Seafood allergy: A comprehensive review of fish and shellfish allergens

Ruethers, Thimo; Taki, Aya C.; Johnston, Elecia B.; Nugraha, Roni; Le, Thu Thao; Kalic, Tanja; McLean, Thomas R.; Kamath, Sandip D.; Lopata, Andreas L.

doi:10.1016/j.molimm.2018.04.008

Cited by 261 publications

(272 citation statements)

References 283 publications

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“…1 Tropomyosin exhibits a high degree of structural conservation between species. 2 Several studies have shown clinical cross-reactivity between crustaceans, mollusks, insects, mites and nematodes is due mainly to shared IgE (B-cell) epitopes of tropomyosin. [3][4][5] However, there is a lack of understanding whether this high degree of structural and sequence conservation among tropomyosins would also lead to cross-reactive T-cell epitopes.…”

Section: Introductionmentioning

confidence: 99%

Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin

Kamath

Scheiblhofer

Johnson

et al. 2020

Preprint

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Background: Tropomyosins are highly conserved proteins, an attribute that forms the molecular basis for their IgE antibody cross-reactivity. Despite structural similarities, their allergenicity varies greatly between ingested and inhaled invertebrate sources. In this study, we investigated the relationship between the structural stability of different tropomyosins, their endolysosomal degradation patterns and T-cell reactivity. Methods:We investigated the differences between four tropomyosins -the major shrimp allergen Pen m 1 and the minor allergens Der p 10 (dust mite), Bla g 7 (cockroach) and Ani s 3 (fish parasite) -in terms of IgE binding, structural stability, endolysosomal degradation and subsequent peptide generation,and T-cell cross-reactivity in a BALB/c murine model. Results:Despite their conserved primary structure and consequent IgE co-reactivity, the invertebrate tropomyosins displayed different protein stabilities. Pen m 1 and Ani s 3, but not Der p 10 and Bla g 7 elicited differential melting temperatures that were pH-dependent. Endolysosomal experiments demonstrated differential degradation, as a function of stability, generating different peptide repertoires.Pen m 1 T-cell clones, with specificity for sequences highly conserved in all four tropomyosins, did not proliferate with Der p 10, Bla g 7 and Ani s 3, indicating that these peptides were not naturally produced for other invertebrate tropomyosins. Conclusions:Our data suggest that, although invertebrate tropomyosins exhibit a high degree of IgE cross-reactivity due to conserved B-cell epitopes, they do not necessarily share identical cross-reactive T-cell epitopes. This is likely due to differential endolysosomal processing as a function of different structural stabilities. Word Count: 3619 14.Kavan D, Man P. MSTools-Web based application for visualization and presentation of HXMS data. Int J Mass Spectrom. 2011;302(1):53-58. 15.Reese G, Viebranz J, Leong-Kee SM, et al. Reduced allergenic potency of VR9-1, a mutant of the major shrimp allergen Pen a 1 (tropomyosin).

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Section: Introductionmentioning

confidence: 99%

Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin

Kamath

Scheiblhofer

Johnson

et al. 2020

Preprint

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“…IgE‐mediated fish allergy is typically a lifelong disease, with sensitization rates of up to 3% in the general population and up to 8% among fish processing workers . The diagnosis of fish allergy is often confirmed by in vivo allergy skin prick tests (SPT), a relatively non‐invasive point of care testing, providing immediate results. Commercial fish extracts for SPT for approximately 30 (mostly European species) are available, while over 1000 different fish species are consumed worldwide.…”

Section: Introductionmentioning

confidence: 99%

Variability of allergens in commercial fish extracts for skin prick testing

Ruethers

Taki

Nugraha

et al. 2019

Allergy

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Background: Commercial allergen extracts for allergy skin prick testing (SPT) are widely used for diagnosing fish allergy. However, there is currently no regulatory requirement for standardization of protein and allergen content, potentially impacting the diagnostic reliability of SPTs. We therefore sought to analyse commercial fish extracts for the presence and concentration of fish proteins and in vitro IgE reactivity using serum from fish-allergic patients.Methods: Twenty-six commercial fish extracts from five different manufacturers were examined. The protein concentrations were determined, protein compositions analysed by mass spectrometry, followed by SDS-PAGE and subsequent immunoblotting with antibodies detecting 4 fish allergens (parvalbumin, tropomyosin, aldolase and collagen). IgE-reactive proteins were identified using serum from 16 children with confirmed IgE-mediated fish allergy, with focus on cod, tuna and salmon extracts. Results:The total protein, allergen concentration and IgE reactivity of the commercial extracts varied over 10-fold between different manufacturers and fish species. The major fish allergen parvalbumin was not detected by immunoblotting in 6/26 extracts. In 7/12 extracts, five known fish allergens were detected by mass spectrometry. For cod and tuna, almost 70% of patients demonstrated the strongest IgE reactivity to collagen, tropomyosin, aldolase A or β-enolase but not parvalbumin.

