Identification of immunogenic epitopes of two soybean glycinin proteins in chicken

References

• Badley, R. A., Atkinson, D., Hauser, H., Oldani, D., Green, J. P., & Stubbs, J. M. (1975). The structure, physical and chemical properties of the soy bean protein glycinin. Biochimica et Biophysica Acta (BBA) – Protein Structure, 412, 214–228. doi: 10.1016/0005-2795(75)90036-7
   PubMed Web of Science ®Google Scholar
• Bessler, M. H., Ricki, M., & Ogawa, T. (2000). Allergen data collection – Update: Soybean (Glycine max). International Symposium of Food Allergens, 2(3), 1–35.
   Google Scholar
• Codina, R., Ardusso, L., Lockey, R. F., Crisci, C., & Medina, I. (2003). Allergenicity of varieties of soybean. Allergy, 58, 1293–1298. doi: 10.1046/j.1398-9995.2003.00301.x
   PubMed Web of Science ®Google Scholar
• Fernando Guilherme Perazzo Costa, C. C. G., Figueiredo, D. F., Oliveira, C. F. S., & Silva, J. H. V. (2008). Economic and environmental impact of using exogenous enzymes on poultry feeding. International Journal of Poultry Science, 7(5), 311–315.
   Google Scholar
• Hamal, K. R., Burgess, S. C., Pevzner, I. Y., & Erf, G. F. (2006). Maternal antibody transfer from dams to their egg yolks, egg whites, and chicks in meat lines of chickens. Poultry Science, 85, 1364–1372. doi:10.1093/ps/85.8.1364% doi: 10.1093/ps/85.8.1364
   PubMed Web of Science ®Google Scholar
• Helm, R. M. (2002). Food allergy animal models. Annals of the New York Academy of Sciences, 964, 139–150. doi: 10.1111/j.1749-6632.2002.tb04139.x
   PubMed Web of Science ®Google Scholar
• Helm, R. M., Cockrell, G., Connaughton, C., Sampson, H. A., Bannon, G. A., Beilinson, V., et al. (2000). A soybean G2 glycinin allergen. International Archives of Allergy and Immunology, 123, 205–212. doi: 10.1159/000024445
   PubMed Web of Science ®Google Scholar
• Kim, S. K., Kim, T. H., Lee, S. K., Chang, K. H., Cho, S. J., Lee, K. W., et al. (2016). The use of fermented soybean meals during early phase affects subsequent growth and physiological response in broiler chicks. Asian–Australasian Journal of Animal Sciences, 29, 1287–1293. doi: 10.5713/ajas.15.0653
   PubMed Web of Science ®Google Scholar
• Krishnan, H. B., Kim, W.-S., Jang, S., & Kerley, M. S. (2009). All three subunits of soybean β-conglycinin are potential food allergens. Journal of Agricultural and Food Chemistry, 57, 938–943. doi: 10.1021/jf802451g
   PubMed Web of Science ®Google Scholar
• Kwanyen, P. W. R. F., & Burton, J. W. (1998). Soybean protein quality. The proceedings of the world conference on oilseed and edible oils processing. Champaign, IL: AOAC Press (pp. 284–289).
   Google Scholar
• Li, D. F., Blecha, F., Allee, G. L., Hancock, J. D., Nelssen, J. L., Reddy, P. G., et al. (1990). Transient hypersensitivity to soybean meal in the early-weaned pig. Journal of Animal Science, 68, 1790–1799. doi: 10.2527/1990.6861790x
   PubMed Web of Science ®Google Scholar
• Li, D. F., Blecha, F., Nelssen, J. L., Reddy, P. G., Klemm, R., & Goodband, R. D. (1991). Interrelationship between hypersensitivity to soybean proteins and growth performance in early-weaned pigs. Journal of Animal Science, 69, 4062–4069. doi: 10.2527/1991.69104062x
   PubMed Web of Science ®Google Scholar
• Li, D. F., Giesting, D. W., Blecha, F., Allee, G. L., Hancock, J. D., Nelssen, J. L., et al. (1991). Measuring suitability of soybean products for early-weaned pigs with immunological criteria. Journal of Animal Science, 69, 3299–3307. doi: 10.2527/1991.6983299x
   PubMed Web of Science ®Google Scholar
• Liu, C., Wang, H., Cui, Z., He, X., Wang, X., Zeng, X., et al. (2007). Optimization of extraction and isolation for 11S and 7S globulins of soybean seed storage protein. Food Chemistry, 102, 1310–1316. doi: 10.1016/j.foodchem.2006.07.017
   Web of Science ®Google Scholar
• Masteller, E. L., & Thompson, C. B. (1994). B cell development in the chicken. Poultry Science, 73, 998–1011. doi: 10.3382/ps.0730998
   PubMed Web of Science ®Google Scholar
• Nielsen, N. C. (1985). The structure and complexity of the 11S polypeptides in soybeans. Journal of the American Oil Chemists’ Society, 62, 1680–1686. doi: 10.1007/BF02541665
   Web of Science ®Google Scholar
• Nielsen, N. C., Dickinson, C. D., Cho, T. J., Thanh, V. H., Scallon, B. J., Fischer, R. L., et al. (1989). Characterization of the glycinin gene family in soybean. The Plant Cell, 1, 313–328. doi: 10.1105/tpc.1.3.313
   PubMed Web of Science ®Google Scholar
• Taliercio, E., & Kim, S. W. (2013). Epitopes from two soybean glycinin subunits are antigenic in pigs. Journal of the Science of Food and Agriculture, 93, 2927–2932. doi: 10.1002/jsfa.6113
   PubMed Web of Science ®Google Scholar
• Taliercio, E., & Kim, S. W. (2014). Identification of a second major antigenic epitope in the α-subunit of soy β-conglycinin. Food and Agricultural Immunology, 25, 311–321. doi: 10.1080/09540105.2013.791969
   Web of Science ®Google Scholar
• Taliercio, E., Loveless, T. M., & Turano, M. J. (2015). Identification of epitopes of the A1aBx and A5A4B3 subunits of glycinin antigenic in three animal species. Food and Agricultural Immunology, 26, 271–281. doi: 10.1080/09540105.2014.906566
   Web of Science ®Google Scholar
• Taliercio, E., Loveless, T. M., Turano, M. J., & Kim, S. W. (2014). Identification of epitopes of the β subunit of soybean β-conglycinin that are antigenic in pigs, dogs, rabbits and fish. Journal of the Science of Food and Agriculture, 94, 2289–2294. doi: 10.1002/jsfa.6556
   PubMed Web of Science ®Google Scholar
• Tizard, I. (2002). The avian antibody response. Seminars in Avian and Exotic Pet Medicine, 11, 2–14. doi: 10.1053/saep.2002.28216
   Google Scholar
• Utsumi, S., Kohno, M., Mori, T., & Kito, M. (1987). An alternate cDNA encoding glycinin A1aBx subunit. Journal of Agricultural and Food Chemistry, 35, 210–214. doi: 10.1021/jf00074a011
   Web of Science ®Google Scholar
• Vu Huu, T., & Shibasaki, K. (1978). Major proteins of soybean seeds. Subunit structure of beta-conglycinin. Journal of Agricultural and Food Chemistry, 26, 692–695. doi: 10.1021/jf60217a026
   Web of Science ®Google Scholar