Due to the rapid growth of the world’s population and the increasing demand for food, there is an urgent need for alternative, more sustainable sources of protein. Insects have an important role in the diet in some societies and current initiatives are exploring the potential that insects have to offer for the production of food and feed. In this context, the safety implications of both producing and consuming insects are an important aspect to investigate. Here we present a bioinformatics analysis of proteomics data obtained for larvae of four different species of fly to assess the homology of tropomyosin, arginine kinase and myosin light chain with the crustacean orthologous proteins and other known allergenic proteins. The results indicate that the three proteins share homology with known allergens and therefore it is likely that they are also potential allergens. The implications in relation to mass rearing of flies are discussed.
Aalberse, R.C. and Stadler, B.M., 2006. In silico predictability of allergenicity: from amino acid sequence via 3D structure to allergenicity. Molecular Nutrition and Food Research 50: 625-627.
'In silico predictability of allergenicity: from amino acid sequence via 3D structure to allergenicity ' () 50 Molecular Nutrition and Food Research : 625 -627.
Aki, T., Kodama, T., Fujikawa, A., Miura, K., Shigeta, S., Wada, T., Jyo, T., Murooka, Y., Oka, S. and Ono, K., 1995. Immunochemical characterization of recombinant and native tropomyosins as a new allergen from the house dust mite,Dermatophagoides farinae. Journal of Allergy and Clinical Immunology 96: 74-83.
'Immunochemical characterization of recombinant and native tropomyosins as a new allergen from the house dust mite,Dermatophagoides farinae ' () 96 Journal of Allergy and Clinical Immunology : 74 -83.
Ayuso, R., Grishina, G., Bardina, L., Carrillo, T., Blanco, C., Ibáñez, M.D., Sampson, H.A. and Beyer, K., 2008. Myosin light chain is a novel shrimp allergen, Lit v 3. Journal of Allergy and Clinical Immunology 122: 795-802.
'Myosin light chain is a novel shrimp allergen, Lit v 3 ' () 122 Journal of Allergy and Clinical Immunology : 795 -802.
Ayuso, R., Lehrer, S.B. and Reese, G., 2002a. Identification of continuous, allergenic regions of the major shrimp allergen Pen a 1 (tropomyosin). International Archives of Allergy and Immunology 127: 27-37.
'Identification of continuous, allergenic regions of the major shrimp allergen Pen a 1 (tropomyosin) ' () 127 International Archives of Allergy and Immunology : 27 -37.
Ayuso, R., Reese, G., Leong-Kee, S., Plante, M. and Lehrer, S.B., 2002b. Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactivity epitopes of shrimp, house dust mite and cockroach tropomyosins. International Archives of Allergy and Immunology 129: 38-48.
'Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactivity epitopes of shrimp, house dust mite and cockroach tropomyosins ' () 129 International Archives of Allergy and Immunology : 38 -48.
Belkaid, Y., Valenzuela, J.G., Kamhawi, S., Rowton, E., Sacks, D.L. and Ribeiro, J.M., 2000. Delayed-type hypersensitivity toPhlebotomus papatasi sand fly bite: an adaptive response induced by the fly? Proceedings of the National Academy of Sciences of the United States of America 97: 6704-6709.
'Delayed-type hypersensitivity toPhlebotomus papatasi sand fly bite: an adaptive response induced by the fly? ' () 97 Proceedings of the National Academy of Sciences of the United States of America : 6704 -6709.
Binder, M., Mahler, V., Hayek, B., Sperr, W.R., Schöller, M., Prozell, S., Wiedermann, G., Valent, P., Valenta, R. and Duchêne, M., 2001. Molecular and immunological characterization of arginine kinase from indian meal moth,Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen. Journal of Immunology 167: 5470-5477.
'Molecular and immunological characterization of arginine kinase from indian meal moth,Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen ' () 167 Journal of Immunology : 5470 -5477.
Bonds, R.S., Midoro-Horiuti, T. and Goldblum, R., 2008. A structural basis for food allergy: the role of cross-reactivity. Current Opinion in Allergy and Clinical Immunology 8: 82-86.
'A structural basis for food allergy: the role of cross-reactivity ' () 8 Current Opinion in Allergy and Clinical Immunology : 82 -86.
Charlton, A.J., Dickinson, M., Wakefield, M.E., Fitches, E., Kenis, M., Han, R., Zhu, F., Kone, N., Grant, M., Devic, E., Bruggeman, G., Prior, R. and Smith, R., 2015. Exploring the chemical safety of fly larvae as a source of protein for animal feed. Journal of Insects as Food and Feed 1: 7-16.
'Exploring the chemical safety of fly larvae as a source of protein for animal feed ' () 1 Journal of Insects as Food and Feed : 7 -16.
Daul, C.B., Slattery, M., Reese, G. and Lehrer, S.B., 1994. Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. International Archives of Allergy and Immunology 105: 49-55.
'Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin ' () 105 International Archives of Allergy and Immunology : 49 -55.
European Food Safety Authority (EFSA), 2010. Scientific opinion on the assessment of allergenicity of GM plants and microorganisms and derived food and feed. EFSA Journal 8: 1700.
