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Seafood allergy: Allergen, epitope mapping and immunotherapy strategy

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References

  • Abramovitch, J. B., S. Kamath, N. Varese, C. Zubrinich, A. L. Lopata, R. E. O’Hehir, and J. M. Rolland. 2013. IgE reactivity of blue swimmer crab (Portunus pelagicus) tropomyosin, Por p 1, and other allergens; cross-reactivity with black tiger prawn and effects of heating. PLoS One 8 (6):e67487. doi: 10.1371/journal.pone.0067487.
  • Abramovitch, J. B., A. L. Lopata, R. E. O’Hehir, and J. M. Rolland. 2017. Effect of thermal processing on T cell reactivity of shellfish allergens – Discordance with IgE reactivity. PLoS One 12 (3):e0173549. doi: 10.1371/journal.pone.0173549.
  • Albuhairi, S., and R. Rachid. 2020. Novel therapies for treatment of food allergy. Immunology and Allergy Clinics of North America 40 (1):175–86. doi: 10.1016/j.iac.2019.09.007.
  • Ali, A. H., and M. Rosmilah. 2019. Effects of food processing on the stability and quality of shellfish allergens. Journal of US-China Medical Science 16:149–63.
  • Alsailawi, H. A., R. Misnan, and M. Mudhafar. 2021. Major and minor allergen ige reactivity of purple mud crab (Scylla tranquebarica) against A cross-reactive allergen in crustacean and molluscs in patients with A seafood allergy. Research Journal of Pharmacy and Technology 14 (1):239–44. doi: 10.5958/0974-360X.2021.00042.1.
  • An, S., L. Chen, C. Long, X. Liu, X. Xu, X. Lu, M. Rong, Z. Liu, and R. Lai. 2013. Dermatophagoides farinae allergens diversity identification by proteomics. Molecular & Cellular Proteomics 12 (7):1818–28. doi: 10.1074/mcp.M112.027136.
  • Arif, S. H. 2009. A Ca2+‐binding protein with numerous roles and uses: Parvalbumin in molecular biology and physiology. BioEssays 31 (4):410–21. doi: 10.1002/bies.200800170.
  • Asero, R. 2005. Lack of de novo sensitization to tropomyosin in a group of mite-allergic patients treated by house dust mite-specific immunotherapy. International Archives of Allergy and Immunology 137 (1):62–5. doi: 10.1159/000085105.
  • Asero, R., L. Antonicelli, A. Arena, L. Bommarito, B. Caruso, M. Crivellaro, M. De Carli, E. Della Torre, F. Della Torre, E. Heffler, et al. 2009. EpidemAAITO: Features of food allergy in Italian adults attending allergy clinics: A multi-centre study. Clinical and Experimental Allergy 39 (4):547–55. doi: 10.1111/j.1365-2222.2008.03167.x.
  • Asero, R., G. Mistrello, D. Roncarolo, M. Casarini, and P. Falagiani. 1999. True monosensitivity to a tropical sole. Allergy (Copenhagen) 54 (11):1228–9. doi: 10.1034/j.1398-9995.1999.00359.x.
  • Asero, R., V. Pravettoni, E. Scala, and D. Villalta. 2020. House dust mite-shrimp allergen interrelationships. Current Allergy and Asthma Reports 20 (4):9. doi: 10.1007/s11882-020-0902-2.
  • Asturias, J. A., E. Eraso, M. C. Arilla, N. Gómez-Bayón, F. Inácio, and A. Martínez. 2002. Cloning, isolation, and IgE-binding properties of Helix aspersa (brown garden snail) tropomyosin. International Archives of Allergy and Immunology 128 (2):90–6. doi: 10.1159/000059398.
  • Ayuso, R., G. Grishina, L. Bardina, T. Carrillo, C. Blanco, M. D. Ibáñez, H. A. Sampson, and K. Beyer. 2008. Myosin light chain is a novel shrimp allergen, Lit v 3. The Journal of Allergy and Clinical Immunology 122 (4):795–802. doi: 10.1016/j.jaci.2008.07.023.
  • Ayuso, R., G. Grishina, M. D. Ibáñez, C. Blanco, T. Carrillo, R. Bencharitiwong, S. Sánchez, A. Nowak-Wegrzyn, and H. A. Sampson. 2009. Sarcoplasmic calcium-binding protein is an EF-hand-type protein identified as a new shrimp allergen. The Journal of Allergy and Clinical Immunology 124 (1):114–20. doi: 10.1016/j.jaci.2009.04.016.
  • Ayuso, R., S. B. Lehrer, and G. Reese. 2002. Identification of continuous, allergenic regions of the major shrimp allergen Pen a 1 (Tropomyosin). International Archives of Allergy and Immunology 127 (1):27–37. doi: 10.1159/000048166.
  • Ayuso, R., S. Sánchez-Garcia, J. Lin, Z. Fu, M. D. Ibáñez, T. Carrillo, C. Blanco, M. Goldis, L. Bardina, J. Sastre, et al. 2010. Greater epitope recognition of shrimp allergens by children than by adults suggests that shrimp sensitization decreases with age. The Journal of Allergy and Clinical Immunology 125 (6):1286–93.e3. doi: 10.1016/j.jaci.2010.03.010.
  • Barman, M., H. Rabe, B. Hesselmar, S. Johansen, A. S. Sandberg, and A. E. Wold. 2020. Cord blood levels of EPA, a marker of fish intake, correlate with infants’ T-and B-lymphocyte phenotypes and risk for allergic disease. Nutrients 12 (10):3000. doi: 10.3390/nu12103000.
  • Barshow, S. M., M. D. Kulis, W. A. Burks, and E. H. Kim. 2021. Mechanisms of oral immunotherapy. Clinical and Experimental Allergy 51 (4):527–35. doi: 10.1111/cea.13824.
  • Bauermeister, K., A. Wangorsch, L. P. Garoffo, A. Reuter, A. Conti, S. L. Taylor, J. Lidholm, A. M. Dewitt, E. Enrique, S. Vieths, et al. 2011. Generation of a comprehensive panel of crustacean allergens from the North Sea Shrimp Crangon crangon. Molecular Immunology 48 (15-16):1983–92. doi: 10.1016/j.molimm.2011.06.216.
  • Beale, J. E., M. F. Jeebhay, and A. L. Lopata. 2009. Characterisation of purified parvalbumin from five fish species and nucleotide sequencing of this major allergen from Pacific pilchard, Sardinops sagax. Molecular Immunology 46 (15):2985–93. doi: 10.1016/j.molimm.2009.06.018.
  • Binder, M., V. Mahler, B. Hayek, W. R. Sperr, M. Schöller, S. Prozell, G. Wiedermann, P. Valent, R. Valenta, and M. Duchêne. 2001. Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen. Journal of Immunology 167 (9):5470–7. doi: 10.4049/jimmunol.167.9.5470.
  • Bobolea, I., P. Barranco, C. Pastor-Vargas, V. Iraola, F. Vivanco, and S. Quirce. 2011. Arginine kinase from the cellar spider (Holocnemus pluchei): A new asthma-causing allergen. International Archives of Allergy and Immunology 155 (2):180–6. doi: 10.1159/000319822.
  • Brassea-Estardante, H. A., O. Martínez-Cruz, J. L. Cárdenas-López, K. D. García-Orozco, A. Ochoa-Leyva, and A. A. López-Zavala. 2022. Identification of arginine kinase as an allergen of brown crab, Callinectes bellicosus, and in silico analysis of IgE-binding epitopes. Molecular Immunology 143:147–56. doi: 10.1016/j.molimm.2022.01.013.
  • Bugajska-Schretter, A., L. Elfman, T. Fuchs, S. Kapiotis, H. Rumpold, R. Valenta, and S. Spitzauer. 1998. Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion. The Journal of Allergy and Clinical Immunology 101 (1 Pt 1):67–74. doi: 10.1016/S0091-6749(98)70195-2.
  • Bugajska-Schretter, A., M. Grote, L. Vangelista, P. Valent, W. R. Sperr, H. Rumpold, A. Pastore, R. Reichelt, R. Valenta, and S. Spitzauer. 2000. Purification, biochemical, and immunological characterisation of a major food allergen: Different immunoglobulin E recognition of the apo-and calcium-bound forms of carp parvalbumin. Gut 46 (5):661–9. doi: 10.1136/gut.46.5.661.
  • Buyuktiryaki, B., M. Masini, F. Mori, S. Barni, G. Liccioli, L. Sarti, L. Lodi, M. Giovannini, G. Du Toit, A. L. Lopata, et al. 2021. IgE-mediated fish allergy in children. Medicina 57 (1):76. doi: 10.3390/medicina57010076.
  • Cai, Q. F., G. M. Liu, T. Li, K. Hara, X. C. Wang, W. J. Su, and M. J. Cao. 2010. Purification and characterization of parvalbumins, the major allergens in red stingray (Dasyatis akajei). Journal of Agricultural and Food Chemistry 58 (24):12964–9. doi: 10.1021/jf103316h.
  • Carrera, M., Á. González-Fernández, S. Magadán, J. Mateos, L. Pedrós, I. Medina, and J. M. Gallardo. 2019. Molecular characterization of B-cell epitopes for the major fish allergen, parvalbumin, by shotgun proteomics, protein-based bioinformatics and IgE-reactive approaches. Journal of Proteomics 200:123–33. doi: 10.1016/j.jprot.2019.04.005.
  • Carrera, M., M. Pazos, and M. Gasset. 2020. Proteomics-based methodologies for the detection and quantification of seafood allergens. Foods 9 (8):1134. doi: 10.3390/foods9081134.
  • Celi, G., I. Brusca, E. Scala, D. Villalta, E. Pastorello, L. Farioli, G. Cortellini, G. Deleonardi, P. Galati, L. Losappio, et al. 2020. House dust mite allergy and shrimp allergy: A complex interaction. European Annals of Allergy and Clinical Immunology 52 (5):205–9. doi: 10.23822/EurAnnACI.1764-1489.108.
  • Chao, E., H. W. Kim, and D. L. Mykles. 2010. Cloning and tissue expression of eleven troponin-C isoforms in the American lobster, Homarus americanus. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology 157 (1):88–101. doi: 10.1016/j.cbpb.2010.05.007.
