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Veterinary dermatology, v.30 no.1, 2019년, pp.25 - e8
Bexley, Jennifer (Avacta Animal Health, Unit 651, Street 5, Thorp Arch Estate, Wetherby, Yorkshire, LS23 7FZ, UK) , Kingswell, Nicola (Avacta Animal Health, Unit 651, Street 5, Thorp Arch Estate, Wetherby, Yorkshire, LS23 7FZ, UK) , Olivry, Thierry (Department of Clinical Sciences, College of Veterinary Medicine, North Carolina State University, Research Building, 1060 William Moore Drive, Raleigh, NC, 27606, USA)
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BackgroundIn humans, a cross‐reactive clinical allergy has been reported between three chicken and fish meat proteins: beta‐enolase, aldolase A and parvalbumin.ObjectiveTo evaluate if IgE cross‐reactivity between chicken and fish also existed in the dog.AnimalsSera from dogs with s...
RésuméContexteChez l'homme, une allergie clinique réactive croisée a été décrite entre trois protéines de poulet et de poisson : beta‐énolase, aldolase A et parvalbumine.ObjectifEvaluer si la réactivité croisée IgE entre le poulet et le poisson existe aussi chez le chien.SujetsLes sera de chiens suspects de dermatose allergique avec des IgE anti‐poulet et poisson.Matériel et méthodeLes sera ont été analysés par ELISA et immunoblotting avec le poulet, le poisson blanc (haddock et morue) et le saumon. Les ELISA inhibiteur réciproque et l'immunoblotting inhibiteur ont été réalisés. Le séquençage des protéines et l'identification des bandes sur extraits multiples a été déterminé par spectrométrie de masse.RésultatsSur les 53 sera canins archivés testés par ELISA contre le poulet, le poisson blanc et le saumon, respectivement, 15 (28%), 12 (23%) et 26 (49%), avaient des IgE élevés contre un, deux ou les trois extraits. Sept des sera triple‐réactifs ont été soumis à l’ELISA d'inhibition réciproque. Une inhibition >50% a été trouvée entre le poulet‐poisson, poulet‐saumon et poisson blanc‐saumon respectivement pour les sept, quatre et cinq des sept chiens. L'immunoblotting a identifié les protéines porteuses d'IgE multiple comme des protéines de poids moléculaire identiques dans trois extraits ; ceux‐ci ont été partiellement à totalement cross‐réactifs par immunoblotting inhibiteur. La spectrométrie de masse a identifié neuf protéines cross‐réactives : pyruvate kinase, créatine kinase, alpha‐actine, glyceraldehyde‐3‐phosphate dehydrogénase, beta‐énolase, aldolase, malate dehydrogénase, lactate dehydrogénase et triose‐phosphate isomérase 1. Tous ces éléments ont été rapportés précédemment chez l'homme pour les allergènes de poisson, les crustacés et /ou le poulet.Conclusion et importance clinqueSi un de ces nouveaux allergènes cross‐réactifs poulet‐poisson est la cause d'allergie clinique doit être déterminée chez les chiens réagissant à au moins deux de ces sources fréquentes de nourriture.
Olivry, Thierry, Mueller, Ralf S.. Critically appraised topic on adverse food reactions of companion animals (3): prevalence of cutaneous adverse food reactions in dogs and cats. BMC veterinary research, vol.13, 51-.
Comp Med Jackson HA 316 52 2002 Evaluation of a spontaneous canine model of immunoglobulin E‐mediated food hypersensitivity: dynamic changes in serum and fecal allergen‐specific immunoglobulin E values relative to dietary change
Jackson, H. A., Jackson, M. W., Coblentz, L., Hammerberg, B.. Evaluation of the clinical and allergen specific serum immunoglobulin E responses to oral challenge with cornstarch, corn, soy and a soy hydrolysate diet in dogs with spontaneous food allergy. Veterinary dermatology, vol.14, no.4, 181-187.
Ishida, Rinei, Masuda, Kenichi, Kurata, Keigo, Ohno, Koichi, Tsujimoto, Hajime. Lymphocyte Blastogenic Responses to Inciting Food Allergens in Dogs with Food Hypersensitivity. Journal of veterinary internal medicine, vol.18, no.1, 25-30.