Fernandes, J., Reshef, A., Patton, L., Ayuso, R., Reese, G. and Lehrer, S.B., 2003. Immunoglobulin E antibody reactivity to the major shrimp allergen, tropomyosin, in unexposed Orthodox Jews. Clinical and Experimental Allergy 33: 956-961.
'Immunoglobulin E antibody reactivity to the major shrimp allergen, tropomyosin, in unexposed Orthodox Jews ' () 33 Clinical and Experimental Allergy : 956 -961.
Fiers, M.W.E.J., Kleter, G.A., Nijland, H., Peijnenburg, A.A.C.M., Nap, J.P. and Van Ham, R.C.H.J., 2004. Allermatch™, a webtool for the prediction of potential allergenicity according to current FAO/WHO Codex alimentarius guidelines. BMC Bioinformatics 5: 133.
'Allermatch™, a webtool for the prediction of potential allergenicity according to current FAO/WHO Codex alimentarius guidelines ' () 5 BMC Bioinformatics : 133.
Food and Agriculture Organisation/World Health Organisation (FAO/WHO), 2001. Evaluation of allergenicity of genetically modified foods. Report of a Joint FAO/WHO Expert Consultation of Allergenicity of Foods Derived from Biotechnology, pp. 1-27.
García-Orozco, K.D., Aispuro-Hernandez, E., Yepiz-Plascencia, G., Calderón-de-la-Barca and A.M., Sotelo-Mundo, R.R., 2007. Molecular characterization of arginine kinase, an allergen from the shrimpLitopenaeus vannamei. International Archives of Allergy and Immunology 144: 23-28.
'Molecular characterization of arginine kinase, an allergen from the shrimpLitopenaeus vannamei ' () 144 International Archives of Allergy and Immunology : 23 -28.
Hindley, J., Wünschmann, S., Satinover, S.M., Woodfolk, J.A., Chew, F.T., Chapman, M.D. and Pomés, A., 2006. Bla g 6: a troponin C allergen fromBlattella germanica with IgE binding calcium dependence. Journal of Allergy and Clinical Immunology 117: 1389-1395.
'Bla g 6: a troponin C allergen fromBlattella germanica with IgE binding calcium dependence ' () 117 Journal of Allergy and Clinical Immunology : 1389 -1395.
Huang, Y.Y., Liu, G.M., Cai, Q.F., Weng, W.Y., Maleki, S.J., Su, W.J. and Cao, M.J., 2010. Stability of major allergen tropomyosin and other food proteins of mud crab (Scylla serrata) byin vitro gastrointestinal digestion. Food and Chemical Toxicology 48: 1196-1201.
'Stability of major allergen tropomyosin and other food proteins of mud crab (Scylla serrata) byin vitro gastrointestinal digestion ' () 48 Food and Chemical Toxicology : 1196 -1201.
Liu, Z., Xia, L., Wu, Y., Chen, J. and Roux, K.H., 2009. Identification and characterization of an arginine kinase as a major allergen from silkworm (Bombyx mori) larvae. International archives of allergy and immunology 150: 8-14.
'Identification and characterization of an arginine kinase as a major allergen from silkworm (Bombyx mori) larvae ' () 150 International archives of allergy and immunology : 8 -14.
Martinez, A., Martinez, J., Palacios, R. and Panzani, R.C., 1997. Importance of tropomyosin in the allergy to household arthropods. Cross-reactivity with other invertebrate extracts. Allergologia et Immunopathologia 25: 118-126.
'Importance of tropomyosin in the allergy to household arthropods. Cross-reactivity with other invertebrate extracts ' () 25 Allergologia et Immunopathologia : 118 -126.
Ramirez, D.A. Jr. and Bahna, S.L., 2009. Food hypersensitivity by inhalation. Clinical and Molecular Allergy 7: 4.
'Food hypersensitivity by inhalation ' () 7 Clinical and Molecular Allergy : 4.
Schroeckenstein, D.C., Meier-Davis, S. and Bush, R.K. 1990. Occupational sensitivity toTenebrio molitor Linnaeus (yellow mealworm). The Journal of Allergy and Clinical Immunology 86: 182-188.
'Occupational sensitivity toTenebrio molitor Linnaeus (yellow mealworm) ' () 86 The Journal of Allergy and Clinical Immunology : 182 -188.
Schroeckenstein, D.C., Meier-Davis, S. Graziano, F.M., Falomo, A. and Bush, R.K., 1988. Occupational sensitivity toAlphitobius diaperinus (Panzer) (lesser mealworm). The Journal of Allergy and Clinical Immunology 82: 1081-1088.
'Occupational sensitivity toAlphitobius diaperinus (Panzer) (lesser mealworm) ' () 82 The Journal of Allergy and Clinical Immunology : 1081 -1088.
Shafique, R.H., Inam, M., Ismail, M. and Chaudhary, F.R., 2012. Group 10 allergens (tropomyosins) from house-dust mites may cause covariation of sensitization to allergens from other invertebrates. Allergy and Rhinology 3: e74-e90.