  • Chen, H. L., M. J. Cao, Q. F. Cai, W. J. Su, H. Y. Mao, and G. M. Liu. 2013. Purification and characterisation of sarcoplasmic calcium-binding protein, a novel allergen of red swamp crayfish (Procambarus clarkii). Food Chemistry 139 (1-4):213–23. doi: 10.1016/j.foodchem.2013.01.119.
  • Chen, H. L., H. Y. Mao, M. J. Cao, Q. F. Cai, W. J. Su, Y. X. Zhang, and G. M. Liu. 2013. Purification, physicochemical and immunological characterization of arginine kinase, an allergen of crayfish (Procambarus clarkii). Food and Chemical Toxicology 62:475–84. doi: 10.1016/j.fct.2013.09.014.
  • Cheng, J. H., H. Wang, and D. W. Sun. 2022. An overview of tropomyosin as an important seafood allergen: Structure, cross-reactivity, epitopes, allergenicity, and processing modifications. Comprehensive Reviews in Food Science and Food Safety 21 (1):127–47. doi: 10.1111/1541-4337.12889.
  • Chuang, J. G., S. N. Su, B. L. Chiang, H. J. Lee, and L. P. Chow. 2010. Proteome mining for novel IgE‐binding proteins from the German cockroach (Blattella germanica) and allergen profiling of patients. Proteomics 10 (21):3854–67. doi: 10.1002/pmic.201000348.
  • Connett, G. J., I. Gerez, E. A. Cabrera-Morales, A. Yuenyongviwat, J. Ngamphaiboon, P. Chatchatee, P. Sangsupawanich, S.-E. Soh, G.-C. Yap, L. P.-C. Shek, et al. 2012. A population-based study of fish allergy in the Philippines, Singapore and Thailand. International Archives of Allergy and Immunology 159 (4):384–90. doi: 10.1159/000338940.
  • Cortellini, G., I. Spadolini, A. Santucci, V. Cova, C. Conti, A. Corvetta, and G. Passalacqua. 2011. Improvement of shrimp allergy after sublingual immunotherapy for house dust mites: A case report. European Annals of Allergy and Clinical Immunology 43 (5):162–4.
  • Das Dores, S., C. Chopin, A. Romano, A.-V. Galland-Irmouli, D. Quaratino, C. Pascual, J. Fleurence, and J.-L. Gueant. 2002. IgE‐binding and cross‐reactivity of a new 41 kDa allergen of codfish. Allergy 57 (s72):84–7. doi: 10.1034/j.1398-9995.57.s72.6.x.
  • Dasanayaka, B. P., Z. Li, S. N. Pramod, Y. Chen, M. U. Khan, and H. Lin. 2022. A review on food processing and preparation methods for altering fish allergenicity. Critical Reviews in Food Science and Nutrition 62 (7):1951–70. doi: 10.1080/10408398.2020.1848791.
  • Daul, C. B., M. Slattery, G. Reese, and S. B. Lehrer. 1994. Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. International Archives of Allergy and Immunology 105 (1):49–55. doi: 10.1159/000236802.
  • Davis, C. M., R. S. Gupta, O. N. Aktas, V. Diaz, S. D. Kamath, and A. L. Lopata. 2020. Clinical management of seafood allergy. The Journal of Allergy and Clinical Immunology. In Practice 8 (1):37–44. doi: 10.1016/j.jaip.2019.10.019.
  • Dong, X., and V. Raghavan. 2022. Recent advances of selected novel processing techniques on shrimp allergenicity: A review. Trends in Food Science & Technology 124:334–44. doi: 10.1016/j.tifs.2022.04.024.
  • Dong, X., J. Wang, and V. Raghavan. 2020. Effects of high-intensity ultrasound processing on the physiochemical and allergenic properties of shrimp. Innovative Food Science & Emerging Technologies 65:102441. doi: 10.1016/j.ifset.2020.102441.
  • Ebo, D. G., A. Kuehn, C. H. Bridts, C. Hilger, F. Hentges, and W. J. Stevens. 2010. Monosensitivity to pangasius and tilapia caused by allergens other than parvalbumin. Journal of Investigational Allergology and Clinical Immunology 20 (1):84–8.
  • Fang, L., G. Li, J. Zhang, R. Gu, M. Cai, and J. Lu. 2019. Identification and mutational analysis of continuous, immunodominant epitopes of the major oyster allergen Cra g 1. Clinical Immunology 201:20–9. doi: 10.1016/j.clim.2019.02.008.
  • Francis, F., V. Doyen, F. Debaugnies, G. Mazzucchelli, R. Caparros, T. Alabi, C. Blecker, E. Haubruge, and F. Corazza. 2019. Limited cross reactivity among arginine kinase allergens from mealworm and cricket edible insects. Food Chemistry 276:714–8. doi: 10.1016/j.foodchem.2018.10.082.
  • Freidl, R., A. Gstoettner, U. Baranyi, I. Swoboda, F. Stolz, M. Focke-Tejkl, T. Wekerle, R. van Ree, R. Valenta, and B. Linhart. 2017. Blocking antibodies induced by immunization with a hypoallergenic parvalbumin mutant reduce allergic symptoms in a mouse model of fish allergy. The Journal of Allergy and Clinical Immunology 139 (6):1897–905.e1. doi: 10.1016/j.jaci.2016.10.018.
  • Fu, L., J. Wang, S. Ni, C. Wang, and Y. Wang. 2018. Identification of allergenic epitopes and critical amino acids of major allergens in Chinese shrimp (Penaeus chinensis) by immunoinformatics coupled with competitive-binding strategy. Journal of Agricultural and Food Chemistry 66 (11):2944–53. doi: 10.1021/acs.jafc.7b06042.
  • Gajewski, K. G., and Y. H. P. Hsieh. 2009. Monoclonal antibody specific to a major fish allergen: Parvalbumin. Journal of Food Protection 72 (4):818–25. doi: 10.4315/0362-028x-72.4.818.
  • Gámez, C., M. P. Zafra, M. Boquete, V. Sanz, C. Mazzeo, M. D. Ibáñez, S. Sánchez-García, J. Sastre, and V. del Pozo. 2014. New shrimp IgE‐binding proteins involved in mite‐seafood cross‐reactivity. Molecular Nutrition & Food Research 58 (9):1915–25. doi: 10.1002/mnfr.201400122.
  • Gámez, C., M. P. Zafra, V. Sanz, C. Mazzeo, M. D. Ibáñez, J. Sastre, and V. del Pozo. 2015. Simulated gastrointestinal digestion reduces the allergic reactivity of shrimp extract proteins and tropomyosin. Food Chemistry 173:475–81. doi: 10.1016/j.foodchem.2014.10.063.
  • García-Orozco, K. D., E. Aispuro-Hernández, G. Yepiz-Plascencia, A. M. Calderón-De-La-Barca, and R. R. Sotelo-Mundo. 2007. Molecular characterization of arginine kinase, an allergen from the shrimp Litopenaeus vannamei. International Archives of Allergy and Immunology 144 (1):23–8. doi: 10.1159/000102610.
  • Gelis, S., M. Rueda, A. Valero, E. A. Fernández, M. Moran, and E. Fernández-Caldas. 2020. Shellfish allergy: Unmet needs in diagnosis and treatment. Journal of Investigational Allergology & Clinical Immunology 30 (6):409–20. doi: 10.18176/jiaci.0565.
  • Giuffrida, M. G., D. Villalta, G. Mistrello, S. Amato, and R. Asero. 2014. Shrimp allergy beyond tropomyosin in Italy: Clinical relevance of arginine kinase, sarcoplasmic calcium binding protein and hemocyanin. European Annals of Allergy and Clinical Immunology 46 (5):172–7.
  • González-Fernández, J., M. Alguacil-Guillén, C. Cuéllar, and A. Daschner. 2018. Possible allergenic role of tropomyosin in patients with adverse reactions after fish intake. Immunological Investigations 47 (4):416–29. doi: 10.1080/08820139.2018.1451882.
  • González-Fernández, J., A. Daschner, and C. Cuéllar. 2017. Allergenicity of vertebrate tropomyosins: Challenging an immunological dogma. Allergologia et Immunopathologia 45 (3):297–304. doi: 10.1016/j.aller.2016.08.002.
  • Griesmeier, U., M. Bublin, C. Radauer, S. Vázquez‐Cortés, Y. Ma, M. Fernández‐Rivas, and H. Breiteneder. 2010. Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff. Molecular Nutrition & Food Research 54 (6):861–9. doi: 10.1002/mnfr.200900043.
  • Gupta, R. S., C. M. Warren, B. M. Smith, J. Jiang, J. A. Blumenstock, M. M. Davis, R. P. Schleimer, and K. C. Nadeau. 2019. Prevalence and severity of food allergies among US adults. JAMA Network Open 2 (1):e185630-e185630. doi: 10.1001/jamanetworkopen.2018.5630.
  • Hales, B. J., A. C. Martin, L. J. Pearce, I. A. Laing, C. M. Hayden, J. Goldblatt, P. N. Le Souëf, and W. R. Thomas. 2006. IgE and IgG anti-house dust mite specificities in allergic disease. The Journal of Allergy and Clinical Immunology 118 (2):361–7. doi: 10.1016/j.jaci.2006.04.001.
  • Hamada, Y., Y. Nagashima, and K. Shiomi. 2001. Identification of collagen as a new fish allergen. Bioscience, Biotechnology, and Biochemistry 65 (2):285–91. doi: 10.1271/bbb.65.285.
  • Han, T. J., F. Huan, M. Liu, M. S. Li, Y. Yang, G. X. Chen, D. Lai, M. J. Cao, and G. M. Liu. 2021. IgE epitope analysis of sarcoplasmic-calcium-binding protein, a heat-resistant allergen in Crassostrea angulate. Food & Function 12 (18):8570–82. doi: 10.1039/d1fo01058a.
  • Han, T.-J., M. Liu, F. Huan, M.-S. Li, F. Xia, Y.-Y. Chen, G.-X. Chen, M.-J. Cao, and G.-M. Liu. 2020. Identification and cross-reactivity analysis of sarcoplasmic-calcium-binding protein: A novel allergen in Crassostrea angulata. Journal of Agricultural and Food Chemistry 68 (18):5221–31. doi: 10.1021/acs.jafc.0c01543.
  • Hansen, T. K., C. Bindslev-Jensen, P. S. Skov, and L. K. Poulsen. 1997. Codfish allergy in adults: IgE cross-reactivity among fish species. Annals of Allergy, Asthma & Immunology 78 (2):187–94. doi: 10.1016/S1081-1206(10)63386-8.
