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Seed Storage Protein, Functional Diversity and Association with Allergy

Jain, Abha·2023·Allergies

Abstract

Plants are essential for humans as they serve as a source of food, fuel, medicine, oils, and more. The major elements that are utilized for our needs exist in storage organs, such as seeds. These seeds are rich in proteins, show a broad spectrum of physiological roles, and are classified based on their sequence, structure, and conserved motifs. With the improvements to our knowledge of the basic sequence and our structural understanding, we have acquired better insights into seed proteins and their role. However, we still lack a systematic analysis towards understanding the functional diversity associated within each family and their associations with allergy. This review puts together the information about seed proteins, their classification, and diverse functional roles along with their associations with allergy.

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Figure 1 Structural features of seed storage proteins. Three-dimensional structures of different seed storage proteins made using PyMol (www.pymol.org, accessed on 1 December 2022). Figure 1. Structural features of seed storage proteins. Three-dimensional structures of different seed storage proteins made using PyMol (www.pymol.org, accessed on 1 December 2022).
Figure 1 Structural features of seed storage proteins. Three-dimensional structures of different seed storage proteins made using PyMol (www.pymol.org, accessed on 1 December 2022). Figure 1. Structural features of seed storage proteins. Three-dimensional structures of different seed storage proteins made using PyMol (www.pymol.org, accessed on 1 December 2022).CC-BY · From the PDF

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Research works printed but not linked: 144

  1. Kumar, 2019, Nutraceuticals derived from seed storage proteins: Implications for health wellness, Biocatal. Agric. Biotechnol., 17, 710, 10.1016/j.bcab.2019.01.044 · DOI
  2. Szyniarowski, 2004, Thiamine binding and metabolism in germinating seeds of selected cereals and legumes, Plant Physiol. Biochem., 42, 187, 10.1016/j.plaphy.2004.01.002 · DOI
  3. Agrawal, 2013, Comparative proteomics reveals a role for seed storage protein AmA1 in cellular growth, development, and nutrient accumulation, J. Proteome Res., 12, 4904, 10.1021/pr4007987 · DOI
  4. Delatorre, 2013, Interactions between indole-3-acetic acid (IAA) with a lectin from Canavalia maritima seeds reveal a new function for lectins in plant physiology, Biochimie, 95, 1697, 10.1016/j.biochi.2013.05.008 · DOI
  5. Businge, 2013, The effect of carbohydrates and osmoticum on storage reserve accumulation and germination of Norway spruce somatic embryos, Physiol. Plant., 149, 273, 10.1111/ppl.12039 · DOI
  6. Pinto, 2011, Plant storage proteins with antimicrobial activity: Novel insights into plant defense mechanisms, FASEB J., 25, 3290, 10.1096/fj.11-184291 · DOI
  7. Ribeiro, 2012, Antifungal and other biological activities of two 2S albumin-homologous proteins against pathogenic fungi, Protein J., 31, 59, 10.1007/s10930-011-9375-4 · DOI
  8. Nair, 2012, Jatropha curcas hemagglutinin is similar to a 2S albumin allergen from the same source and has unique sugar affinities, Planta, 236, 1499, 10.1007/s00425-012-1702-2 · DOI
  9. Borad, 2008, Pathogenesis-related proteins for the plant protection, Asian J. Exp. Sci., 22, 189
  10. Peumans, 2001, Ribosome-inactivating proteins from plants: More than RNA N-glycosidases?, FASEB J., 15, 1493, 10.1096/fj.00-0751rev · DOI