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“…TnC is an Arthropoda panallergen and has been characterized as a minor allergen in shrimps, 3 whereas it is an important cockroach allergen (Bla g6, Per a6). TnC is an Arthropoda panallergen and has been characterized as a minor allergen in shrimps, 3 whereas it is an important cockroach allergen (Bla g6, Per a6).…”

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“…In our 2 patients, IgE binding was shown towards TnC and ESE in TML, and towards CAL in both TML and TMF. TnC is an Arthropoda panallergen and has been characterized as a minor allergen in shrimps, 3 whereas it is an important cockroach allergen (Bla g6, Per a6). 4 Bla g6 from Blattella germanica showed a 78.84% identity with TnC from TM (https ://www.unipr ot.org/blast ).…”

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confidence: 99%

The cockroach allergen‐like protein is involved in primary respiratory and food allergy to yellow mealworm (Tenebrio molitor)

Nebbia

Lamberti

Giorgis

et al. 2019

Clin Experimental Allergy

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Insects have been proposed as a high quality, efficient and sustainable alternative protein source for humans and animals, and a vast selection of edible products is currently available in many European countries. However, respiratory allergy among professional and domestic breeders and food allergy among consumers are known. 1,2We here report the case of 2 patients (Pt#1 and Pt#2, both male, 24 and 27 years old, respectively) employed in the production of insect flour made of yellow mealworm larvae (Tenebrio molitor larvae, TML) and black soldier fly larvae (Hermetia illucens larvae, HIL).The patients did not show the previous history of food or respiratory allergies. In the same factory, a total of ten workers handled TML, eight out of ten without developing any symptom. The first symptoms of the 2 patients (rhinoconjunctivitis, itching and contact erythema) appeared after some weeks of repetitive exposure to TML. They did not report any symptoms when exposed to HIL.The symptoms were particularly severe during the sifting of TML from their faeces (TMF), and when the patients entered the rearing room after the sifting operation, they disappeared after 24 hours.The sensitization therefore presumably occurred through a percutaneous route and/or by inhalation. After developing symptoms, Pt#1 continued to work using adequate protection devices, while Pt#2 left the job. The 2 patients were used to eat such edible insects as the greater wax moth, crickets and HI. They experienced an oral allergy syndrome (OAS) characterized by oral pruritus and tightness in the throat, as soon as they start eating for the first time a TML hamburger. Symptoms recovered spontaneously in about 40 minutes. Following this episode, they continued to tolerate other edible insects, but never tried to taste TML again and refused to undergo provocation test.In order to characterize the patients' allergic profile, we performed: skin prick tests (SPTs) with a standard battery of inhalant and food allergens, specific IgE for TM, Der p10, Dermatophagoides pteronyssinus, Dermatophagoides farinae and Prawn (ImmunoCap Thermo Fisher Scientific Inc) and basophil activation test (BAT) with TML and TMF protein extracts. Immunoblot analyses of both protein extracts and LC-MS/MS analysis followed by protein database screening were performed in order to identify the allergens involved in the TM sensitization (see Appendix S1).The SPTs with inhalant and food allergens were negative in both patients, except for Grass in Pt#1 and Alternaria in Pt#2. Specific TM IgEs were present in both patients (21.00 and 10.63 kU A /L, respectively), while no specific IgEs were found for house dust mites, Prawn and Der p10. BAT were positive in both subjects for TMF and TML (Figure 1).Immunoblotting showed a 15 kDa reactive band in both the TML and TMF extracts, when incubated with both patients' sera ( Figure 2, panel A). Three additional aspecific bands were also detected in the healthy control patients' serum pool, but only in the TML extract ( Figure 2). The cockroach all...

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Seafood allergy: A comprehensive review of fish and shellfish allergens

Cited by 261 publications

References 283 publications

Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin

Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin

Variability of allergens in commercial fish extracts for skin prick testing

The cockroach allergen‐like protein is involved in primary respiratory and food allergy to yellow mealworm (Tenebrio molitor)

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