  • He, X.-R., Y. Yang, S. Kang, Y.-X. Chen, P.-Y. Zheng, G.-X. Chen, X.-M. Chen, M.-J. Cao, T. Jin, and G.-M. Liu. 2022. Crystal structure analysis and IgE epitope mapping of allergic predominant region in Scylla paramamosain Filamin C, Scy p 9. Journal of Agricultural and Food Chemistry 70 (4):1282–92. doi: 10.1021/acs.jafc.1c07922.
  • Heizmann, C. W. 2019. Ca2+-binding proteins of the EF-hand superfamily: Diagnostic and prognostic biomarkers and novel therapeutic targets. In Calcium-binding proteins of the EF-hand superfamily, 157–86. New York, NY: Humana Press.
  • Hindley, J., S. Wünschmann, S. M. Satinover, J. A. Woodfolk, F. T. Chew, M. D. Chapman, and A. Pomés. 2006. Bla g 6: A troponin C allergen from Blattella germanica with IgE binding calcium dependence. The Journal of Allergy and Clinical Immunology 117 (6):1389–95. doi: 10.1016/j.jaci.2006.02.017.
  • Hoffmann, H. J., E. Valovirta, O. Pfaar, P. Moingeon, J. M. Schmid, S. H. Skaarup, L.-O. Cardell, K. Simonsen, M. Larché, S. R. Durham, et al. 2017. Novel approaches and perspectives in allergen immunotherapy. Allergy 72 (7):1022–34. doi: 10.1111/all.13135.
  • Hoppe, S., H. Steinhart, and A. Paschke. 2006. Identification of a 28 kDa lychee allergen as a triose-phosphate isomerase. Food and Agricultural Immunology 17 (1):9–19. doi: 10.1080/09540100500538307.
  • Hu, M.-J., G.-Y. Liu, Y. Yang, T.-M. Pan, Y.-X. Liu, L.-C. Sun, M.-J. Cao, and G.-M. Liu. 2017. Cloning, expression, and the effects of processing on sarcoplasmic-calcium-binding protein: An important allergen in mud crab. Journal of Agricultural and Food Chemistry 65 (30):6247–57. doi: 10.1021/acs.jafc.7b02381.
  • Ishikawa, M., M. Ishida, K. Shimakura, Y. Nagashima, and K. Shiomi. 1998. Purification and IgE-binding epitopes of a major allergen in the gastropod Turbo cornutus. Bioscience, Biotechnology, and Biochemistry 62 (7):1337–43. doi: 10.1271/bbb.62.1337.
  • Ishikawa, M., K. Shimakura, Y. Nagashima, and K. Shiomi. 1997. Isolation and properties of allergenic proteins in the oyster Crassostrea gigas. Fisheries Science 63 (4):610–4. doi: 10.2331/fishsci.63.610.
  • Ishikawa, M., F. Suzuki, M. Ishida, Y. Nagashima, and K. Shiomi. 2001. Identification of tropomyosin as a major allergen in the octopus Octopus vulgaris and elucidation of its IgE-binding epitopes. Fisheries Science 67 (5):934–42. doi: 10.1046/j.1444-2906.2001.00344.x.
  • Jarilla, B. R., K. Uda, T. Suzuki, L. P. Acosta, M. Urabe, and T. Agatsuma. 2014. Characterization of arginine kinase from the caenogastropod Semisulcospira libertina, an intermediate host of Paragonimus westermani. Journal of Molluscan Studies 80 (4):444–51. doi: 10.1093/mollus/eyu053.
  • Jenkins, J. A., H. Breiteneder, and E. C. Mills. 2007. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. The Journal of Allergy and Clinical Immunology 120 (6):1399–405. doi: 10.1016/j.jaci.2007.08.019.
  • Jeong, K. Y., C.-r Kim, S. Un, M.-h Yi, I.-Y. Lee, J. W. Park, C.-S. Hong, and T.-S. Yong. 2010. Allergenicity of recombinant troponin C from Tyrophagus putrescentiae. International Archives of Allergy and Immunology 151 (3):207–13. doi: 10.1159/000242358.
  • Jeong, K. Y., J. Y. Lee, M. Son, M. H. Yi, T. S. Yong, J. U. Shin, K. H. Lee, Y. J. Kim, K. H. Park, H. J. Park, et al. 2015. Profiles of IgE sensitization to Der f 1, Der f 2, Der f 6, Der f 8, Der f 10, and Der f 20 in Korean house dust mite allergy patients. Allergy, Asthma & Immunology Research 7 (5):483–8. doi: 10.4168/aair.2015.7.5.483.
  • Kalic, T., S. D. Kamath, T. Ruethers, A. C. Taki, R. Nugraha, T. T. K. Le, P. Humeniuk, N. A. Williamson, D. Hira, J. M. Rolland, et al. 2020. Collagen-an important fish allergen for improved diagnosis. The Journal of Allergy and Clinical Immunology. In Practice 8 (9):3084–92.e10. doi: 10.1016/j.jaip.2020.04.063.
  • Kalic, T., F. Morel-Codreanu, C. Radauer, T. Ruethers, A. C. Taki, I. Swoboda, C. Hilger, K. Hoffmann-Sommergruber, M. Ollert, C. Hafner, et al. 2019. Patients allergic to fish tolerate ray based on the low allergenicity of its parvalbumin. The Journal of Allergy and Clinical Immunology. In Practice 7 (2):500–8.e11. doi: 10.1016/j.jaip.2018.11.011.
  • Kalyanasundaram, A., and T. C. Santiago. 2015. Identification and characterization of new allergen troponin C (Pen m 6.0101) from Indian black tiger shrimp Penaeus monodon. European Food Research and Technology 240 (3):509–15. doi: 10.1007/s00217-014-2349-y.
  • Kamath, S. D., E. B. Johnston, S. Iyer, P. M. Schaeffer, J. Koplin, K. Allen, and A. L. Lopata. 2017. IgE reactivity to shrimp allergens in infants and their cross-reactivity to house dust mite. Pediatric Allergy and Immunology 28 (7):703–7. doi: 10.1111/pai.12764.
  • Kamath, S. D., A. M. A. Rahman, T. Komoda, and A. L. Lopata. 2013. Impact of heat processing on the detection of the major shellfish allergen tropomyosin in crustaceans and molluscs using specific monoclonal antibodies. Food Chemistry 141 (4):4031–9. doi: 10.1016/j.foodchem.2013.06.105.
  • Kamath, S. D., A. M. A. Rahman, A. Voskamp, T. Komoda, J. M. Rolland, R. E. O’hehir, and A. L. Lopata. 2014. Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: A comprehensive allergenomic approach. Molecular Nutrition & Food Research 58 (5):1144–55. doi: 10.1002/mnfr.201300584.
  • Kelso, J. M., R. T. Jones, and J. W. Yunginger. 1996. Monospecific allergy to swordfish. Annals of Allergy, Asthma & Immunology 77 (3):227–8. doi: 10.1016/S1081-1206(10)63260-7.
  • Khan, M. U., I. Ahmed, H. Lin, Z. Li, J. Costa, I. Mafra, Y. Chen, and Y.-N. Wu. 2019. Potential efficacy of processing technologies for mitigating crustacean allergenicity. Critical Reviews in Food Science and Nutrition 59 (17):2807–30. doi: 10.1080/10408398.2018.1471658.
  • Khanaruksombat, S., C. Srisomsap, D. Chokchaichamnankit, P. Punyarit, and P. Phiriyangkul. 2014. Identification of a novel allergen from muscle and various organs in banana shrimp (Fenneropenaeus merguiensis). Annals of Allergy, Asthma & Immunology 113 (3):301–6. doi: 10.1016/j.anai.2014.06.002.
  • Khurana, T., M. Collison, F. T. Chew, and J. E. Slater. 2014. Bla g 3: A novel allergen of German cockroach identified using cockroach-specific avian single-chain variable fragment antibody. Annals of Allergy, Asthma & Immunology 112 (2):140–5.e1. doi: 10.1016/j.anai.2013.11.007.
  • Kios, K., S. Kakasis, F. Syropoulou, and I. S. Boziaris. 2023. Seafood and shellfish. In Functional foods and their implications for health promotion, 281–302. Academic Press.
  • Kobayashi, Y., H. Akiyama, J. Huge, H. Kubota, S. Chikazawa, T. Satoh, T. Miyake, H. Uhara, R. Okuyama, R. Nakagawara, et al. 2016. Fish collagen is an important panallergen in the Japanese population. Allergy 71 (5):720–3. doi: 10.1111/all.12836.
  • Kondo, Y., J. Ahn, R. Komatsubara, A. Terada, T. Yasuda, I. Tsuge, and A. Urisu. 2009. Comparison of allergenic properties of salmon (Oncorhynchus nerka) between landlocked and anadromous species. Allergology International 58 (2):295–9. doi: 10.2332/allergolint.08-OA-0064.
  • Kondo, Y., R. Komatsubara, Y. Nakajima, T. Yasuda, M. Kakami, I. Tsuge, and A. Urisu. 2006. Parvalbumin is not responsible for cross-reactivity between tuna and marlin: A case report. The Journal of Allergy and Clinical Immunology 118 (6):1382–3. doi: 10.1016/j.jaci.2006.07.047.
  • Kubota, H., A. Kobayashi, Y. Kobayashi, K. Shiomi, and N. Hamada-Sato. 2016. Reduction in IgE reactivity of Pacific mackerel parvalbumin by heat treatment. Food Chemistry 206:78–84. doi: 10.1016/j.foodchem.2016.03.043.
  • Kuehn, A., F. Codreanu-Morel, C. Lehners-Weber, V. Doyen, S.-A. Gomez-André, F. Bienvenu, J. Fischer, N. Ballardini, M. van Hage, J.-M. Perotin, et al. 2016. Cross‐reactivity to fish and chicken meat – A new clinical syndrome. Allergy 71 (12):1772–81. doi: 10.1111/all.12968.
  • Kuehn, A., C. Hilger, C. Lehners-Weber, F. Codreanu-Morel, M. Morisset, C. Metz-Favre, G. Pauli, F. de Blay, D. Revets, C. P. Muller, et al. 2013. Identification of enolases and aldolases as important fish allergens in cod, salmon and tuna: Component resolved diagnosis using parvalbumin and the new allergens. Clinical and Experimental Allergy 43 (7):811–22. doi: 10.1111/cea.12117.
