Tropomyosin from tilapia (<i>Oreochromis mossambicus</i>) as an allergen

Liu, R.; Holck, Askild Lorentz; Yang, Eunjin; Liu, C.; Xue, Wei

doi:10.1111/cea.12056

Cited by 87 publications

(58 citation statements)

References 52 publications

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“…Herein, we have chosen tropomyosin sequences from four common edible fish species, Salmo salar , Epinephelus coioides , Siniperca chuatsi and Thunnus thynnus for comparison. To our knowledge, these fish tropomyosins have not been documented as ingestion-related allergens (however, see Liu et al which shows that tilapia tropomyosin may be related to autoimmune diseases [60]) and are thus valid candidates for such a homologous conversion. The advantage of homologous substitution is that MEM49 would retain its natural conformation and thereby ensuring a strong allergen-specific IgG response [61].…”

Section: Discussionmentioning

confidence: 99%

Immunization with Hypoallergens of Shrimp Allergen Tropomyosin Inhibits Shrimp Tropomyosin Specific IgE Reactivity

Wai

Leung

et al. 2014

PLoS ONE

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Designer proteins deprived of its IgE-binding reactivity are being sought as a regimen for allergen-specific immunotherapy. Although shrimp tropomyosin (Met e 1) has long been identified as the major shellfish allergen, no immunotherapy is currently available. In this study, we aim at identifying the Met e 1 IgE epitopes for construction of hypoallergens and to determine the IgE inhibitory capacity of the hypoallergens. IgE-binding epitopes were defined by three online computational models, ELISA and dot-blot using sera from shrimp allergy patients. Based on the epitope data, two hypoallergenic derivatives were constructed by site-directed mutagenesis (MEM49) and epitope deletion (MED171). Nine regions on Met e 1 were defined as the major IgE-binding epitopes. Both hypoallergens MEM49 and MED171 showed marked reduction in their in vitro reactivity towards IgE from shrimp allergy patients and Met e 1-sensitized mice, as well as considerable decrease in induction of mast cell degranulation as demonstrated in passive cutaneous anaphylaxis assay. Both hypoallergens were able to induce Met e 1-recognizing IgG antibodies in mice, specifically IgG2a antibodies, that strongly inhibited IgE from shrimp allergy subjects and Met e 1-sensitized mice from binding to Met e 1. These results indicate that the two designer hypoallergenic molecules MEM49 and MED171 exhibit desirable preclinical characteristics, including marked reduction in IgE reactivity and allergenicity, as well as ability to induce blocking IgG antibodies. This approach therefore offers promises for development of immunotherapeutic regimen for shrimp tropomyosin allergy.

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Section: Discussionmentioning

confidence: 99%

Immunization with Hypoallergens of Shrimp Allergen Tropomyosin Inhibits Shrimp Tropomyosin Specific IgE Reactivity

Wai

Leung

et al. 2014

PLoS ONE

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“…Vitellogenin, a fish yolk protein, has been identified as a food allergen in caviar from different fishes (85, 86). In 2013, tropomyosin, a filamentous muscle protein, was purified, cloned, and identified as a fish allergen in tilapia-sensitized patients (87). This tilapia allergen showed high homology (88%) to the human homolog.…”

Section: Fish Allergensmentioning

confidence: 99%

Fish Allergens at a Glance: Variable Allergenicity of Parvalbumins, the Major Fish Allergens

Swoboda²,

et al. 2014

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Fish is a common trigger of severe, food-allergic reactions. Only a limited number of proteins induce specific IgE-mediated immune reactions. The major fish allergens are the parvalbumins. They are members of the calcium-binding EF-hand protein family characterized by a conserved protein structure. They represent highly cross-reactive allergens for patients with specific IgE to conserved epitopes. These patients might experience clinical reactions with various fish species. On the other hand, some individuals have IgE antibodies directed against unique, species-specific parvalbumin epitopes, and these patients show clinical symptoms only with certain fish species. Furthermore, different parvalbumin isoforms and isoallergens are present in the same fish and might display variable allergenicity. This was shown for salmon homologs, where only a single parvalbumin (beta-1) isoform was identified as allergen in specific patients. In addition to the parvalbumins, several other fish proteins, enolases, aldolases, and fish gelatin, seem to be important allergens. New clinical and molecular insights advanced the knowledge and understanding of fish allergy in the last years. These findings were useful for the advancement of the IgE-based diagnosis and also for the management of fish allergies consisting of advice and treatment of fish-allergic patients.

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“…Proteins containing known epitopes are likely to be allergens, but absence of epitopes from a previously known allergenic homolog does not provide evidence that protein is safe. This remark is supported by the fact that the sequence of the allergenic fi sh tropomyosin Ore m 4.0101 [Liu et al, 2013] does not contain epitopes from shrimp tropomyosin. It could not be predicted as an allergen only on the basis of the presence of known epitopes from the set used in this work.…”

Section: Resultsmentioning

confidence: 89%

“…On the other hand, the number of protein sequences recorded in databases is growing rapidly and it is possible that the above-mentioned criteria will not be fulfi lled by new vertebrate tropomyosin sequences. The fi rst allergenic tropomyosin of vertebrate origin -protein from fi sh Oreochromis mossambicus (Ore m 4.0101, UniProt accession No: K4PEK4, Allergome code 10146) has been recently described [Liu et al, 2013] on the basis of experimental results. Some vertebrate tropomyosins (e.g.…”

Section: Introductionmentioning

confidence: 99%

The Occurrence of Sequences Identical with Epitopes from the Allergen Pen a 1.0102 Among Food and Non-Food Proteins

Minkiewicz¹,

Sokołowska²,

Darewicz³

2015

Pol. J. Food Nutr. Sci.

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Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen

Cited by 87 publications

References 52 publications

Immunization with Hypoallergens of Shrimp Allergen Tropomyosin Inhibits Shrimp Tropomyosin Specific IgE Reactivity

Immunization with Hypoallergens of Shrimp Allergen Tropomyosin Inhibits Shrimp Tropomyosin Specific IgE Reactivity

Fish Allergens at a Glance: Variable Allergenicity of Parvalbumins, the Major Fish Allergens

The Occurrence of Sequences Identical with Epitopes from the Allergen Pen a 1.0102 Among Food and Non-Food Proteins

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