Bexley, Jennifer, Nuttall, Timothy J., Hammerberg, Bruce, Halliwell, Richard E.. Co‐sensitization and cross‐reactivity between related and unrelated food allergens in dogs – a serological study. Veterinary dermatology, vol.28, no.1, 31-e7.
MARTÍN, ÁUREA, SIERRA, MARÍA-PAZ, GONZÁLEZ, JOSÉ L., ARÉVALO, MARÍA-ÁNGELES. Identification of allergens responsible for canine cutaneous adverse food reactions to lamb, beef and cow's milk. Veterinary dermatology, vol.15, no.6, 349-356.
OHMORI, Keitaro, MASUDA, Kenichi, KAWARAI, Shinpei, YASUDA, Nobutaka, SAKAGUCHI, Masahiro, TSUJIMOTO, Hajime. Identification of Bovine Serum Albumin as an IgE-Reactive Beef Component in a Dog with Food Hypersensitivity against Beef. The Journal of veterinary medical science, vol.69, no.8, 865-867.
Vincent, Delphine, Elkins, Aaron, Condina, Mark R., Ezernieks, Vilnis, Rochfort, Simone. Quantitation and Identification of Intact Major Milk Proteins for High-Throughput LC-ESI-Q-TOF MS Analyses. PloS one, vol.11, no.10, e0163471-.
Kelso,. Pollen-food allergy syndrome. Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, vol.30, no.7, 905-907.
Hilger, C., Thill, L., Grigioni, F., Lehners, C., Falagiani, P., Ferrara, A., Romano, C., Stevens, W., Hentges, F.. IgE antibodies of fish allergic patients cross-react with frog parvalbumin. Allergy, vol.59, no.6, 653-660.
Kuehn, A., Lehners, C., Hilger, C., Hentges, F.. Food allergy to chicken meat with IgE reactivity to muscle α‐parvalbumin. Allergy, vol.64, no.10, 1557-1558.
Hemmer, Wolfgang, Klug, Christoph, Swoboda, Ines. Update on the bird-egg syndrome and genuine poultry meat allergy. Allergo journal international, vol.25, 68-75.
Kuehn, A., Codreanu‐Morel, F., Lehners‐Weber, C., Doyen, V., Gomez‐André, S.‐A., Bienvenu, F., Fischer, J., Ballardini, N., van Hage, M., Perotin, J.‐M., Silcret‐Grieu, S., Chabane, H., Hentges, F., Ollert, M., Hilger, C., Morisset, M.. Cross‐reactivity to fish and chicken meat – a new clinical syndrome. Allergy, vol.71, no.12, 1772-1781.
J Invest Allergol Clin Immunol González‐de‐Olano D 215 22 2012 Asthma after chicken consumption due to cross‐reactivity between fish and chicken parvalbumin
J Investig Allergol Clin Immunol Alvarez‐Perea A 209 24 2014 Pork‐cat syndrome as a cause of occupational asthma
Quirce, S., Marañón, F., Umpiérrez, A., De Las Heras, M., Fernández‐Caldas, E., Sastre, J.. Chicken serum albumin (Gal d 5*) is a partially heat‐labile inhalant and food allergen implicated in the bird‐egg syndrome. Allergy, vol.56, no.8, 754-762.
Hilger, C., Swiontek, K., Hentges, F., Donnay, C., de Blay, F., Pauli, G.. Occupational Inhalant Allergy to Pork followed by Food Allergy to Pork and Chicken: Sensitization to Hemoglobin and Serum Albumin. International archives of allergy and immunology, vol.151, no.2, 173-178.
Mueller, Ralf S., Olivry, Thierry, Prélaud, Pascal. Critically appraised topic on adverse food reactions of companion animals (2): common food allergen sources in dogs and cats. BMC veterinary research, vol.12, 9-.
Olivry, Thierry, Bexley, Jennifer, Mougeot, Isabelle. Extensive protein hydrolyzation is indispensable to prevent IgE-mediated poultry allergen recognition in dogs and cats. BMC veterinary research, vol.13, 251-.