  11. Shikhi, 2019, Comparative study of 7S globulin from Corylus avellana and Solanum lycopersicum revealed importance of salicylic acid and Cu-binding loop in modulating their function, Biochem. Biophys. Res. Commun., 522, 127, 10.1016/j.bbrc.2019.11.072 · DOI
  12. Jain, 2015, Purification, identification and preliminary crystallographic studies of an allergenic protein from Solanum melongena, Acta Crystallogr. Sect. F Struct. Biol. Commun., 71, 221, 10.1107/S2053230X15000734 · DOI
  13. Rose, 2006, Defense proteins from Vigna unguiculata seed exudates: Characterization and inhibitory activity against Fusarium oxysporum, Plant Soil, 286, 181, 10.1007/s11104-006-9036-0 · DOI
  14. Viernes, 2012, Antihypertensive Peptides from Vicilin, the Major Storage Protein of Mung Bean (Vigna radiata (L.) R. Wilczek), J. Biol. Sci., 12, 393, 10.3923/jbs.2012.393.399 · DOI
  15. Jain, 2017, Crystal structure of nonspecific lipid transfer protein from Solanum melongena, Proteins Struct. Funct. Bioinform., 85, 1820, 10.1002/prot.25335 · DOI
  16. Jain, 2020, The structure of MP-4 from Mucuna pruriens at 2.22 Å resolution, Acta Crystallogr. Sect. F Struct. Biol. Commun., 76, 47, 10.1107/S2053230X20000199 · DOI
  17. Fang, 2010, Thermostable Kunitz trypsin inhibitor with cytokine inducing, antitumor and HIV-1 reverse transcriptase inhibitory activities from Korean large black soybeans, J. Biosci. Bioeng., 109, 211, 10.1016/j.jbiosc.2009.08.483 · DOI
  18. Ye, 2011, Antitumor and HIV-1 Reverse Transcriptase Inhibitory Activities of a Hemagglutinin and a Protease Inhibitor from Mini-Black Soybean, Evid.-Based Complement. Altern. Med., 2011, 851396, 10.1155/2011/851396 · DOI
  19. Edstam, 2011, Evolutionary history of the non-specific lipid transfer proteins, Mol. Plant, 4, 947, 10.1093/mp/ssr019 · DOI
  20. Breiteneder, 2004, A classification of plant food allergens, J. Allergy Clin. Immunol., 113, 821, 10.1016/j.jaci.2004.01.779 · DOI
  21. Shewry, 2002, Cereal seed storage proteins: Structures, properties and role in grain utilization, J. Exp. Bot., 53, 947, 10.1093/jexbot/53.370.947 · DOI
  22. Kreis, 1989, Unusual features of cereal seed protein structure and evolution, Bioessays, 10, 201, 10.1002/bies.950100606 · DOI
  23. Templeman, 1987, Biochemistry of fern spore germination: Globulin storage proteins in Matteuccia struthiopteris L., Plant Physiol., 85, 343, 10.1104/pp.85.2.343 · DOI
  24. Jain, 2016, Crystal structure of the vicilin from Solanum melongena reveals existence of different anionic ligands in structurally similar pockets, Sci. Rep., 6, 23600, 10.1038/srep23600 · DOI
  25. Bailey, 1970, The structure of legumin, a storage protein of broad bean (Vicia faba) seed, Eur. J. Biochem., 17, 460, 10.1111/j.1432-1033.1970.tb01187.x · DOI
  26. Konopska, 1983, Legumin and albumin of pea cotyledons during seed germination, Biol. Plant., 25, 15, 10.1007/BF02878261 · DOI
  27. Lawrence, 1994, Structure of Phaseolin at 2·2 Å Resolution: Implications for a Common Vicilin/Legumin Structure and the Genetic Engineering of Seed Storage Proteins, J. Mol. Biol., 238, 748, 10.1006/jmbi.1994.1333 · DOI
  28. Kumar, 2018, Docking, thermodynamics and molecular dynamics (MD) studies of a non-canonical protease inhibitor, MP-4, from Mucuna pruriens, Sci. Rep., 8, 689, 10.1038/s41598-017-18733-9 · DOI
  29. Radauer, C., Lackner, P., and Breiteneder, H. (2008). The Bet v 1 fold: An ancient, versatile scaffold for binding of large, hydrophobic ligands. BMC Evol. Biol., 8. · DOI
  30. Hauser, 2008, Molecular properties of plant food allergens: A current classification into protein families, Open Immunol. J., 1, 1, 10.2174/1874226200801010001 · DOI
  31. Lee, 1998, Rice non-specific lipid transfer protein: The 1.6 A crystal structure in the unliganded state reveals a small hydrophobic cavity, J. Mol. Biol., 276, 437, 10.1006/jmbi.1997.1550 · DOI
