The lipid interaction capacity of Sin a 2 and Ara h 1, major mustard and peanut allergens of the cupin superfamily, endorses allergenicity

Allergy: European Journal of Allergy and Clinical Immunology

Volumn 71, Issue 9, 2016, Pages 1284-1294

  Angelina, A ^a   Sirvent, S ^a   Palladino, C ^b   Vereda, A ^c   Cuesta Herranz, J ^c   Eiwegger, T ^d,e   Rodriguez R ^a   Breiteneder, H ^b   Villalba, M ^a   Palomares, O ^a  

^a UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

^b MEDICAL UNIVERSITY OF VIENNA   (Austria)

^c Hospital UniversitarioFundación Jiménez Díaz   (Spain)

^d UNIV KLIN KINDER JUGENDHEILKUNDE   (Austria)

^e HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

11S and 7S globulins; allergens; dendritic cells; food allergy; lipid binding capacity

Indexed keywords

11S GLOBULIN; FOOD ALLERGEN; GLOBULIN; IMMUNOGLOBULIN 7S; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 10; INTERLEUKIN 1BETA; INTERLEUKIN 4; LIPID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; RECOMBINANT ALLERGEN; TOLL LIKE RECEPTOR 2; TRANSCRIPTION FACTOR AP 1; UNCLASSIFIED DRUG; ALLERGEN; ARA H 1 PROTEIN, ARACHIS HYPOGAEA; CYTOKINE; GLYCOPROTEIN; IMMUNOGLOBULIN E; PLANT ANTIGEN; PLANT PROTEIN; SIN A 2 PROTEIN, SINAPIS ALBA;

ALLERGENICITY; ARTICLE; BINDING ASSAY; CELL VIABILITY; CONTROLLED STUDY; CYTOKINE PRODUCTION; DENDRITIC CELL; DIGESTION; DISULFIDE BOND; FOOD ALLERGY; HUMAN; HUMAN CELL; MICROSOME; PEANUT; PEANUT ALLERGY; PHOSPHOLIPID VESICLE; PLANT SEED; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN LIPID INTERACTION; SINAPIS ALBA; TRANSCRIPTION INITIATION; CHEMISTRY; CYTOPLASM VESICLE; ENDOSOME; IMMUNOLOGY; LYSOSOME; METABOLISM; MOLECULAR MODEL; PROTEIN CONFORMATION;

ALLERGENS; ANTIGENS, PLANT; CYTOKINES; CYTOPLASMIC VESICLES; DENDRITIC CELLS; ENDOSOMES; FOOD HYPERSENSITIVITY; GLYCOPROTEINS; HUMANS; IMMUNOGLOBULIN E; LIPIDS; LYSOSOMES; MODELS, MOLECULAR; NF-KAPPA B; PEANUT HYPERSENSITIVITY; PHOSPHATIDYLGLYCEROLS; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEOLYSIS; TOLL-LIKE RECEPTOR 2;

EID: 84962736401     PISSN: 01054538     EISSN: 13989995     Source Type: Journal    
DOI: 10.1111/all.12887     Document Type: Article

References (45)