  • Kuehn, A., I. Swoboda, K. Arumugam, C. Hilger, and F. Hentges. 2014. Fish allergens at a glance: Variable allergenicity of parvalbumins, the major fish allergens. Frontiers in Immunology 5:179. doi: 10.3389/fimmu.2014.00179.
  • Kumeta, H., H. Nakayama, and K. Ogura. 2017. Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel. Scientific Reports 7 (1):1–7. doi: 10.1038/s41598-017-17281-6.
  • Kyosaka, I., S. Fujita, Y. Shimizu, and H. Saeki. 2019. Digestibility in the gastrointestinal tract and migration to blood of β′-component (Onk k 5), a major salmon roe IgE-binding protein. Food Chemistry 289:694–700. doi: 10.1016/j.foodchem.2019.03.089.
  • Larco-Rojas, X., M. González-Gutiérrez, S. Vázquez-Cortés, B. Bartolomé, C. Pastor-Vargas, and M. Fernández-Rivas. 2017. Occupational asthma and urticaria in a fishmonger due to creatine kinase, a cross-reactive fish allergen. Journal of Investigational Allergology & Clinical Immunology 27 (6):386–8. doi: 10.18176/jiaci.0195.
  • Lee, B. J., and H. S. Park. 2004. Common whelk (Buccinum undatum) allergy: Identification of IgE-binding components and effects of heating and digestive enzymes. Journal of Korean Medical Science 19 (6):793–9. doi: 10.3346/jkms.2004.19.6.793.
  • Lee, C.-S., L.-C. Tsai, P.-L. Chao, C.-Y. Lin, M.-W. Hung, A.-I. Chien, Y.-T. Chiang, and S.-H. Han. 2004. Protein sequence analysis of a novel 103 kDa Dermatophagoides pteronyssinus mite allergen and prevalence of serum immunoglobulin E reactivity to rDer p 11 in allergic adult patients. Clinical and Experimental Allergy 34 (3):354–62. doi: 10.1111/j.1365-2222.2004.01878.x.
  • Lee, M. F., P. P. Song, G. Y. Hwang, S. J. Lin, and Y. H. Chen. 2012. Sensitization to Per a 2 of the American cockroach correlates with more clinical severity among airway allergic patients in Taiwan. Annals of Allergy, Asthma & Immunology 108 (4):243–8. doi: 10.1016/j.anai.2012.01.014.
  • Lees-Miller, J. P., and D. M. Helfman. 1991. The molecular basis for tropomyosin isoform diversity. BioEssays 13 (9):429–37. doi: 10.1002/bies.950130902.
  • Leung, N. Y., C. Y. Wai, M. H. Ho, R. Liu, K. S. Lam, J. J. Wang, S. A. Shu, K. H. Chu, and P. S. Leung. 2017. Screening and identification of mimotopes of the major shrimp allergen tropomyosin using one-bead-one-compound peptide libraries. Cellular & Molecular Immunology 14 (3):308–18. doi: 10.1038/cmi.2015.83.
  • Leung, N. Y. H., C. Y. Y. Wai, S. Shu, J. Wang, T. P. Kenny, K. H. Chu, and P. S. Leung. 2014. Current immunological and molecular biological perspectives on seafood allergy: A comprehensive review. Clinical Reviews in Allergy & Immunology 46 (3):180–97. doi: 10.1007/s12016-012-8336-9.
  • Leung, T. F., E. Yung, Y. S. Wong, C. W. Lam, and G. W. Wong. 2009. Parent‐reported adverse food reactions in Hong Kong Chinese pre-schoolers: Epidemiology, clinical spectrum and risk factors. Pediatric Allergy and Immunology 20 (4):339–46. doi: 10.1111/j.1399-3038.2008.00801.x.
  • Leung, Y. H. N. 2015. Identification of IgE mimotopes of the shrimp allergen tropomyosin and evaluation on the therapeutic potential of mimotope-based immunotherapy. Doctoral diss., The Chinese University of Hong Kong.
  • Li, J., Z. Li, D. Kong, S. Li, Y. Yu, and H. Li. 2020. IgE and IgG4 responses to shrimp allergen tropomyosin and its epitopes in patients from coastal areas of northern China. Molecular Medicine Reports 22 (1):371–9. doi: 10.3892/mmr.2020.11084.
  • Li, M.-S., F. Xia, M. Liu, X.-R. He, Y.-Y. Chen, T.-L. Bai, G.-X. Chen, L. Wang, M.-J. Cao, and G.-M. Liu. 2019. Cloning, expression, and epitope identification of myosin light chain 1: An allergen in mud crab. Journal of Agricultural and Food Chemistry 67 (37):10458–69. doi: 10.1021/acs.jafc.9b04294.
  • Li, Z. S., Y. Shimizu, and H. Saeki. 2017. Grey mullet roe contains yolk protein having IgE cross-reactivity to chum salmon roe major allergen (Onc k 5). Fisheries Science 83 (2):301–8. doi: 10.1007/s12562-016-1057-x.
  • Lindstrøm, C. D. V., T. Van Do, I. Hordvik, C. Endresen, and S. Elsayed. 1996. Cloning of two distinct cDNAs encoding parvalbumin, the major allergen of Atlantic salmon (Salmo salar). Scandinavian Journal of Immunology 44 (4):335–44. doi: 10.1046/j.1365-3083.1996.d01-314.x.
  • Liu, M., F. Huan, M. Li, T. Han, F. Xia, Y. Yang, Q. Liu, G. Chen, M. Cao, and G. Liu. 2021. Mapping and IgE-binding capacity analysis of heat/digested stable epitopes of mud crab allergens. Food Chemistry 344:128735. doi: 10.1016/j.foodchem.2020.128735.
  • Liu, G. M., Y. Y. Huang, Q. F. Cai, W. Y. Weng, W. J. Su, and M. J. Cao. 2011. Comparative study of in vitro digestibility of major allergen, tropomyosin and other proteins between Grass prawn (Penaeus monodon) and Pacific white shrimp (Litopenaeus vannamei). Journal of the Science of Food and Agriculture 91 (1):163–70. doi: 10.1002/jsfa.4167.
  • Liu, G.-Y., X.-J. Mei, M.-J. Hu, Y. Yang, M. Liu, M.-S. Li, M.-L. Zhang, M.-J. Cao, and G.-M. Liu. 2018. Analysis of the allergenic epitopes of tropomyosin from mud crab using phage display and site-directed mutagenesis. Journal of Agricultural and Food Chemistry 66 (34):9127–37. doi: 10.1021/acs.jafc.8b03466.
  • Liu, R., A. L. Holck, E. Yang, C. Liu, and W. Xue. 2013. Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen. Clinical and Experimental Allergy 43 (3):365–77. doi: 10.1111/cea.12056.
  • Liu, R., H. B. Krishnan, W. Xue, and C. Liu. 2011. Characterization of allergens isolated from the freshwater fish blunt snout bream (Megalobrama amblycephala). Journal of Agricultural and Food Chemistry 59 (1):458–63. doi: 10.1021/jf103942p.
  • Liu, W. L., Q. X. Zeng, and R. Z. Luo. 2020. Predictors for short-term efficacy of allergen-specific sublingual immunotherapy in children with allergic rhinitis. Mediators of Inflammation 2020:1847061. doi: 10.1155/2020/1847061.
  • Liu, Y. Y., X. F. Chen, J. W. Hu, Z. W. Chen, L. J. Zhang, M. J. Cao, and G. M. Liu. 2016. Purification and characterization of protamine, the allergen from the milt of large yellow croaker (Pseudosciaena crocea), and its components. Journal of Agricultural and Food Chemistry 64 (9):1999–2011. doi: 10.1021/acs.jafc.5b05899.
  • Liu, Z., L. Xia, Y. Wu, Q. Xia, J. Chen, and K. H. Roux. 2009. Identification and characterization of an arginine kinase as a major allergen from silkworm (Bombyx mori) larvae. International Archives of Allergy and Immunology 150 (1):8–14. doi: 10.1159/000210375.
  • Lopata, A. L., and M. F. Jeebhay. 2013. Airborne seafood allergens as a cause of occupational allergy and asthma. Current Allergy and Asthma Reports 13 (3):288–97. doi: 10.1007/s11882-013-0347-y.
  • Lu, X., H. Lu, L. Guo, Z. Zhang, X. Zhao, M. Zhong, S. Li, and Y. Zhang. 2015. Cloning and characterization of a novel hemocyanin variant LvHMCV4 from shrimp Litopenaeus vannamei. Fish & Shellfish Immunology 46 (2):398–405. doi: 10.1016/j.fsi.2015.06.022.
  • Lyons, S. A. 2021. A pan-European perspective on food allergy: Prevalence, predictors and patient profiles. Doctoral diss., Utrecht University.
  • Ma, J. J., T. R. Pavase, Z. X. Li, and H. Lin. 2017. Optimisation of an extraction technique of fish allergens suitable for detection and diagnosis. Czech Journal of Food Sciences 35 (1):24–31. doi: 10.17221/578/2015-CJFS.
  • Mao, H. Y., M. J. Cao, S. J. Maleki, Q. F. Cai, W. J. Su, Y. Yang, and G. M. Liu. 2013. Structural characterization and IgE epitope analysis of arginine kinase from Scylla paramamosain. Molecular Immunology 56 (4):463–70. doi: 10.1016/j.molimm.2013.04.016.
  • Matricardi, P. M., J. Kleine-Tebbe, H. J. Hoffmann, R. Valenta, C. Hilger, S. Hofmaier, R. C. Aalberse, I. Agache, R. Asero, B. Ballmer-Weber, et al. 2016. EAACI molecular allergology user’s guide. Pediatric Allergy and Immunology 27:1–250. doi: 10.1111/pai.12563.
  • Matsuo, H., T. Yokooji, and T. Taogoshi. 2015. Common food allergens and their IgE-binding epitopes. Allergology International 64 (4):332–43. doi: 10.1016/j.alit.2015.06.009.
  • McGowan, E. C., and C. A. Keet. 2013. Prevalence of self-reported food allergy in the National Health and Nutrition Examination Survey (NHANES) 2007-2010. The Journal of Allergy and Clinical Immunology 132 (5):1216–9.e5. doi: 10.1016/j.jaci.2013.07.018.