  32. Akkerdaas, 2000, β (1, 2)-xylose and α (1, 3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens, J. Biol. Chem., 275, 11451, 10.1074/jbc.275.15.11451 · DOI
  33. Douliez, 2000, Steady-state tyrosine fluorescence to study the lipid-binding properties of a wheat non-specific lipid-transfer protein (nsLTP1), Biochim. Biophys. Acta, 1467, 65, 10.1016/S0005-2736(00)00197-8 · DOI
  34. Hoh, 2005, Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding, Acta Crystallogr. D Biol. Crystallogr., 61, 397, 10.1107/S0907444905000417 · DOI
  35. Rueckert, 1990, Lipid transfer proteins, Chem. Phys. Lipids, 56, 1, 10.1016/0009-3084(90)90083-4 · DOI
  36. Thoma, 1993, A non-specific lipid transfer protein from Arabidopsis is a cell wall protein, Plant J., 3, 427, 10.1046/j.1365-313X.1993.t01-25-00999.x · DOI
  37. Molina, 1995, The defensive role of nonspecific lipid-transfer proteins in plants, Trends Microbiol., 3, 72, 10.1016/S0966-842X(00)88879-4 · DOI
  38. Marion, 2007, Plant lipid binding proteins: Properties and applications, Biotechnol. Adv., 25, 195, 10.1016/j.biotechadv.2006.11.003 · DOI
  39. Liu, 2015, Non-specific lipid transfer proteins in plants: Presenting new advances and an integrated functional analysis, J. Exp. Bot., 66, 5663, 10.1093/jxb/erv313 · DOI
  40. Jung, 2003, Three pathogen-inducible genes encoding lipid transfer protein from pepper are differentially activated by pathogens, abiotic, and environmental stresses, Plant Cell Environ., 26, 915, 10.1046/j.1365-3040.2003.01024.x · DOI
  41. Park, 2002, Induction of pepper cDNA encoding a lipid transfer protein during the resistance response to tobacco mosaic virus, Plant Mol. Biol., 48, 243, 10.1023/A:1013383329361 · DOI
  42. Nielsen, 1996, New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins, Plant Mol. Biol., 31, 539, 10.1007/BF00042227 · DOI
  43. Gonorazky, 2005, Stress induction and antimicrobial properties of a lipid transfer protein in germinating sunflower seeds, J. Plant Physiol., 162, 618, 10.1016/j.jplph.2004.10.006 · DOI
  44. Molina, 1997, Enhanced tolerance to bacterial pathogens caused by the transgenic expression of barley lipid transfer protein LTP2, Plant J., 12, 669, 10.1046/j.1365-313X.1997.00669.x · DOI
  45. Maldonado, 2002, A putative lipid transfer protein involved in systemic resistance signalling in Arabidopsis, Nature, 419, 399, 10.1038/nature00962 · DOI
  46. Lleonart, 1992, Food allergy: Identification of the major IgE-binding component of peach (Prunus persica), Ann. Allergy, 69, 128
  47. Alexeev, 2010, The structural characteristics of nonspecific lipid transfer proteins explain their resistance to gastroduodenal proteolysis, Biochemistry, 49, 2130, 10.1021/bi901939z · DOI
  48. Barber, 2002, cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family, Clin. Exp. Allergy, 32, 87, 10.1046/j.0022-0477.2001.01257.x · DOI
  49. Salcedo, 2004, Plant non-specific lipid transfer proteins as food and pollen allergens, Clin. Exp. Allergy, 34, 1336, 10.1111/j.1365-2222.2004.02018.x · DOI
  50. Asero, 1999, Detection and clinical characterization of patients with oral allergy syndrome caused by stable allergens in Rosaceae and nuts, Ann. Allergy Asthma Immunol., 83, 377, 10.1016/S1081-1206(10)62834-7 · DOI
  51. 2002, Lipid transfer protein as a potential panallergen?, Allergy, 57, 873, 10.1034/j.1398-9995.2002.23541.x · DOI
  52. Pastorello, 2004, Clinical role of lipid transfer proteins in food allergy, Mol. Nutr. Food Res., 48, 356, 10.1002/mnfr.200400047 · DOI
  53. Bruix, 2003, Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis, Biochemistry, 42, 13839, 10.1021/bi0352217 · DOI