1. Sicherer SH, Leung DY. Advances in allergic skin disease, anaphylaxis, and hypersensitivity reactions to foods, drugs, and insects in 2014. J Allergy Clin Immunol 2015;135:357–367.
2. Nwaru BI, Hickstein L, Panesar SS, Roberts G, Muraro A, Sheikh A. Prevalence of common food allergies in Europe: a systematic review and meta-analysis. Allergy 2014;69:992–1007.
3. Carrard A, Rizzuti D, Sokollik C. Update on food allergy. Allergy 2015;70:1511–1520.
4. Vereda A, Sirvent S, Villalba M, Rodriguez R, Cuesta-Herranz J, Palomares O. Improvement of mustard (Sinapis alba) allergy diagnosis and management by linking clinical features and component-resolved approaches. J Allergy Clin Immunol 2011;127:1304–1307.
5. Menendez-Arias L, Moneo I, Dominguez J, Rodriguez R. Primary structure of the major allergen of yellow mustard (Sinapis alba L.) seed, Sin a I. Eur J Biochem 1988;177:159–166.
6. Palomares O, Cuesta-Herranz J, Vereda A, Sirvent S, Villalba M, Rodriguez R. Isolation and identification of an 11S globulin as a new major allergen in mustard seeds. Ann Allergy Asthma Immunol 2005;94:586–592.
7. Sirvent S, Akotenou M, Cuesta-Herranz J, Vereda A, Rodriguez R, Villalba M et al. The 11S globulin Sin a 2 from yellow mustard seeds shows IgE cross-reactivity with homologous counterparts from tree nuts and peanut. Clin Transl Allergy 2012;2:23.
8. Sirvent S, Palomares O, Vereda A, Villalba M, Cuesta-Herranz J, Rodriguez R. nsLTP and profilin are allergens in mustard seeds: cloning, sequencing and recombinant production of Sin a 3 and Sin a 4. Clin Exp Allergy 2009;39:1929–1936.
9. Palomares O, Vereda A, Cuesta-Herranz J, Villalba M, Rodriguez R. Cloning, sequencing, and recombinant production of Sin a 2, an allergenic 11S globulin from yellow mustard seeds. J Allergy Clin Immunol 2007;119:1189–1196.
10. Barre A, Borges JP, Rouge P. Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: a structural basis for their IgE-binding cross-reactivity. Biochimie 2005;87:499–506.
11. Burks AW, Cockrell G, Stanley JS, Helm RM, Bannon GA. Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity. J Clin Invest 1995;96:1715–1721.
12. Maleki SJ, Kopper RA, Shin DS, Park CW, Compadre CM, Sampson H et al. Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. J Immunol 2000;164:5844–5849.
13. Shin D, Compadre CM, Maleki SJ, Kopper RA, Sampson H, Huang SK et al. Bichemical and structural analysis of the IgE binding sites on Ara h 1, an abundant and highly allergenic peanut protein. J Biol Chem 1998;273:13753–13759.
14. Chruszcz M, Maleki SJ, Majorek KA, Demas M, Bublin M, Solberg R et al. Structural and immunologic characterization of Ara h 1, a major peanut allergen. J Biol Chem 2011;286:39318–39327.
15. Cabanos C, Urabe H, Tandang-Silvas MR, Utsumi S, Mikami B, Maruyama N. Crystal structure of the major peanut allergen Ara h 1. Mol Immunol 2011;49:115–123.
16. Palomares O, Crameri R, Rhyner C. The contribution of biotechnology toward progress in diagnosis, management, and treatment of allergic diseases. Allergy 2014;69:1588–1601.
17. Breiteneder H, Mills EN. Molecular properties of food allergens. J Allergy Clin Immunol 2005;115:14–23.
18. Sirvent S, Palomares O, Cuesta-Herranz J, Villalba M, Rodriguez R. Analysis of the structural and immunological stability of 2S albumin, nonspecific lipid transfer protein, and profilin allergens from mustard seeds. J Agric Food Chem 2012;60:6011–6018.
19. Oeder S, Alessandrini F, Wirz OF, Braun A, Wimmer M, Frank U et al. Pollen-derived nonallergenic substances enhance Th2-induced IgE production in B cells. Allergy 2015;70:1450–1460.
20. Bublin M, Eiwegger T, Breiteneder H. Do lipids influence the allergic sensitization process? J Allergy Clin Immunol 2014;134:521–529.
21. Hammad H, Plantinga M, Deswarte K, Pouliot P, Willart MA, Kool M et al. Inflammatory dendritic cells–not basophils–are necessary and sufficient for induction of Th2 immunity to inhaled house dust mite allergen. J Exp Med 2010;207:2097–2111.
22. Berin MC, Mayer L. Can we produce true tolerance in patients with food allergy? J Allergy Clin Immunol 2013;131:14–22.
23. Palomares O, Martin-Fontecha M, Lauener R, Traidl-Hoffmann C, Cavkaytar O, Akdis M et al. Regulatory T cells and immune regulation of allergic diseases: roles of IL-10 and TGF-beta. Genes Immun 2014;15:511–520.