  • Mejrhit, N., O. Azdad, A. Chda, M. El Kabbaoui, A. Bousfiha, R. Bencheikh, A. Tazi, and L. Aarab. 2017. Evaluation of the sensitivity of Moroccans to shrimp tropomyosin and effect of heating and enzymatic treatments. Food and Agricultural Immunology 28 (6):969–80. doi: 10.1080/09540105.2017.1323187.
  • Minhas, J., J. A. Saryan, and D. S. Balekian. 2017. Salmon roe (ikura)-induced anaphylaxis in a child. Annals of Allergy, Asthma & Immunology 118 (3):365–6. doi: 10.1016/j.anai.2016.11.020.
  • Miyazawa, H., H. Fukamachi, Y. Inagaki, G. Reese, C. B. Daul, S. B. Lehrer, S. Inouye, and M. Sakaguchi. 1996. Identification of the first major allergen of a squid (Todarodes pacificus). The Journal of Allergy and Clinical Immunology 98 (5 Pt 1):948–53. doi: 10.1016/s0091-6749(96)80011-x.
  • Mol, S., and S. Cosansu. 2022. Seafood safety, potential hazards and future perspective. Turkish Journal of Fisheries and Aquatic Sciences 22 (6):TRJFAS20533. doi: 10.4194/TRJFAS20533.
  • Moonesinghe, H., H. Mackenzie, C. Venter, S. Kilburn, P. Turner, K. Weir, and T. Dean. 2016. Prevalence of fish and shellfish allergy: A systematic review. Annals of Allergy, Asthma & Immunology 117 (3):264–72.e4. doi: 10.1016/j.anai.2016.07.015.
  • Morii, A., H. Mita, S. Ishizaki, and K. Shiomi. 2013. Importance of conformation for the IgE reactivity of sarcoplasmic calcium-binding protein from the black tiger shrimp Penaeus monodon. European Food Research and Technology 236 (1):165–70. doi: 10.1007/s00217-012-1867-8.
  • Mota, I., C. Martins, and L. M. Borrego. 2017. Regulatory B cells and allergy: Uncovering the link. Journal of Investigational Allergology and Clinical Immunology 27 (4):204–12. doi: 10.18176/jiaci.0157.
  • Mukherjee, S., P. Horka, K. Zdenkova, and E. Cermakova. 2023. Parvalbumin: A major fish allergen and a forensically relevant marker. Genes 14 (1):223. doi: 10.3390/genes14010223.
  • Myrset, H. R., C. K. Fæste, P. E. Kristiansen, and M. M. Dooper. 2013. Mapping of the immunodominant regions of shrimp tropomyosin Pan b 1 by human IgE-binding and IgE receptor crosslinking studies. International Archives of Allergy and Immunology 162 (1):25–38. doi: 10.1159/000350791.
  • Nakamura, R., R. Satoh, Y. Nakajima, N. Kawasaki, T. Yamaguchi, J.-I. Sawada, H. Nagoya, and R. Teshima. 2009. Comparative study of GH-transgenic and non-transgenic amago salmon (Oncorhynchus masou ishikawae) allergenicity and proteomic analysis of amago salmon allergens. Regulatory Toxicology and Pharmacology 55 (3):300–8. doi: 10.1016/j.yrtph.2009.08.002.
  • Nowak-Wegrzyn, A., S. Sato, A. Fiocchi, and M. Ebisawa. 2019. Oral and sublingual immunotherapy for food allergy. Current Opinion in Allergy and Clinical Immunology 19 (6):606–13. doi: 10.1097/ACI.0000000000000587.
  • Nugraha, R., S. D. Kamath, E. Johnston, S. Karnaneedi, T. Ruethers, and A. L. Lopata. 2019. Conservation analysis of B-cell allergen epitopes to predict clinical cross-reactivity between shellfish and inhalant invertebrate allergens. Frontiers in Immunology 10:2676. doi: 10.3389/fimmu.2019.02676.
  • Nugraha, R., S. D. Kamath, E. Johnston, K. R. Zenger, J. M. Rolland, R. E. O’Hehir, and A. L. Lopata. 2018. Rapid and comprehensive discovery of unreported shellfish allergens using large-scale transcriptomic and proteomic resources. The Journal of Allergy and Clinical Immunology 141 (4):1501–4.e8. doi: 10.1016/j.jaci.2017.11.028.
  • Paparo, L., R. Nocerino, L. Cosenza, R. Aitoro, V. D’Argenio, V. Del Monaco, C. Di Scala, A. Amoroso, M. Di Costanzo, F. Salvatore, et al. 2016. Epigenetic features of FoxP3 in children with cow’s milk allergy. Clinical Epigenetics 8 (1):1–6. doi: 10.1186/s13148-016-0252-z.
  • Pascal, M., G. Grishina, A. C. Yang, S. Sánchez-García, J. Lin, D. Towle, M. D. Ibañez, J. Sastre, H. A. Sampson, and R. Ayuso. 2015. Molecular diagnosis of shrimp allergy: Efficiency of several allergens to predict clinical reactivity. The Journal of Allergy and Clinical Immunology. In Practice 3 (4):521–9.e10. doi: 10.1016/j.jaip.2015.02.001.
  • Patil, S. U., A. O. Ogunniyi, A. Calatroni, V. R. Tadigotla, B. Ruiter, A. Ma, J. Moon, J. C. Love, and W. G. Shreffler. 2015. Peanut oral immunotherapy transiently expands circulating Ara h 2-specific B cells with a homologous repertoire in unrelated subjects. The Journal of Allergy and Clinical Immunology 136 (1):125–34.e12. doi: 10.1016/j.jaci.2015.03.026.
  • Perez-Gordo, M., J. Lin, L. Bardina, C. Pastor-Vargas, B. Cases, F. Vivanco, J. Cuesta-Herranz, and H. A. Sampson. 2012. Epitope mapping of Atlantic salmon major allergen by peptide microarray immunoassay. International Archives of Allergy and Immunology 157 (1):31–40. doi: 10.1159/000324677.
  • Perez-Gordo, M., C. Pastor-Vargas, J. Lin, L. Bardina, B. Cases, M. D. Ibáñez, F. Vivanco, J. Cuesta-Herranz, and H. A. Sampson. 2013. Epitope mapping of the major allergen from Atlantic cod in Spanish population reveals different IgE-binding patterns. Molecular Nutrition & Food Research 57 (7):1283–90. doi: 10.1002/mnfr.201200332.
  • Perez-Gordo, M., S. Sanchez-Garcia, B. Cases, C. Pastor, F. Vivanco, and J. Cuesta-Herranz. 2008. Identification of vitellogenin as an allergen in Beluga caviar allergy. Allergy 63 (4):479–80. doi: 10.1111/j.1398-9995.2007.01614.x.
  • Pérez-Pérez, J., E. Fernández-Caldas, F. Marañón, J. Sastre, M. L. Bernal, J. Rodríguez, and C. A. Bedate. 2000. Molecular cloning of paramyosin, a new allergen of Anisakis simplex. International Archives of Allergy and Immunology 123 (2):120–9. doi: 10.1159/000024442.
  • Peters, B., M. Nielsen, and A. Sette. 2020. T cell epitope predictions. Annual Review of Immunology 38:123–45. doi: 10.1146/annurev-immunol-082119-124838.
  • Piboonpocanun, S., O. Jirapongsananuruk, T. Tipayanon, S. Boonchoo, and R. E. Goodman. 2011. Identification of hemocyanin as a novel non‐cross‐reactive allergen from the giant freshwater shrimp Macrobrachium rosenbergii. Molecular Nutrition & Food Research 55 (10):1492–8. doi: 10.1002/mnfr.201000602.
  • Porcaro, F., L. Caminiti, G. Crisafulli, S. Arasi, F. Chiera, G. La Monica, and G. B. Pajno. 2016. Management of food allergy to fish with oral immunotherapy: A pediatric case report. Pediatric Allergy, Immunology, and Pulmonology 29 (2):104–7. doi: 10.1089/ped.2015.0593.
  • Potocnakova, L., M. Bhide, and L. B. Pulzova. 2016. An introduction to B-cell epitope mapping and in silico epitope prediction. Journal of Immunology Research 2016:6760830. doi: 10.1155/2016/6760830.
  • Pyrhönen, K., S. Näyhä, M. Kaila, L. Hiltunen, and E. Läärä. 2009. Occurrence of parent‐reported food hypersensitivities and food allergies among children aged 1-4 yr. Pediatric Allergy and Immunology 20 (4):328–38. doi: 10.1111/j.1399-3038.2008.00792.x.
  • Rahman, A. M. A., S. Kamath, A. L. Lopata, and R. J. Helleur. 2010. Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry. Rapid Communications in Mass Spectrometry 24 (16):2462–70. doi: 10.1002/rcm.4664.
  • Rahman, A. M. A., S. D. Kamath, S. Gagné, A. L. Lopata, and R. Helleur. 2013. Comprehensive proteomics approach in characterizing and quantifying allergenic proteins from northern shrimp: Toward better occupational asthma prevention. Journal of Proteome Research 12 (2):647–56. doi: 10.1021/pr300755p.
  • Rahman, A. M. A., S. D. Kamath, A. L. Lopata, J. J. Robinson, and R. J. Helleur. 2011. Biomolecular characterization of allergenic proteins in snow crab (Chionoecetes opilio) and de novo sequencing of the second allergen arginine kinase using tandem mass spectrometry. Journal of Proteomics 74 (2):231–41. doi: 10.1016/j.jprot.2010.10.010.
  • Ramos, J., D. A. Cheong, N. Lee, B. W, and Chua, K. Y. 2001. cDNA cloning and expression of Blo t 11, the Blomia tropicalis allergen homologous to paramyosin. International Archives of Allergy and Immunology 126 (4):286–93. doi: 10.1159/000049525.
  • Rao, P. S., D. Rajagopal, and K. A. Ganesh. 1998. B-and T-cell epitopes of tropomyosin, the major shrimp allergen. Allergy 53 (46 Suppl):44–7. doi: 10.1111/j.1398-9995.1998.tb04959.x.
  • Reese, G., J. Viebranz, S. M. Leong-Kee, M. Plante, I. Lauer, S. Randow, M. S.-M. Moncin, R. Ayuso, S. B. Lehrer, and S. Vieths. 2005. Reduced allergenic potency of VR9-1, a mutant of the major shrimp allergen Pen a 1 (tropomyosin). Journal of Immunology 175 (12):8354–64. doi: 10.4049/jimmunol.175.12.8354.