  54. Palomares, 2004, Solution structure and stability against digestion of rproBnIb, a recombinant 2S albumin from rapeseed: Relationship to its allergenic properties, Biochemistry, 43, 16036, 10.1021/bi048069x · DOI
  55. Shewry, 2004, Solution structure of a methionine-rich 2S albumin from sunflower seeds: Relationship to its allergenic and emulsifying properties, Biochemistry, 43, 6976, 10.1021/bi0496900 · DOI
  56. Hennig, 1995, Crystal structure of narbonin at 1.8 Å resolution, Acta Crystallogr. Sect. D Biol. Crystallogr., 51, 177, 10.1107/S0907444994009807 · DOI
  57. Gaur, 2010, Crystal structure and functional insights of hemopexin fold protein from grass pea, Plant Physiol., 152, 1842, 10.1104/pp.109.150680 · DOI
  58. Gaur, 2011, The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 67, 193, 10.1107/S1744309110051250 · DOI
  59. Ullah, 2015, Crystal structure of mature 2S albumin from Moringa oleifera seeds, Biochem. Biophys. Res. Commun., 468, 365, 10.1016/j.bbrc.2015.10.087 · DOI
  60. Shewry, 1995, Seed storage proteins: Structures and biosynthesis, Plant Cell, 7, 945
  61. Gane, 1998, Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase, J. Mol. Evol., 46, 488, 10.1007/PL00006329 · DOI
  62. Maleki, 2000, Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation, J. Immunol., 164, 5844, 10.4049/jimmunol.164.11.5844 · DOI
  63. Wang, 2012, Proteomic analysis of embryonic axis of Pisum sativum seeds during germination and identification of proteins associated with loss of desiccation tolerance, J. Proteom., 77, 68, 10.1016/j.jprot.2012.07.005 · DOI
  64. Rose, 2003, Effect of sugars on the association between cowpea vicilin (7S storage proteins) and fungal cells, Biocell, 27, 173, 10.32604/biocell.2003.27.173 · DOI
  65. Dooper, 2009, Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals, J. Investig. Allergol. Clin. Immunol., 19, 283
  66. Ko, 2000, The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 Å resolution, Acta Crystallogr. Sect. D Biol. Crystallogr., 56, 411, 10.1107/S0907444900002237 · DOI
  67. Lawrence, 1990, The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution, EMBO J., 9, 9, 10.1002/j.1460-2075.1990.tb08074.x · DOI
  68. Maruyama, 2003, Creation of soybean β-conglycinin β with strong phagocytosis-stimulating activity, Biochim. et Biophys. Acta (BBA)-Proteins Proteom., 1648, 99, 10.1016/S1570-9639(03)00113-4 · DOI
  69. Adachi, 2003, Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer, Proc. Natl. Acad. Sci. USA, 100, 7395, 10.1073/pnas.0832158100 · DOI
  70. Adachi, 2001, Crystal structure of soybean proglycinin A1aB1b homotrimer, J. Mol. Biol., 305, 291, 10.1006/jmbi.2000.4310 · DOI
  71. Koiwa, 1999, Crystal structure of tobacco PR-5d protein at 1.8 Å resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins, J. Mol. Biol., 286, 1137, 10.1006/jmbi.1998.2540 · DOI
  72. Batalia, 1996, The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family, Nat. Genet., 3, 19
  73. Ko, 1994, Structures of three crystal forms of the sweet protein thaumatin, Acta Crystallogr. Sect. D Biol. Crystallogr., 50, 813, 10.1107/S0907444994005512 · DOI
  74. Shih, 2001, Purification of an osmotin-like protein from the seeds of Benincasa hispida and cloning of the gene encoding this protein, Plant Sci., 160, 817, 10.1016/S0168-9452(00)00450-7 · DOI
  75. Degano, 2003, Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier, J. Mol. Biol., 325, 123, 10.1016/S0022-2836(02)01197-X · DOI
  76. Biesiadka, 2002, Crystal structures of two homologous pathogenesis-related proteins from yellow lupine, J. Mol. Biol., 319, 1223, 10.1016/S0022-2836(02)00385-6 · DOI