24. Sirvent S, Canto B, Gomez F, Blanca N, Cuesta-Herranz J, Canto G et al. Detailed characterization of Act d 12 and Act d 13 from kiwi seeds: implication in IgE cross-reactivity with peanut and tree nuts. Allergy 2014;69:1481–1488.
25. Egger M, Jurets A, Wallner M, Briza P, Ruzek S, Hainzl S et al. Assessing protein immunogenicity with a dendritic cell line-derived endolysosomal degradome. PLoS One 2011;6:e17278.
26. Dearman RJ, Alcocer MJ, Kimber I. Influence of plant lipids on immune responses in mice to the major Brazil nut allergen Ber e 1. Clin Exp Allergy 2007;37:582–591.
27. van Wijk F, Nierkens S, Hassing I, Feijen M, Koppelman SJ, de Jong GA et al. The effect of the food matrix on in vivo immune responses to purified peanut allergens. Toxicol Sci 2005;86:333–341.
28. Petersen A, Rennert S, Kull S, Becker WM, Notbohm H, Goldmann T et al. Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8. Biol Chem 2014;395:239–250.
29. Pasquato N, Berni R, Folli C, Folloni S, Cianci M, Pantano S et al. Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens. J Mol Biol 2006;356:684–694.
30. Onaderra M, Monsalve RI, Mancheno JM, Villalba M, Martinez del Pozo A, Gavilanes JG et al. Food mustard allergen interaction with phospholipid vesicles. Eur J Biochem 1994;225:609–615.
31. Mirotti L, Florsheim E, Rundqvist L, Larsson G, Spinozzi F, Leite-de-Moraes M et al. Lipids are required for the development of Brazil nut allergy: the role of mouse and human iNKT cells. Allergy 2013;68:74–83.
32. Bossios A, Theodoropoulou M, Mondoulet L, Rigby NM, Papadopoulos NG, Bernard H et al. Effect of simulated gastro-duodenal digestion on the allergenic reactivity of beta-lactoglobulin. Clin Transl Allergy 2011;1:6.
33. Akkerdaas JH, Schocker F, Vieths S, Versteeg S, Zuidmeer L, Hefle SL et al. Cloning of oleosin, a putative new hazelnut allergen, using a hazelnut cDNA library. Mol Nutr Food Res 2006;50:18–23.
34. Bøgh KL, Madsen CB. Food allergens: is there a correlation between stability to digestion and allergenicity? Crit Rev Food Sci Nutr 2015;56:1545–1567.
35. Sirvent S, Canto B, Cuesta-Herranz J, Gomez F, Blanca N, Canto G et al. Act d 12 and Act d 13: two novel, masked, relevant allergens in kiwifruit seeds. J Allergy Clin Immunol 2014;133:1765–1767.
36. Maleki SJ, Chung SY, Champagne ET, Raufman JP. The effects of roasting on the allergenic properties of peanut proteins. J Allergy Clin Immunol 2000;106:763–768.
37. Eiwegger T, Rigby N, Mondoulet L, Bernard H, Krauth MT, Boehm A et al. Gastro-duodenal digestion products of the major peanut allergen Ara h 1 retain an allergenic potential. Clin Exp Allergy 2006;36:1281–1288.
38. Wang Y, Sunwoo H, Cherian G, Sim JS. Fatty acid determination in chicken egg yolk: a comparison of different methods. Poult Sci 2000;79:1168–1171.
39. Constant S, Pfeiffer C, Woodard A, Pasqualini T, Bottomly K. Extent of T cell receptor ligation can determine the functional differentiation of naive CD4+ T cells. J Exp Med 1995;182:1591–1596.
40. Buatois V, Baillet M, Becart S, Mooney N, Leserman L, Machy P. MHC class II-peptide complexes in dendritic cell lipid microdomains initiate the CD4 Th1 phenotype. J Immunol 2003;171:5812–5819.
41. Delamarre L, Holcombe H, Mellman I. Presentation of exogenous antigens on major histocompatibility complex (MHC) class I and MHC class II molecules is differentially regulated during dendritic cell maturation. J Exp Med 2003;198:111–122.
42. Kuronuma K, Mitsuzawa H, Takeda K, Nishitani C, Chan ED, Kuroki Y et al. Anionic pulmonary surfactant phospholipids inhibit inflammatory responses from alveolar macrophages and U937 cells by binding the lipopolysaccharide-interacting proteins CD14 and MD-2. J Biol Chem 2009;284:25488–25500.
43. Hussaarts L, Yazdanbakhsh M, Guigas B. Priming dendritic cells for th2 polarization: lessons learned from helminths and implications for metabolic disorders. Front Immunol 2014;5:499.
44. Konieczna P, Schiavi E, Ziegler M, Groeger D, Healy S, Grant R et al. Human dendritic cell DC-SIGN and TLR-2 mediate complementary immune regulatory activities in response to Lactobacillus rhamnosus JB-1. PLoS One 2015;10:e0120261.
45. Marrack P, McKee AS, Munks MW. Towards an understanding of the adjuvant action of aluminium. Nat Rev Immunol 2009;9:287–293.