J Investig Allergol Clin Immunol Tomm JM 443 23 2013 Pyruvate kinase and phosphopyruvate hydratase as novel IgE reactive proteins in prawn
Lee, Chih-Hung, Wu, Chia-Ching, Tyan, Yu-Chang, Yu, Wei-Tai, Huang, Edward S., Yu, Hsu-Sheng. Identification of pyruvate kinase as a novel allergen in whiteleg shrimp (Litopenaeus vannamei) by specific-IgE present in patients with shrimp allergy. Food chemistry, vol.258, 359-365.
Kuehn, A., Hilger, C., Lehners‐Weber, C., Codreanu‐Morel, F., Morisset, M., Metz‐Favre, C., Pauli, G., de Blay, F., Revets, D., Muller, C. P., Vogel, L., Vieths, S., Hentges, F.. 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 : journal of the British Society for Allergy and Clinical Immunology, vol.43, no.7, 811-822.
Nakamura, R., Satoh, R., Nakajima, Y., Kawasaki, N., Yamaguchi, T., Sawada, J.i., Nagoya, H., Teshima, R.. 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 : RTP, vol.55, no.3, 300-308.
Kuehn, Annette, Swoboda, Ines, Arumugam, Karthik, Hilger, Christiane, Hentges, François. Fish Allergens at a Glance: Variable Allergenicity of Parvalbumins, the Major Fish Allergens. Frontiers in immunology, vol.5, 179-.
Mohamad Yadzir, Zailatul Hani, Misnan, Rosmilah, Bakhtiar, Faizal, Abdullah, Noormalin, Murad, Shahnaz. Tropomyosin and Actin Identified as Major Allergens of the Carpet Clam ( Paphia textile ) and the Effect of Cooking on Their Allergenicity. BioMed research international, vol.2015, 254152-.
Abdel Rahman, A.M., Kamath, S.D., Lopata, A.L., Robinson, J.J., Helleur, R.J.. 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, vol.74, no.2, 231-241.
Restani, Patrizia, Ballabio, Cinzia, Tripodi, Salvatore, Fiocchi, Alessandro. Meat allergy. Current opinion in allergy and clinical immunology, vol.9, no.3, 265-269.
J Investig Allergol Clin Immunol Tomm JM 159 23 2013 Identification of new potential allergens from Nile perch (Lates niloticus) and cod (Gadus morhua)
van der Ventel, M.L., Nieuwenhuizen, N.E., Kirstein, F., Hikuam, C., Jeebhay, M.F., Swoboda, I., Brombacher, F., Lopata, A.L.. Differential responses to natural and recombinant allergens in a murine model of fish allergy. Molecular immunology, vol.48, no.4, 637-646.
Chen, Y.‐H., Lee, M.‐F., Lan, J.‐L., Chen, C.‐S., Wang, H.‐L., Hwang, G.‐Y., Wu, C.‐H.. Hypersensitivity to Forcipomyia taiwana (biting midge): clinical analysis and identification of major For t 1, For t 2 and For t 3 allergens. Allergy, vol.60, no.12, 1518-1523.
Bauermeister, K., Wangorsch, A., Garoffo, L.P., Reuter, A., Conti, A., Taylor, S.L., Lidholm, J., DeWitt, A.M., Enrique, E., Vieths, S., Holzhauser, T., Ballmer-Weber, B., Reese, G.. Generation of a comprehensive panel of crustacean allergens from the North Sea Shrimp Crangon crangon. Molecular immunology, vol.48, no.15, 1983-1992.
Hoppe, Sonja, Steinhart, Hans, Paschke, Angelika. Identification of a 28 kDa lychee allergen as a triose-phosphate isomerase. Food and agricultural immunology, vol.17, no.1, 9-19.
Sander, Ingrid, Flagge, Angelika, Merget, Rolf, Halder, Thomas M., Meyer, Helmut E., Baur, Xaver. Identification of wheat flour allergens by means of 2-dimensional immunoblotting. The Journal of allergy and clinical immunology : official organ of American Academy of Allergy, vol.107, no.5, 907-913.
Yang, Y., Chen, Z.W., Hurlburt, B.K., Li, G.L., Zhang, Y.X., Fei, D.X., Shen, H.W., Cao, M.J., Liu, G.M.. Identification of triosephosphate isomerase as a novel allergen in Octopus fangsiao. Molecular immunology, vol.85, 35-46.