  77. Dolot, 2016, Crystallographic and CD probing of ligand-induced conformational changes in a plant PR-10 protein, J. Struct. Biol., 193, 55, 10.1016/j.jsb.2015.11.008 · DOI
  78. Ruszkowski, 2014, Specific binding of gibberellic acid by Cytokinin-Specific Binding Proteins: A new aspect of plant hormone-binding proteins with the PR-10 fold, Acta Crystallogr. Sect. D Biol. Crystallogr., 70, 2032, 10.1107/S1399004714010578 · DOI
  79. Sliwiak, 2014, Likelihood-based molecular-replacement solution for a highly pathological crystal with tetartohedral twinning and sevenfold translational noncrystallographic symmetry, Acta Crystallogr. Sect. D Biol. Crystallogr., 70, 471, 10.1107/S1399004713030319 · DOI
  80. Ruszkowski, 2013, The landscape of cytokinin binding by a plant nodulin, Acta Crystallogr. Sect. D Biol. Crystallogr., 69, 2365, 10.1107/S0907444913021975 · DOI
  81. Huet, 2013, High-resolution structure of a papaya plant-defence barwin-like protein solved by in-house sulfur-SAD phasing, Acta Crystallogr. Sect. D Biol. Crystallogr., 69, 2017, 10.1107/S0907444913018015 · DOI
  82. Bewley, J.D., and Black, M. (1994). Cellular events during germination and seedling growth. Seeds, Springer. · DOI
  83. Oriowo, 1991, Variation in the interaction of some phenylethylamine and imidazoline derivatives with alpha-1 adrenoceptors in rabbit arteries: Further evidence for the variable receptor affinity hypothesis, J. Pharmacol. Exp. Ther., 257, 651
  84. Boulter, D. (1984). Biochemistry of storage protein synthesis and deposition in the developing legume seed. Advances in Botanical Research, Academic Press.
  85. Below, 2000, Carbon/nitrogen interactions during ear and kernel development of maize, Physiol. Model. Kernel Set Maize, 29, 15
  86. Leung, 1998, Abscisic Acid Signal Transduction, Annu. Rev. Plant Physiol. Plant Mol. Biol., 49, 199, 10.1146/annurev.arplant.49.1.199 · DOI
  87. Schroeder, 2001, Guard Cell Signal Transduction, Annu. Rev. Plant Physiol. Plant Mol. Biol., 52, 627, 10.1146/annurev.arplant.52.1.627 · DOI
  88. Hunter, 1998, The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease, Philos. Trans. R. Soc. B Biol. Sci., 353, 583, 10.1098/rstb.1998.0228 · DOI
  89. Ashton, 1976, Mobilization of storage proteins of seeds, Annu. Rev. Plant Physiol., 27, 95, 10.1146/annurev.pp.27.060176.000523 · DOI
  90. Sangwan, 1992, Phosphoenolpyruvate carboxylase activity and concentration in the endosperm of developing and germinating castor oil seeds, Plant Physiol., 99, 445, 10.1104/pp.99.2.445 · DOI
  91. Shimizu, 1990, Accumulation of thiamine and thiamine-binding protein during development of rice seed, J. Plant Physiol., 137, 123, 10.1016/S0176-1617(11)80022-2 · DOI
  92. Molin, 1980, Thiamin phosphorylation by thiamin pyrophosphotransferase during seed germination, Plant Physiol., 66, 313, 10.1104/pp.66.2.313 · DOI
  93. Howle, 1991, GTP-specific pyrophosphorylation of thiamin in dark-grown soybean (Glycine max) seedling axes, Physiol. Plant., 81, 24, 10.1111/j.1399-3054.1991.tb01707.x · DOI
  94. Mitsunaga, 1987, A possible role for thiamine-binding protein in the germination of rice seed, J. Plant Physiol., 130, 279, 10.1016/S0176-1617(87)80232-8 · DOI
  95. Sexton, 2006, Parallels in fungal pathogenesis on plant and animal hosts, Eukaryot. Cell, 5, 1941, 10.1128/EC.00277-06 · DOI
  96. Peumans, 1995, Lectins as plant defense proteins, Plant Physiol., 109, 347, 10.1104/pp.109.2.347 · DOI
  97. Brinda, 2004, Determinants of quaternary association in legume lectins, Protein Sci., 13, 1735, 10.1110/ps.04651004 · DOI
  98. Loris, 1998, Legume lectin structure, Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzymol., 1383, 9, 10.1016/S0167-4838(97)00182-9 · DOI
