to be responsible for the majority of allergic reactions, while the aisoform seems to be predominant in cartilaginous fish [25,26]. Some fish species seem also to express multiple isoforms of b-PV such as b1 and b2 seen in barramundi and isoforms 1 to 9 in zebrafish [47,51].…”

Section: Parvalbuminmentioning

confidence: 99%

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Allergenicity of bony and cartilaginous fish – molecular and immunological properties

Stephen

Sharp

Ruethers

et al. 2017

Clin Experimental Allergy

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Allergy to bony fish is common and probably increasing world-wide. The major heat-stable pan-fish allergen, parvalbumin (PV), has been identified and characterized for numerous fish species. In contrast, there are very few reports of allergic reactions to cartilaginous fish despite widespread consumption. The molecular basis for this seemingly low clinical cross-reactivity between these two fish groups has not been elucidated. PV consists of two distinct protein lineages, α and β. The α-lineage of this protein is predominant in muscle tissue of cartilaginous fish (Chondrichthyes), while β-PV is abundant in muscle tissue of bony fish (Osteichthyes). The low incidence of allergic reactions to ingested rays and sharks is likely due to the lack of molecular similarity, resulting in reduced immunological cross-reactivity between the two PV lineages. Structurally and physiologically, both protein lineages are very similar; however, the amino acid homology is very low with 47-54%. Furthermore, PV from ancient fish species such as the coelacanth demonstrates 62% sequence homology to leopard shark α-PV and 70% to carp β-PV. This indicates the extent of conservation of the PV isoforms lineages across millennia. This review highlights prevalence data on fish allergy and sensitization to fish, and details the molecular diversity of the two protein lineages of the major fish allergen PV among different fish groups, emphasizing the immunological and clinical differences in allergenicity.

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Extract-Based and Molecular Diagnostics in Fish Allergy

Kuehn

Radauer

Lopata

et al. 2017

Molecular Allergy Diagnostics

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Differential IgE binding to isoallergens from Asian seabass (Lates calcarifer) in children and adults

Cited by 22 publications

References 31 publications

Conservation Analysis of B-Cell Allergen Epitopes to Predict Clinical Cross-Reactivity Between Shellfish and Inhalant Invertebrate Allergens

Conservation Analysis of B-Cell Allergen Epitopes to Predict Clinical Cross-Reactivity Between Shellfish and Inhalant Invertebrate Allergens

Allergenicity of bony and cartilaginous fish – molecular and immunological properties

Extract-Based and Molecular Diagnostics in Fish Allergy

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