Leucoagglutinating phytohemagglutinin: purification, characterization, proteolytic digestion and assessment for allergenicity potential in BALB/c mice

References

• Remington BC, Baumert JL, Marx DB, Taylor SL. Quantitative risk assessment of foods containing peanut advisory labeling. Food Chem Toxicol 2013;62C:179–187
   Google Scholar
• Mills EN, Breiteneder H. Food allergy and its relevance to industrial food proteins. Biotechnol Adv 2005;23:409–414
   Google Scholar
• Verma P, Chhabra N, Sharma R. Severe marking-nut dermatitis. Dermatitis 2012;23:293–294
   PubMed Web of Science ®Google Scholar
• Verma AK, Kumar S, Das M, Dwivedi PD. A comprehensive review of legume allergy. Clin Rev Allergy Immunol 2013;45:30–46
   PubMed Web of Science ®Google Scholar
• Kasera R, Singh AB, Kumar R, et al. Effect of thermal processing and γ-irradiation on allergenicity of legume proteins. Food Chem Toxicol 2012;50:3456–3461
   PubMed Web of Science ®Google Scholar
• Foster ES, Kimber I, Dearman RJ. Relationship between protein digestibility and allergenicity: comparisons pepsin and cathepsin. Toxicology 2013;309:30–38
   PubMed Web of Science ®Google Scholar
• Kumar S, Verma AK, Das M, Dwivedi PD. Molecular mechanisms of IgE mediated food allergy. Int Immunopharmacol 2012;13:432–439
   PubMed Web of Science ®Google Scholar
• Kumar S, Verma AK, Das M, et al. Clinical complications of kidney bean (Phaseolus vulgaris L.) consumption. Nutrition 2013;29:821–827
   PubMed Web of Science ®Google Scholar
• Kasera R, Singh BP, Lavasa S, et al. Kidney bean: a major sensitizer among legumes in asthma and rhinitis patients from India. PLoS One 2011;6:e27193
   PubMed Web of Science ®Google Scholar
• Kumar S, Sharma A, Verma AK, et al. Allergenicity potential of red kidney bean (Phaseolus vulgaris L.) proteins in orally treated BALB/c mice and passively sensitized RBL-2H3 cells. Cell Immunol 2013;284:37–44
   PubMed Web of Science ®Google Scholar
• Kumar S, Verma AK, Misra A, et al. Allergenic responses of red kidney bean (Phaseolus vulgaris cv chitra) polypeptides in BALB/c mice recognized by bronchial asthma and allergic rhinitis patients. Food Res Intl 2011;44:2868–2879
   Web of Science ®Google Scholar
• Kumar S, Verma AK, Sharma A, et al. Phytohemagglutinins augment red kidney bean (Phaseolus vulgaris L.) induced allergic manifestations. J Proteomics 2013;93:50–64
   PubMed Web of Science ®Google Scholar
• Astwood JD, Leach JN, Fuchs RL. Stability of food allergens to digestion in vitro. Nat Biotechnol 1996;14:1269–1273
   PubMed Web of Science ®Google Scholar
• Misra A, Kumar R, Mishra V, et al. Potential allergens of green gram (Vigna radiata L. Millsp) identified as members of cupin superfamily and seed albumin. Clin Exp Allergy 2011;41:1157–1168
   PubMed Web of Science ®Google Scholar
• Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. PNAS 1979;76:4350–4354
   PubMed Web of Science ®Google Scholar
• Report of Department of Biotechnology (DBT), India. Protocols for food and feed safety assessment of GE crops, 2008, Page 18
   Google Scholar
• Thomas K, Aalbers M, Bannon GA, et al. A multi-laboratory evaluation of a common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins. Regul Toxicol Pharmacol 2004;39:87–98
   PubMed Web of Science ®Google Scholar
• Sun J, Arias K, Alvarez D, et al. Impact of CD40 ligand, B cells, and mast cells in peanut induced anaphylactic responses. J Immunol 2007;179:6696–6703
   PubMed Web of Science ®Google Scholar
• Misra A, Kumar R, Mishra V, et al. Partial characterization of red gram (Cajanus cajan L. Millsp) polypeptides recognized by patients exhibiting rhinitis and bronchial asthma. Food Chem Toxicol 2010;48:2725–2736
   PubMed Web of Science ®Google Scholar
• Voller A, Bidwel DE, Barlett A. Enzyme-linked immunosorbent assay. Manual of clinical immunology. Washington: American Society of Microbiology; 1980
   Google Scholar
• Dalal I, Binson I, Reifen R, et al. Food allergy is a matter of geography after all: sesame as a major cause of severe IgE mediated food allergic reactions among infants and young children in Israel. Allergy 2002;57:362–365
   PubMed Web of Science ®Google Scholar
• Misra A, Prasad R, Das M, Dwivedi PD. Prevalence of legume sensitization in patients of naso-bronchial allergy. Immunopharmacol Immunotoxicol 2008;30:529–542
   PubMed Web of Science ®Google Scholar
• Misra A, Prasad R, Das M, Dwivedi PD. Probing novel allergenic proteins of commonly consumed legumes. Immunopharmacol Immunotoxicol 2009;31:186–194
   PubMed Web of Science ®Google Scholar
• Breiteneder H, Clare Mills EN. Plant food allergens—structural and functional aspects of allergenicity. Biotechnol Adv 2005;23:395–399
   PubMed Web of Science ®Google Scholar
• Kumari D, Arora N, Kasera R, et al. Isolation and characterization of a 28 kDa major allergen from blackgram (Phaseolus mungo). Immunobiology 2012;217:895–904
   PubMed Web of Science ®Google Scholar
• Burks AW, Williams LW, Connaughton C, et al. Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge. J Allergy Clin Immunol 1992;90:962–969
   PubMed Web of Science ®Google Scholar
• Koppelman SJ, Wensing M, Ertmann M, et al. Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing, Ara h2 is the most important peanut allergen. Clin Exp Allergy 2004;34:583–590
   PubMed Web of Science ®Google Scholar
• Sánchez-Monge R, Pascual CY, Díaz-Perales A, et al. Isolation and characterization of relevant allergens from boiled lentils. J Allergy Clin Immunol 2000;106:955–961
   PubMed Web of Science ®Google Scholar
• Verma AK, Kumar S, Das M, Dwivedi PD. Impact of thermal processing on legume allergens. Plant Food Human Nutr 2012;67:430–441
   PubMed Web of Science ®Google Scholar
• Fu TJ, Abbott UR, Hatzos C. Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid – a comparative study. J Agric Food Chem 2002;50:7154–7160
   PubMed Web of Science ®Google Scholar
• Herman RA, Korjagin VA, Schafer BW. Quantitative measurement of protein digestion in simulated gastric fluid. Regul Toxicol Pharmacol 2005;41:175–184
   PubMed Web of Science ®Google Scholar
• Bashir ME, Andersen P, Fuss IJ, et al. An enterichelminth infection protects against an allergic response to dietary antigen. J Immunol 2002;169:3284–3292
   PubMed Web of Science ®Google Scholar
• Bashir ME, Louie S, Shi HN, Nagler-Anderson C. Toll-like receptor 4 signaling by intestinal microbes influences susceptibility to food allergy. J Immunol 2004;172:6978–6987
   PubMed Web of Science ®Google Scholar
• Helm RM. Food allergy animal models: an overview. Ann NY Acad Sci 2002;964:139–150
   PubMed Web of Science ®Google Scholar