A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: innate protection by antiproteases. The Journal of experimental medicine, vol.182, no.5, 1537-1544.
Shakib, Farouk, Schulz, Oliver, Sewell, Herb. A mite subversive: cleavage of CD23 and CD25 by Der p 1 enhances allergenicity. Immunology today, vol.19, no.7, 313-316.
Randall, Thomas A., London, Robert E., Fitzgerald, Michael C., Mueller, Geoffrey A.. Proteases of Dermatophagoides pteronyssinus. International journal of molecular sciences, vol.18, no.6, 1204-.
Ogburn, Ryenne N., Randall, Thomas A., Xu, Yingrong, Roberts, Julia H., Mebrahtu, Betelihem, Karnuta, Jaret M., Rider, S. Dean, Kissling, Grace E., London, Robert E., Pomés, Anna, Arlian, Larry, Fitzgerald, Michael C., Mueller, Geoffrey A.. Are dust mite allergens more abundant and/or more stable than other Dermatophagoides pteronyssinus proteins?. The Journal of allergy and clinical immunology : official organ of American Academy of Allergy, vol.139, no.3, 1030-1032.e1.
Lehesranta, Satu J., Davies, Howard V., Shepherd, Louise V.T., Nunan, Naoise, McNicol, Jim W., Auriola, Seppo, Koistinen, Kaisa M., Suomalainen, Soile, Kokko, Harri I., Kärenlampi, Sirpa O.. Comparison of Tuber Proteomes of Potato Varieties, Landraces, and Genetically Modified Lines. Plant physiology, vol.138, no.3, 1690-1699.
Wang, Xuchu, Chang, Lili, Tong, Zheng, Wang, Dongyang, Yin, Qi, Wang, Dan, Jin, Xiang, Yang, Qian, Wang, Liming, Sun, Yong, Huang, Qixing, Guo, Anping, Peng, Ming. Proteomics Profiling Reveals Carbohydrate Metabolic Enzymes and 14-3-3 Proteins Play Important Roles for Starch Accumulation during Cassava Root Tuberization. Scientific reports, vol.6, 19643-.
Kobayashi, Ayako, Kobayashi, Yukihiro, Shiomi, Kazuo. Fish allergy in patients with parvalbumin-specific immunoglobulin E depends on parvalbumin content rather than molecular differences in the protein among fish species. Bioscience, biotechnology, and biochemistry, vol.80, no.10, 2018-2021.
Kobayashi, Y., Yang, T., Yu, C.T., Ume, C., Kubota, H., Shimakura, K., Shiomi, K., Hamada-Sato, N.. Quantification of major allergen parvalbumin in 22 species of fish by SDS-PAGE. Food chemistry, vol.194, 345-353.
Griesmeier, U., Vázquez‐Cortés, S., Bublin, M., Radauer, C., Ma, Y., Briza, P., Fernández‐Rivas, M., Breiteneder, H.. Expression levels of parvalbumins determine allergenicity of fish species. Allergy, vol.65, no.2, 191-198.
D'Urbano, L. E., Pellegrino, K., Artesani, M. C., Donnanno, S., Luciano, R., Riccardi, C., Tozzi, A. E., Ravà, L., De Benedetti, F., Cavagni, G.. Performance of a component-based allergen-microarray in the diagnosis of cow's milk and hen's egg allergy. Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, vol.40, no.10, 1561-1570.
Klemans, R. J. B., van Os‐Medendorp, H., Blankestijn, M., Bruijnzeel‐Koomen, C. A. F. M., Knol, E. F., Knulst, A. C.. Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review. Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, vol.45, no.4, 720-730.
Sato, Sakura, Yanagida, Noriyuki, Ohtani, Kiyotaka, Koike, Yumi, Ebisawa, Motohiro. A review of biomarkers for predicting clinical reactivity to foods with a focus on specific immunoglobulin E antibodies. Current opinion in allergy and clinical immunology, vol.15, no.3, 250-258.
Patelis, A., Borres, M. P., Kober, A., Berthold, M.. Multiplex component‐based allergen microarray in recent clinical studies. Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, vol.46, no.8, 1022-1032.
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