'Group 10 allergens (tropomyosins) from house-dust mites may cause covariation of sensitization to allergens from other invertebrates ' () 3 Allergy and Rhinology : e74 -e90.
Shanti, K.N,. Martin, B.M., Nagpal, S., Metcalfe, D.D. and Rao, P.V., 1993. Identification of tropomyosin as the major shrimp allergen and characterization of its IgE binding epitopes. Journal of Immunology 151: 5354-5363.
'Identification of tropomyosin as the major shrimp allergen and characterization of its IgE binding epitopes ' () 151 Journal of Immunology : 5354 -5363.
Shiomi, K., Sato, Y., Hamamoto, S., Mita, H. and Shimakura, K., 2008. Sarcoplasmic calcium-binding protein: identification as a new allergen of the black tiger shrimpPenaeus monodon. International Archives of Allergy and Immunology 146: 91-98.
'Sarcoplasmic calcium-binding protein: identification as a new allergen of the black tiger shrimpPenaeus monodon ' () 146 International Archives of Allergy and Immunology : 91 -98.
Smith, W., Mills, K.L., Hazell, L.A., Hart, B.J. and Thomas, W.R., 1999. Molecular analysis of the group 1 and 2 allergens from the house dust mite,Euroglyphus maynei. International Archives of Allergy and Immunology 118: 15-22.
'Molecular analysis of the group 1 and 2 allergens from the house dust mite,Euroglyphus maynei ' () 118 International Archives of Allergy and Immunology : 15 -22.
Srinroch, C., Srisomsap, C., Chokchaichamnankit, D., Punyarit, P. and Phiriyangkul, P., 2015. Identification of novel allergen in edible insect,Gryllus bimaculatus and its cross-reactivity withMacrobrachium spp. allergens. Food Chemistry 184: 160-166.
'Identification of novel allergen in edible insect,Gryllus bimaculatus and its cross-reactivity withMacrobrachium spp. allergens ' () 184 Food Chemistry : 160 -166.
Tsabouri, S., Triga, M., Makris, M., Kalogeromitros, D., Church, M.K. and Priftis, K.N., 2012. Fish and shellfish allergy in children: review of a persistent food allergy. Pediatric Allergy and Immunology 23: 608-615.
'Fish and shellfish allergy in children: review of a persistent food allergy ' () 23 Pediatric Allergy and Immunology : 608 -615.
Van Huis, A., 2013. Potential of insects as food and feed in assuring food security. Annual Review of Entomology 58: 563-583.
'Potential of insects as food and feed in assuring food security ' () 58 Annual Review of Entomology : 563 -583.
Van Huis, A., Van Itterbeeck, J., Klunder, H., Mertens, E., Halloran, A., Muir, G. and Vantomme, P., 2013. Edible insects: future prospects for food and feed security. Food and Agriculture Organization of the United Nations (FAO), Rome, Italy, FAO Forestry Paper no. 171, 201 pp. Available at:http://www.fao.org/docrep/018/i3253e/i3253e.pdf.
Verhoeckx, K.C.M, Van Broekhoven, S., Den Hartog-Jager, C.F., Gaspari, M., De Jong, G.A.H., Wichers, H.J., Van Hoffen, E., Houben, G.F. and Knulst, A.C., 2014. House dust mite (Der p 10) and crustacean allergic patients may react to food containing Yellow mealworm proteins. Food and Chemical Toxicology 65: 364-373.
'House dust mite (Der p 10) and crustacean allergic patients may react to food containing Yellow mealworm proteins ' () 65 Food and Chemical Toxicology : 364 -373.
Witteman, A.M., Akkerdaas, J.H., Van Leeuwen, J., Van der Zee, J.S. and Aalberse, R.C., 1994. Identification of a cross-reactive allergen (presumably tropomyosin) in shrimp, mite and insects. International Archives of Allergy and Immunology 105: 56-61.
'Identification of a cross-reactive allergen (presumably tropomyosin) in shrimp, mite and insects ' () 105 International Archives of Allergy and Immunology : 56 -61.
Woo, C.K. and Bahna, S.L., 2011. Not all shellfish ‘allergy’ is allergy! Clinical and Translational Allergy 1: 3.
'Not all shellfish ‘allergy’ is allergy! ' () 1 Clinical and Translational Allergy : 3.
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Due to the rapid growth of the world’s population and the increasing demand for food, there is an urgent need for alternative, more sustainable sources of protein. Insects have an important role in the diet in some societies and current initiatives are exploring the potential that insects have to offer for the production of food and feed. In this context, the safety implications of both producing and consuming insects are an important aspect to investigate. Here we present a bioinformatics analysis of proteomics data obtained for larvae of four different species of fly to assess the homology of tropomyosin, arginine kinase and myosin light chain with the crustacean orthologous proteins and other known allergenic proteins. The results indicate that the three proteins share homology with known allergens and therefore it is likely that they are also potential allergens. The implications in relation to mass rearing of flies are discussed.
All Time | Past 365 days | Past 30 Days | |
---|---|---|---|
Abstract Views | 0 | 0 | 0 |
Full Text Views | 77 | 51 | 19 |
PDF Views & Downloads | 91 | 70 | 17 |