  • Refaat, M. M., M. Y. Attia, and H. M. Saber. 2014. Desensitization efficacy by sublingual immunotherapy of shrimps extract in asthmatic, rhinitis and urticaria allergic patients. Food and Nutrition Sciences 05 (17):1704–10. doi: 10.4236/fns.2014.517183.
  • Renz, H., K. J. Allen, S. H. Sicherer, H. A. Sampson, G. Lack, K. Beyer, and H. C. Oettgen. 2018. Food allergy. Nature Reviews Disease Primers 4 (1):1–20. doi: 10.1038/nrdp.2017.98.
  • Rosmilah, M., M. Shahnaz, A. Masita, A. Noormalin, and M. Jamaludin. 2005. Identification of major allergens of two species of local snappers: Lutjanus argentimaculatus (merah/red snapper) and Lutjanus johnii (jenahak/golden snapper). Tropical Biomedicine 22 (2):171–7.
  • Rosmilah, M., M. Shahnaz, H. M. Zailatul, A. Noormalin, and I. Normilah. 2012. Identification of tropomyosin and arginine kinase as major allergens of Portunus pelagicus (blue swimming crab). Tropical Biomedicine. 29 (3):467–78.
  • Rossi, R. E., G. Monasterolo, C. Incorvaia, P. Moingeon, F. Frati, G. Passalacqua, L. Rossi, and G. W. Canonica. 2010. Lack of neo-sensitization to Pen a 1 in patients treated with mite sublingual immunotherapy. Clinical and Molecular Allergy 8 (1):4. doi: 10.1186/1476-7961-8-4.
  • Ruano, F. J., and E. Haroun-Díaz. 2023. Selective allergy to whiff (Lepidorhombus whiffiagonis): Identification of enolase as a new major allergen. Journal of Investigational Allergology and Clinical Immunology 33 (1). doi: 10.18176/jiaci.0809.
  • Ruethers, T., R. Nugraha, A. C. Taki, A. O’Malley, S. Karnaneedi, S. Zhang, A. B. Kapingidza, S. Mehr, S. D. Kamath, M. Chruszcz, et al. 2022. The first reptilian allergen and major allergen for fish-allergic patients: Crocodile β‐parvalbumin. Pediatric Allergy and Immunology 33 (5):e13781. doi: 10.1111/pai.13781.
  • Ruethers, T., A. C. Taki, E. B. Johnston, R. Nugraha, T. T. K. Le, T. Kalic, T. R. McLean, S. D. Kamath, and A. L. Lopata. 2018. Seafood allergy: A comprehensive review of fish and shellfish allergens. Molecular Immunology 100:28–57. doi: 10.1016/j.molimm.2018.04.008.
  • Ruethers, T., A. C. Taki, S. Karnaneedi, S. Nie, T. Kalic, D. Dai, S. Daduang, M. Leeming, N. A. Williamson, H. Breiteneder, et al. 2021. Expanding the allergen repertoire of salmon and catfish. Allergy 76 (5):1443–53. doi: 10.1111/all.14574.
  • Ryan, J. F., R. Hovde, J. Glanville, S.-C. Lyu, X. Ji, S. Gupta, R. J. Tibshirani, D. C. Jay, S. D. Boyd, R. S. Chinthrajah, et al. 2016. Successful immunotherapy induces previously unidentified allergen-specific CD4+ T-cell subsets. Proceedings of the National Academy of Sciences of the United States of America 113 (9):1286–95. doi: 10.1073/pnas.1520180113.
  • Sakaguchi, M., M. Toda, T. Ebihara, S. Irie, H. Hori, A. Imai, M. Yanagida, H. Miyazawa, H. Ohsuna, Z. Ikezawa, et al. 2000. IgE antibody to fish gelatin (type I collagen) in patients with fish allergy. The Journal of Allergy and Clinical Immunology 106 (3):579–84. doi: 10.1067/mai.2000.108499.
  • Sampath, V., S. B. Sindher, W. Zhang, and K. C. Nadeau. 2018. New treatment directions in food allergy. Annals of Allergy, Asthma & Immunology 120 (3):254–62. doi: 10.1016/j.anai.2018.01.004.
  • Sanchez-Trincado, J. L., M. Gomez-Perosanz, and P. A. Reche. 2017. Fundamentals and methods for T-and B-cell epitope prediction. Journal of Immunology Research 2017:1–14. doi: 10.1155/2017/2680160.
  • Sander, I., P. Rozynek, H.-P. Rihs, V. van Kampen, F. T. Chew, W. S. Lee, N. Kotschy-Lang, R. Merget, T. Brüning, and M. Raulf-Heimsoth. 2011. Multiple wheat flour allergens and cross-reactive carbohydrate determinants bind IgE in baker’s asthma. Allergy 66 (9):1208–15. doi: 10.1111/j.1398-9995.2011.02636.x.
  • Saptarshi, S. R., M. F. Sharp, S. D. Kamath, and A. L. Lopata. 2014. Antibody reactivity to the major fish allergen parvalbumin is determined by isoforms and impact of thermal processing. Food Chemistry 148:321–8. doi: 10.1016/j.foodchem.2013.10.035.
  • Scala, E., D. Abeni, A. Aruanno, E. Boni, I. Brusca, F. Cappiello, E. Caprini, F. Buzzulini, G. Deleonardi, A. Demonte, et al. 2022. Mollusk allergy in shrimp-allergic patients: Still a complex diagnosis. An Italian real-life cross-sectional multicenter study. The World Allergy Organization Journal 15 (9):100685. doi: 10.1016/j.waojou.2022.100685.
  • Schnabel, E., S. Sausenthaler, B. Schaaf, T. Schafer, I. Lehmann, H. Behrendt, O. Herbarth, M. Borte, U. Kramer, A. von Berg, et al. 2010. Prospective association between food sensitization and food allergy: Results of the LISA birth cohort study. Clinical and Experimental Allergy 40 (3):450–7. doi: 10.1111/j.1365-2222.2009.03400.x.
  • Schoos, A.-M. M., D. Bullens, B. L. Chawes, J. Costa, L. De Vlieger, A. DunnGalvin, M. M. Epstein, J. Garssen, C. Hilger, K. Knipping, et al. 2020. Immunological outcomes of allergen-specific immunotherapy in food allergy. Frontiers in Immunology 11:568598. doi: 10.3389/fimmu.2020.568598.
  • Shamji, M. H., and S. R. Durham. 2017. Mechanisms of allergen immunotherapy for inhaled allergens and predictive biomarkers. The Journal of Allergy and Clinical Immunology 140 (6):1485–98. doi: 10.1016/j.jaci.2017.10.010.
  • Shanti, K. N., B. M. Martin, S. Nagpal, D. D. Metcalfe, and P. V. S. Rao. 1993. Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. The Journal of Immunology 151 (10):5354–63. doi: 10.4049/jimmunol.151.10.5354.
  • Sharp, M. F., S. D. Kamath, M. Koeberl, D. R. Jerry, R. E. O’Hehir, D. E. Campbell, and A. L. Lopata. 2014. Differential IgE binding to isoallergens from Asian seabass (Lates calcarifer) in children and adults. Molecular Immunology 62 (1):77–85. doi: 10.1016/j.molimm.2014.05.010.
  • Sharp, M. F., and A. L. Lopata. 2014. Fish allergy: In review. Clinical Reviews in Allergy & Immunology 46 (3):258–71. doi: 10.1007/s12016-013-8363-1.
  • Sharp, M. F., J. N. Stephen, L. Kraft, T. Weiss, S. D. Kamath, and A. L. Lopata. 2015. Immunological cross-reactivity between four distant parvalbumins-impact on allergen detection and diagnostics. Molecular Immunology 63 (2):437–48. doi: 10.1016/j.molimm.2014.09.019.
  • Sharp, M. F., A. C. Taki, T. Ruethers, J. N. Stephen, N. L. Daly, A. L. Lopata, and S. D. Kamath. 2021. IgE and IgG4 epitopes revealed on the major fish allergen Lat c 1. Molecular Immunology 131:155–63. doi: 10.1016/j.molimm.2020.12.033.
  • Shek, L. P.-C., E. A. Cabrera-Morales, S. E. Soh, I. Gerez, P. Z. Ng, F. C. Yi, S. Ma, and B. W. Lee. 2010. A population-based questionnaire survey on the prevalence of peanut, tree nut, and shellfish allergy in 2 Asian populations. The Journal of Allergy and Clinical Immunology 126 (2):324–31. doi: 10.1016/j.jaci.2010.06.003.
  • Shen, H. W., M. J. Cao, Q. F. Cai, M. M. Ruan, H. Y. Mao, W. J. Su, and G. M. Liu. 2012. Purification, cloning, and immunological characterization of arginine kinase, a novel allergen of Octopus fangsiao. Journal of Agricultural and Food Chemistry 60 (9):2190–9. doi: 10.1021/jf203779w.
  • Shimizu, Y., A. Nakamura, H. Kishimura, A. Hara, K. Watanabe, and H. Saeki. 2009. Major allergen and its IgE cross-reactivity among salmonid fish roe allergy. Journal of Agricultural and Food Chemistry 57 (6):2314–9. doi: 10.1021/jf8031759.
  • Shiomi, K., Y. Sato, S. Hamamoto, H. Mita, and K. Shimakura. 2008. Sarcoplasmic calcium-binding protein: Identification as a new allergen of the black tiger shrimp Penaeus monodon. International Archives of Allergy and Immunology 146 (2):91–8. doi: 10.1159/000113512.
  • Sližienė, A., M. Plečkaitytė, M. Zaveckas, K. Juškaitė, V. Rudokas, G. Žvirblis, and A. Žvirblienė. 2022. Monoclonal antibodies against the newly identified allergen β-enolase from common carp (Cyprinus carpio). Food and Agricultural Immunology 33 (1):129–49. doi: 10.1080/09540105.2022.2028741.
  • Sookrung, N., W. Chaicumpa, A. Tungtrongchitr, P. Vichyanond, C. Bunnag, P. Ramasoota, P. Tongtawe, Y. Sakolvaree, and P. Tapchaisri. 2006. Periplaneta americana arginine kinase as a major cockroach allergen among Thai patients with major cockroach allergies. Environmental Health Perspectives 114 (6):875–80. doi: 10.1289/ehp.8650.
  • Srinroch, C., C. Srisomsap, D. Chokchaichamnankit, P. Punyarit, and P. Phiriyangkul. 2015. Identification of novel allergen in edible insect, Gryllus bimaculatus and its cross-reactivity with Macrobrachium spp. allergens. Food Chemistry 184:160–6. doi: 10.1016/j.foodchem.2015.03.094.