  99. Farahnak, 2010, Carbohydrate Detection and Lectin Isolation from Tegumental Tissue of Fasciola hepatica, Iran. J. Parasitol., 5, 20
  100. Komath, 2006, Beyond carbohydrate binding: New directions in plant lectin research, Org. Biomol. Chem., 4, 973, 10.1039/b515446d · DOI
  101. Elezgaray, 2008, Pore formation induced by an antimicrobial peptide: Electrostatic effects, Biophys. J., 95, 5748, 10.1529/biophysj.108.136655 · DOI
  102. Araujo, 2005, Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: Isolation of the cDNAs, heterologous expression and structural studies, Biol. Chem., 386, 561, 10.1515/BC.2005.066 · DOI
  103. Yount, 2013, Peptide antimicrobials: Cell wall as a bacterial target, Ann. N. Y. Acad. Sci., 1277, 127, 10.1111/nyas.12005 · DOI
  104. Nawrot, 2014, Global proteomic analysis of Chelidonium majus and Corydalis cava (Papaveraceae) extracts revealed similar defense-related protein compositions, Fitoterapia, 94, 77, 10.1016/j.fitote.2014.01.015 · DOI
  105. Yang, 2007, Expression of a novel small antimicrobial protein from the seeds of motherwort (Leonurus japonicus) confers disease resistance in tobacco, Appl. Environ. Microbiol., 73, 939, 10.1128/AEM.02016-06 · DOI
  106. Stirpe, 2004, Ribosome-inactivating proteins, Toxicon, 44, 371, 10.1016/j.toxicon.2004.05.004 · DOI
  107. Endo, 1987, The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins, J. Biol. Chem., 262, 5908, 10.1016/S0021-9258(18)45660-8 · DOI
  108. Endo, 1987, RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes, J. Biol. Chem., 262, 8128, 10.1016/S0021-9258(18)47538-2 · DOI
  109. Li, 1991, Trichosanthin, a potent HIV-1 inhibitor, can cleave supercoiled DNA in vitro, Nucleic Acids Res., 19, 6309, 10.1093/nar/19.22.6309 · DOI
  110. Barbieri, 1997, Polynucleotide: Adenosine glycosidase activity of ribosome-inactivating proteins: Effect on DNA, RNA and poly (A), Nucleic Acids Res., 25, 518, 10.1093/nar/25.3.518 · DOI
  111. Hudak, 2000, A novel mechanism for inhibition of translation by pokeweed antiviral protein: Depurination of the capped RNA template, Rna, 6, 369, 10.1017/S1355838200991337 · DOI
  112. Barbieri, 1994, Unexpected activity of saporins, Nature, 372, 624, 10.1038/372624a0 · DOI
  113. Buitink, 2008, Intracellular glasses and seed survival in the dry state, C. R. Biol., 331, 788, 10.1016/j.crvi.2008.08.002 · DOI
  114. Singh, 1987, Characterization of osmotin A thaumatin-like protein associated with osmotic adaptation in plant cells, Plant Physiol., 85, 529, 10.1104/pp.85.2.529 · DOI
  115. Goyal, 2005, LEA proteins prevent protein aggregation due to water stress, Biochem. J., 388, 151, 10.1042/BJ20041931 · DOI
  116. Grelet, 2005, Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying, Plant Physiol., 137, 157, 10.1104/pp.104.052480 · DOI
  117. Houston, 2009, Quantitative proteomics of seed filling in castor: Comparison with soybean and rapeseed reveals differences between photosynthetic and nonphotosynthetic seed metabolism, Plant Physiol., 151, 857, 10.1104/pp.109.141622 · DOI
  118. Marsoni, 2008, Proteomic analysis of somatic embryogenesis in Vitis vinifera, Plant Cell Rep., 27, 347, 10.1007/s00299-007-0438-0 · DOI
  119. Cooper, 2003, A network of rice genes associated with stress response and seed development, Proc. Natl. Acad. Sci. USA, 100, 4945, 10.1073/pnas.0737574100 · DOI
  120. Subbaiah, 2000, A Ca2+-dependent cysteine protease is associated with anoxia-induced root tip death in maize, J. Exp. Bot., 51, 721
  121. Job, 2005, Patterns of protein oxidation in Arabidopsis seeds and during germination, Plant Physiol., 138, 790, 10.1104/pp.105.062778 · DOI
  122. Xiong, 2007, Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis, Plant Physiol., 143, 291, 10.1104/pp.106.092106 · DOI