  • Stephen, J. N., M. F. Sharp, T. Ruethers, A. Taki, D. E. Campbell, and A. L. Lopata. 2017. Allergenicity of bony and cartilaginous fish-molecular and immunological properties. Clinical and Experimental Allergy 47 (3):300–12. doi: 10.1111/cea.12892.
  • Suzuki, M., Y. Kobayashi, Y. Hiraki, H. Nakata, and K. Shiomi. 2011. Paramyosin of the disc abalone Haliotis discus discus: Identification as a new allergen and cross-reactivity with tropomyosin. Food Chemistry 124 (3):921–6. doi: 10.1016/j.foodchem.2010.07.020.
  • Suzuki, M., K. Shimizu, Y. Kobayashi, S. Ishizaki, and K. Shiomi. 2014. Paramyosin from the disc abalone Haliotis discus discus. Journal of Food Biochemistry 38 (4):444–51. doi: 10.1111/jfbc.12072.
  • Swoboda, I., A. Bugajska-Schretter, B. Linhart, P. Verdino, W. Keller, U. Schulmeister, W. R. Sperr, P. Valent, G. Peltre, S. Quirce, et al. 2007. A recombinant hypoallergenic parvalbumin mutant for immunotherapy of IgE-mediated fish allergy. Journal of Immunology 178 (10):6290–6. doi: 10.4049/jimmunol.178.10.6290.
  • Swoboda, I., A. Bugajska‐Schretter, R. Valenta, and S. Spitzauer. 2002. Recombinant fish parvalbumins: Candidates for diagnosis and treatment of fish allergy. Allergy 57 (s72):94–6. doi: 10.1034/j.1398-9995.57.s72.21.x.
  • Syed, A., M. A. Garcia, S.-C. Lyu, R. Bucayu, A. Kohli, S. Ishida, J. P. Berglund, M. Tsai, H. Maecker, G. O’Riordan, et al. 2014. Peanut oral immunotherapy results in increased antigen-induced regulatory T-cell function and hypomethylation of forkhead box protein 3 (FOXP3). The Journal of Allergy and Clinical Immunology 133 (2):500–10. doi: 10.1016/j.jaci.2013.12.1037.
  • Takagi, T., and K. Konishi. 1984. Amino acid sequence of the β chain of sarcoplasmic calcium binding protein (SCP) obtained from shrimp tail muscle. Journal of Biochemistry 96 (1):59–67. doi: 10.1093/oxfordjournals.jbchem.a134829.
  • Thyagarajan, A., S. M. Jones, A. Calatroni, L. Pons, M. Kulis, C. S. Woo, M. Kamalakannan, B. P. Vickery, A. M. Scurlock, A. Wesley Burks, et al. 2012. Evidence of pathway‐specific basophil anergy induced by peanut oral immunotherapy in peanut-allergic children. Clinical and Experimental Allergy 42 (8):1197–205. doi: 10.1111/j.1365-2222.2012.04028.x.
  • Tomm, J. M., C. Krause, J. C. Simon, R. Treudler, M. von Bergen, and M. Averbeck. 2013. Pyruvate kinase and phosphopyruvate hydratase as novel IgE reactive proteins in prawn. Journal of Investigational Allergology & Clinical Immunology 23 (6):443.
  • Tsabouri, S., M. Triga, M. Makris, D. Kalogeromitros, M. K. Church, and K. N. Priftis. 2012. Fish and shellfish allergy in children: Review of a persistent food allergy. Pediatric Allergy and Immunology 23 (7):608–15. doi: 10.1111/j.1399-3038.2012.01275.x.
  • Tsai, C. L., K. Perng, Y. C. Hou, C. J. Shen, I. N. Chen, and Y. T. Chen. 2023. Effect of species, muscle location, food processing and refrigerated storage on the fish allergens, tropomyosin and parvalbumin. Food Chemistry 402:134479. doi: 10.1016/j.foodchem.2022.134479.
  • Tsai, L. C., P. L. Chao, H. D. Shen, R. B. Tang, T. C. Chang, Z. N. Chang, M. W. Hung, B. L. Lee, and K. Y. Chua. 1998. Isolation and characterization of a novel 98 kDa Dermatophagoides farinae mite allergen. The Journal of Allergy and Clinical Immunology 102 (2):295–303. doi: 10.1016/s0091-6749(98)70099-5.
  • Untersmayr, E., K. Szalai, A. B. Riemer, W. Hemmer, I. Swoboda, B. Hantusch, I. Schöll, S. Spitzauer, O. Scheiner, R. Jarisch, et al. 2006. Mimotopes identify conformational epitopes on parvalbumin, the major fish allergen. Molecular Immunology 43 (9):1454–61. doi: 10.1016/j.molimm.2005.07.038.
  • van der Ventel, M. L., N. E. Nieuwenhuizen, F. Kirstein, C. Hikuam, M. F. Jeebhay, I. Swoboda, F. Brombacher, and A. L. Lopata. 2011. Differential responses to natural and recombinant allergens in a murine model of fish allergy. Molecular Immunology 48 (4):637–46. doi: 10.1016/j.molimm.2010.11.001.
  • van der Kleij, H. P. M., H. J. M. Warmenhoven, R. van Ree, S. A. Versteeg, R. H. H. Pieters, S. C. Dreskin, A. C. Knulst, E. van Hoffen, D. J. E. Opstelten, S. J. Koppelman, et al. 2019. Chemically modified peanut extract shows increased safety while maintaining immunogenicity. Allergy 74 (5):986–95. doi: 10.1111/all.13687.
  • Van Do, T., I. Hordvik, C. Endresen, and S. Elsayed. 2003. The major allergen (parvalbumin) of codfish is encoded by at least two isotypic genes: cDNA cloning, expression and antibody binding of the recombinant allergens. Molecular Immunology 39 (10):595–602. doi: 10.1016/s0161-5890(02)00200-6.
  • Van Do, T., S. Elsayed, E. Florvaag, I. Hordvik, and C. Endresen. 2005. Allergy to fish parvalbumins: Studies on the cross-reactivity of allergens from 9 commonly consumed fish. The Journal of Allergy and Clinical Immunology 116 (6):1314–20. doi: 10.1016/j.jaci.2005.07.033.
  • Vickery, B. P., J. Lin, M. Kulis, Z. Fu, P. H. Steele, S. M. Jones, A. M. Scurlock, G. Gimenez, L. Bardina, H. A. Sampson, et al. 2013. Peanut oral immunotherapy modifies IgE and IgG4 responses to major peanut allergens. The Journal of Allergy and Clinical Immunology 131 (1):128–34. doi: 10.1016/j.jaci.2012.10.048.
  • Wakabayashi, T. 2015. Mechanism of the calcium-regulation of muscle contraction – In pursuit of its structural basis. Proceedings of the Japan Academy. Series B, Physical and Biological Sciences 91 (7):321–50. doi: 10.2183/pjab.91.321.
  • Wai, C. Y., N. Y. Leung, M. H. Ho, L. J. Gershwin, S. A. Shu, P. S. Leung, and K. H. Chu. 2014. Immunization with hypoallergens of shrimp allergen tropomyosin inhibits shrimp tropomyosin specific IgE reactivity. PLoS One 9 (11):e111649. doi: 10.1371/journal.pone.0111649.
  • Wai, C. Y. Y., N. Y. H. Leung, A. S. Y. Leung, S. M. Ngai, P. Pacharn, Y. S. Yau, J. S. D. Rosa Duque, M. Y. W. Kwan, O. Jirapongsananuruk, W. H. Chan, et al. 2022. Comprehending the allergen repertoire of shrimp for precision molecular diagnosis of shrimp allergy. Allergy 77 (10):3041–51. doi: 10.1111/all.15370.
  • Wai, C. Y. Y., N. Y. H. Leung, P. S. C. Leung, and K. H. Chu. 2016. T cell epitope immunotherapy ameliorates allergic responses in a murine model of shrimp allergy. Clinical and Experimental Allergy 46 (3):491–503. doi: 10.1111/cea.12684.
  • Wambre, E., J. H. DeLong, E. A. James, N. Torres-Chinn, W. Pfützner, C. Möbs, S. R. Durham, S. J. Till, D. Robinson, and W. W. Kwok. 2014. Specific immunotherapy modifies allergen-specific CD4+ T-cell responses in an epitope-dependent manner. The Journal of Allergy and Clinical Immunology 133 (3):872–9.e7. doi: 10.1016/j.jaci.2013.10.054.
  • Wang, B., Z. X. Li, L. Zheng, Y. Liu, and H. Lin. 2011. Identification and characterization of a new IgE-binding protein in mackerel (Scomber japonicus) by MALDI-TOF-MS. Journal of Ocean University of China 10 (1):93–8. doi: 10.1007/s11802-011-1793-6.
  • Wang, S., J. C. Delgado, E. Ravkov, D. D. Eckels, A. Georgelas, I. Y. Pavlov, M. Cusick, K. Sebastian, G. J. Gleich, and L. A. Wagner. 2012. Penaeus monodon tropomyosin induces CD4 T-cell proliferation in shrimp-allergic patients. Human Immunology 73 (4):426–31. doi: 10.1016/j.humimm.2011.12.019.
  • Wang, Y., J. Ma, H. Li, J. Zhou, H. Zhang, and L. Fu. 2021. A sensitive immunosensor based on FRET between gold nanoparticles and InP/ZnS quantum dots for arginine kinase detection. Food Chemistry 354:129536. doi: 10.1016/j.foodchem.2021.129536.
  • Warren, C. M., O. N. Aktas, R. S. Gupta, and C. M. Davis. 2019. Prevalence and characteristics of adult shellfish allergy in the United States. The Journal of Allergy and Clinical Immunology 144 (5):1435–8.e5. doi: 10.1016/j.jaci.2019.07.031.
  • White, A. J., M. J. Northcutt, S. E. Rohrback, R. O. Carpenter, M. M. Niehaus-Sauter, Y. Gao, M. G. Wheatly, and C. M. Gillen. 2011. Characterization of sarcoplasmic calcium binding protein (SCP) variants from freshwater crayfish Procambarus clarkii. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology 160 (1):8–14. doi: 10.1016/j.cbpb.2011.04.003.