  123. Graf, 1990, Antioxidant functions of phytic acid, Free Radic. Biol. Med., 8, 61, 10.1016/0891-5849(90)90146-A · DOI
  124. Akond, 2011, Anthocyanin, total polyphenols and antioxidant activity of common bean, Am. J. Food Technol., 6, 385, 10.3923/ajft.2011.385.394 · DOI
  125. Empson, 1991, Phytic acid as a food antioxidant, J. Food Sci., 56, 560, 10.1111/j.1365-2621.1991.tb05324.x · DOI
  126. Graf, 1987, Phytic acid. A natural antioxidant, J. Biol. Chem., 262, 11647, 10.1016/S0021-9258(18)60858-0 · DOI
  127. Herzig, 2016, Lupin as a perspective protein plant for animal and human nutrition—A review, Acta Vet. Brno, 85, 165, 10.2754/avb201685020165 · DOI
  128. Teugwa, C.M., Boudjeko, T., Tchinda, B.T., Mejiato, P.C., and Zofou, D. (2013). Anti-hyperglycaemic globulins from selected Cucurbitaceae seeds used as antidiabetic medicinal plants in Africa. BMC Complement. Altern. Med., 13. · DOI
  129. Ben, 2006, Soybean bioactive peptides: A new horizon in preventing chronic diseases, Sex. Reprod. Menopause, 4, 91, 10.1016/j.sram.2006.08.012 · DOI
  130. Johansson, 2001, A revised nomenclature for allergy: An EAACI position statement from the EAACI nomenclature task force, Allergy, 56, 813, 10.1034/j.1398-9995.2001.t01-1-00001.x · DOI
  131. Sampson, 1999, Food allergy. Part 1: Immunopathogenesis and clinical disorders, J. Allergy Clin. Immunol., 103, 717, 10.1016/S0091-6749(99)70411-2 · DOI
  132. Taylor, 2006, Food allergen labeling in the USA and Europe, Curr. Opin. Allergy Clin. Immunol., 6, 186, 10.1097/01.all.0000225158.75521.ad · DOI
  133. Sokol, 2020, Prevalence and diagnosis of sesame allergy in children with IgE-mediated food allergy, Pediatr. Allergy Immunol., 31, 214, 10.1111/pai.13143 · DOI
  134. Sampson, 2004, Update on food allergy, J. Allergy Clin. Immunol., 113, 805, 10.1016/j.jaci.2004.03.014 · DOI
  135. Aalberse, 2000, Structural biology of allergens, J. Allergy Clin. Immunol., 106, 228, 10.1067/mai.2000.108434 · DOI
  136. Elfman, 1998, Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion, J. Allergy Clin. Immunol., 101, 67, 10.1016/S0091-6749(98)70195-2 · DOI
  137. Tassin, 1998, Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant nonspecific lipid transfer proteins, Biochemistry, 37, 3623, 10.1021/bi9723515 · DOI
  138. Selitrennikoff, 2001, Antifungal proteins, Appl. Environ. Microbiol., 67, 2883, 10.1128/AEM.67.7.2883-2894.2001 · DOI
  139. Costa, 2022, Are physicochemical properties shaping the allergenic potency of plant allergens?, Clin. Rev. Allergy Immunol., 62, 37, 10.1007/s12016-020-08810-9 · DOI
  140. Dominguez, 1990, Purification and characterization of an allergen of mustard seed, Ann. Allergy, 64, 352
  141. Murtagh, 2003, In vitro stability and immunoreactivity of the native and recombinant plant food 2S albumins Ber e 1 and SFA-8, Clin. Exp. Allergy, 33, 1147, 10.1046/j.1365-2222.2003.01736.x · DOI
  142. Bublin, 2003, Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients, FASEB J., 17, 1697, 10.1096/fj.02-0872fje · DOI
  143. Pedrosa, 2000, Selective neoglycosylation increases the structural stability of vicilin, the 7S storage globulin from pea seeds, Arch. Biochem. Biophys., 382, 203, 10.1006/abbi.2000.2024 · DOI
  144. Koppelman, 1999, Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties, J. Biol. Chem., 274, 4770, 10.1074/jbc.274.8.4770 · DOI

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Metadata

Authors
Jain, A.
Affiliations
Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
Venue
Allergies
Publisher
MDPI AG
Published
2023-01-18
Volume
3
Issue
1
Pages
25-38
ISSN
2313-5786
Cited by
21
References
1
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

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