  • Wijaya, H., S. Putriani, M. Safithri, and K. Tarman. 2020. Isolation and allergenicity of protein collagen from Parang-Parang fish skin (Cirocentrus dorab). IOP Conference Series: Earth and Environmental Science 411 (1):012054. doi: 10.1088/1755-1315/411/1/012054.
  • Wright, B. L., M. Kulis, K. A. Orgel, A. W. Burks, P. Dawson, A. K. Henning, S. M. Jones, R. A. Wood, S. H. Sicherer, R. W. Lindblad, et al. 2016. Component‐resolved analysis of IgA, IgE, and IgG4 during egg OIT identifies markers associated with sustained unresponsiveness. Allergy 71 (11):1552–60. doi: 10.1111/all.12895.
  • Wu, C. C., C. H. Lee, Y. C. Tyan, E. S. Huang, W. T. Yu, and H. S. Yu. 2019. Identification of pyruvate kinase 2 as a possible crab allergen and analysis of allergenic proteins in crabs consumed in Taiwan. Food Chemistry 289:413–8. doi: 10.1016/j.foodchem.2019.03.074.
  • Wu, C. H., M. F. Lee, S. C. Liao, and S. F. Luo. 1996. Sequencing analysis of cDNA clones encoding the American cockroach Cr-PI allergens: Homology with insect hemolymph proteins. The Journal of Biological Chemistry 271 (30):17937–43. doi: 10.1074/jbc.271.30.17937.
  • Wu, Y., Y. Lu, Y. Huang, H. Lin, M. Xu, I. Ahmed, G. Chen, Y. Chen, and Z. Li. 2022. Fish allergens of turbot (Scophthalmus maximus) parvalbumin triggers food allergy via inducing maturation of bone marrow derived dendritic cells and driving Th2 immune response. Food & Function 13 (7):4194–204. doi: 10.1039/d1fo04070g.
  • Xia, F., M.-S. Li, Q.-M. Liu, M. Liu, Y. Yang, M.-J. Cao, G.-X. Chen, T. Jin, and G.-M. Liu. 2019. Crystal structure analysis and conformational epitope mutation of triosephosphate isomerase, a mud crab allergen. Journal of Agricultural and Food Chemistry 67 (46):12918–26. doi: 10.1021/acs.jafc.9b05279.
  • Xu, L. L., J. Chen, L. R. Sun, X. Gao, H. Lin, I. Ahmed, S. N. Pramod, and Z. X. Li. 2020. Analysis of the allergenicity and B cell epitopes in tropomyosin of shrimp (Litopenaeus vannamei) and correlation to cross-reactivity based on epitopes with fish (Larimichthys crocea) and clam (Ruditapes philippinarum). Food Chemistry 323:126763. doi: 10.1016/j.foodchem.2020.126763.
  • Xu, L. L., M. Gasset, H. Lin, C. Yu, J. L. Zhao, X. W. Dang, and Z. X. Li. 2021. Identification of the dominant T-cell epitopes of Lit v 1 shrimp major allergen and their functional overlap with known B-cell epitopes. Journal of Agricultural and Food Chemistry 69 (26):7420–8. doi: 10.1021/acs.jafc.1c02231.
  • Yang, Y., M. J. Cao, M. Alcocer, Q. M. Liu, D. X. Fei, H. Y. Mao, and G. M. Liu. 2015. Mapping and characterization of antigenic epitopes of arginine kinase of Scylla paramamosain. Molecular Immunology 65 (2):310–20. doi: 10.1016/j.molimm.2015.02.010.
  • Yang, Y., Z.-W. Chen, B. K. Hurlburt, G.-L. Li, Y.-X. Zhang, D.-X. Fei, H.-W. Shen, M.-J. Cao, and G.-M. Liu. 2017. Identification of triosephosphate isomerase as a novel allergen in Octopus fangsiao. Molecular Immunology 85:35–46. doi: 10.1016/j.molimm.2017.02.004.
  • Yang, Y., M. J. Hu, T. C. Jin, Y. X. Zhang, G. Y. Liu, Y. B. Li, M. L. Zhang, M. J. Cao, W. J. Su, and G. M. Liu. 2019. A comprehensive analysis of the allergenicity and IgE epitopes of myosinogen allergens in Scylla paramamosain. Clinical and Experimental Allergy 49 (1):108–19. doi: 10.1111/cea.13266.
  • Yang, Y., H. Y. Liu, W. Zeng, Y. J. Yang, J. Zhang, J. Yin, J. L. Wu, and K. F. Lai. 2021. Characterization and epitope prediction of phosphopyruvate hydratase from Penaeus monodon (black tiger shrimp). Journal of Food Science 86 (8):3457–66. doi: 10.1111/1750-3841.15819.
  • Yang, Y., G.-Y. Liu, H. Yang, M.-J. Hu, M.-J. Cao, W.-J. Su, T. Jin, and G.-M. Liu. 2019. Crystal structure determination of Scylla paramamosain arginine kinase, an allergen that may cause cross-reactivity among invertebrates. Food Chemistry 271:597–605. doi: 10.1016/j.foodchem.2018.08.003.
  • Yang, Y., H.-F. Yan, Y.-X. Zhang, H.-L. Chen, M.-J. Cao, M.-S. Li, M.-L. Zhang, X.-R. He, and G.-M. Liu. 2020. Expression and epitope identification of myosin light chain isoform 1, an allergen in Procambarus clarkii. Food Chemistry 317:126422. doi: 10.1016/j.foodchem.2020.126422.
  • Yang, Y., Y.-X. Zhang, M. Liu, S. J. Maleki, M.-L. Zhang, Q.-M. Liu, M.-J. Cao, W.-J. Su, and G.-M. Liu. 2017. Triosephosphate isomerase and filamin C share common epitopes as novel allergens of Procambarus clarkii. Journal of Agricultural and Food Chemistry 65 (4):950–63. doi: 10.1021/acs.jafc.6b04587.
  • Yang, Y., D. Zhao, L. Zhou, T. Zhang, Z. Liu, B. Wu, T. Yu, Y. Zheng, and X. Sun. 2022. Molecular characterization and expression pattern of paramyosin in larvae and adults of Yesso scallop. Biology 11 (3):453. doi: 10.3390/biology11030453.
  • Yoshida, S., A. Ichimura, and K. Shiomi. 2008. Elucidation of a major IgE epitope of Pacific mackerel parvalbumin. Food Chemistry 111 (4):857–61. doi: 10.1016/j.foodchem.2008.04.062.
  • Yu, C., X. Gao, H. Lin, L. Xu, I. Ahmed, M. U. Khan, M. Xu, Y. Chen, and Z. Li. 2020. Purification, characterization, and three-dimensional structure prediction of paramyosin, a novel allergen of Rapana venosa. Journal of Agricultural and Food Chemistry 68 (49):14632–42. doi: 10.1021/acs.jafc.0c04418.
  • Yu, C. J., Y. F. Lin, B. L. Chiang, and L. P. Chow. 2003. Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. Journal of Immunology 170 (1):445–53. doi: 10.4049/jimmunol.170.1.445.
  • Zeng, G. Q., J. Y. Luo, H. M. Huang, P. Y. Zheng, W. T. Luo, N. L. Wei, and B. Q. Sun. 2015. Food allergy and related risk factors in 2540 preschool children: An epidemiological survey in Guangdong Province, southern China. World Journal of Pediatrics 11 (3):219–25. doi: 10.1007/s12519-015-0030-6.
  • Zhang, X., Y. Li, Y. Tao, Y. Wang, C. Xu, and Y. Lu. 2021. A novel method based on infrared spectroscopic inception-resnet networks for the detection of the major fish allergen parvalbumin. Food Chemistry 337:127986. doi: 10.1016/j.foodchem.2020.127986.
  • Zhang, Y. X., H. L. Chen, S. J. Maleki, M. J. Cao, L. J. Zhang, W. J. Su, and G. M. Liu. 2015. Purification, characterization, and analysis of the allergenic properties of myosin light chain in Procambarus clarkii. Journal of Agricultural and Food Chemistry 63 (27):6271–82. doi: 10.1021/acs.jafc.5b01318.
  • Zhang, Y., Y. Ren, Y. Bi, Q. Wang, K. W. Cheng, and F. Chen. 2019. Seafood allergy and potential application of high hydrostatic pressure to reduce seafood allergenicity. International Journal of Food Engineering 15 (8):1–12. doi: 10.1515/ijfe-2018-0392.
  • Zhang, Y., L. Zhu, S. Li, J. Zhang, T. She, J. Yan, Y. Bian, and H. Li. 2016. Identification of the major allergenic epitopes of Eriocheir sinensis roe hemocyanin: A novel tool for food allergy diagnoses. Molecular Immunology 74:125–32. doi: 10.1016/j.molimm.2016.05.003.
  • Zhang, Z. Y., X. M. Li, Z. X. Li, and H. Lin. 2021. Investigation of glycated shrimp tropomyosin as a hypoallergen for potential immunotherapy. Food & Function 12 (6):2750–9. doi: 10.1039/d0fo03039b.
  • Zhang, Z. Y., X. M. Li, H. Xiao, A. Nowak-Wegrzyn, and P. Zhou. 2020. IgE-binding epitope mapping of tropomyosin allergen (Exo m 1) from Exopalaemon modestus, the freshwater Siberian prawn. Food Chemistry 309:125603. doi: 10.1016/j.foodchem.2019.125603.
  • Zhang, Z. Y., X. F. Zhang, W. Chen, and P. Zhou. 2018. Conformation stability, in vitro digestibility and allergenicity of tropomyosin from shrimp (Exopalaemon modestus) as affected by high intensity ultrasound. Food Chemistry 245:997–1009. doi: 10.1016/j.foodchem.2017.11.072.
  • Zheng, L. N., H. Lin, R. Pawar, Z. X. Li, and M. H. Li. 2011. Mapping IgE binding epitopes of major shrimp (Penaeus monodon) allergen with immunoinformatics tools. Food and Chemical Toxicology 49 (11):2954–60. doi: 10.1016/j.fct.2011.07.043.
  • Zuidmeer-Jongejan, L., H. Huber, I. Swoboda, N. Rigby, S. A. Versteeg, B. M. Jensen, S. Quaak, J. H. Akkerdaas, L. Blom, J. Asturias, et al. 2015. Development of a hypoallergenic recombinant parvalbumin for first-in-man subcutaneous immunotherapy of fish allergy. International Archives of Allergy and Immunology 166 (1):41–51. doi: 10.1159/000371657.

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