Crystal structure of the major peanut allergen Ara h 1

Molecular Immunology

Volumn 49, Issue 1-2, 2011, Pages 115-123

  Cabanos, Cerrone ^a   Urabe, Hiroyuki ^a   Tandang Silvas, Mary Rose ^a   Utsumi, Shigeru ^a   Mikami, Bunzo ^a   Maruyama, Nobuyuki ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

7S globulin; Electrostatic potential; Food allergen; IgE epitope; Peanut; Thermal stability; X ray crystallography

Indexed keywords

ALLERGEN ARA H 1; EPITOPE; FOOD ALLERGEN; IMMUNOGLOBULIN; IMMUNOGLOBULIN 7S; MONOMER; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; INTESTINE; NONHUMAN; PEANUT; PRIORITY JOURNAL; TEMPERATURE; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANTIGENS, PLANT; ARACHIS HYPOGAEA; CALORIMETRY, DIFFERENTIAL SCANNING; CRYSTALLOGRAPHY, X-RAY; EPITOPE MAPPING; EPITOPES, B-LYMPHOCYTE; GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

ARA; ARACHIS HYPOGAEA;

EID: 82455198597     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2011.08.004     Document Type: Article

References (45)

1. Adams P.D., Afonine P.V., Bunkoczi G., Chen V.B., Davis I.W., Echols N., Headd J.J., Hung L.W., Kapral G.J., Grosse-Kunstleve R.W., McCoy A.J., Moriarty N.W., Oeffner R., Read R.J., Richardson D.C., Richardson J.S., Terwilliger T.C., Zwart P.H. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D: Biol. Crystallogr. 2010, 66:213-221.
2. Anon The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D: Biol. Crystallogr. 1994, 50:760-763.
3. Astwood J.D., Leach J.N., Fuchs R.L. Stability of food allergens to digestion in vitro. Nat. Biotechnol. 1996, 14:1269-1273.
4. Bindslev-Jensen C., Briggs D., Osterballe M. Can we determine a threshold level for allergenic foods by statistical analysis of published data in the literature?. Allergy 2002, 57:741-746.
5. Bock S.A., Munoz-Furlong A., Sampson H.A. Fatalities due to anaphylactic reactions to foods. J. Allergy Clin. Immunol. 2001, 107:191-193.
6. Boldt A., Fortunato D., Conti A., Petersen A., Ballmer-Weber B., Lepp U., Reese G., Becker W.M. Analysis of the composition of an immunoglobulin E reactive high molecular weight protein complex of peanut extract containing Ara h 1 and Ara h 3/4. Proteomics 2005, 5:675-686.
7. Burks A.W., Shin D., Cockrell G., Stanley J.S., Helm R.M., Bannon G.A. Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. Eur. J. Biochem. 1997, 245:334-339.
8. Burks A.W., Williams L.W., Helm R.M., Connaughton C., Cockrell G., O'Brien T. Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. J. Allergy Clin. Immunol. 1991, 88:172-179.
9. Cabanos C., Urabe H., Masuda T., Tandang-Silvas M.R., Utsumi S., Mikami B., Maruyama N. Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region. Acta Crystallogr. F: Struct. Biol. Cryst. Commun. 2010, 66:1071-1073.
10. de Jong E.C., Van Zijverden M., Spanhaak S., Koppelman S.J., Pellegrom H., Penninks A.H. Identification and partial characterization of multiple major allergens in peanut proteins. Clin. Exp. Allergy 1998, 28:743-751.
11. Dodo H.W., Viquez O.M., Maleki S.J., Konan K.N. cDNA clone of a putative peanut (Arachis hypogaea L.) trypsin inhibitor has homology with peanut allergens Ara h 3 and Ara h 4. J. Agric. Food Chem. 2004, 52:1404-1409.
12. Emmett S.E., Angus F.J., Fry J.S., Lee P.N. Perceived prevalence of peanut allergy in Great Britain and its association with other atopic conditions and with peanut allergy in other household members. Allergy 1999, 54:380-385.
13. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D: Biol. Crystallogr. 2004, 60:2126-2132.
14. Fukuda T., Maruyama N., Salleh M.R., Mikami B., Utsumi S. Characterization and crystallography of recombinant 7S globulins of Adzuki bean and structure-function relationships with 7S globulins of various crops. J. Agric. Food Chem. 2008, 56:4145-4153.
15. Grundy J., Matthews S., Bateman B., Dean T., Arshad S.H. Rising prevalence of allergy to peanut in children: data from 2 sequential cohorts. J. Allergy Clin. Immunol. 2002, 110:784-789.
16. Itoh T., Garcia R.N., Adachi M., Maruyama Y., Tecson-Mendoza E.M., Mikami B., Utsumi S. Structure of 8Salpha globulin, the major seed storage protein of mung bean. Acta Crystallogr. D: Biol. Crystallogr. 2006, 62:824-832.
17. Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22:2577-2637.
18. Kleber-Janke T., Crameri R., Appenzeller U., Schlaak M., Becker W.M. Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int. Arch. Allergy Immunol. 1999, 119:265-274.
19. Koppelman S.J., Knol E.F., Vlooswijk R.A., Wensing M., Knulst A.C., Hefle S.L., Gruppen H., Piersma S. Peanut allergen Ara h 3: isolation from peanuts and biochemical characterization. Allergy 2003, 58:1144-1151.
20. Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D: Biol. Crystallogr. 2004, 60:2256-2268.
21. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
22. Lee B., Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 1971, 55:379-400.
23. Lehmann K., Schweimer K., Reese G., Randow S., Suhr M., Becker W.M., Vieths S., Rosch P. Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Biochem. J. 2006, 395:463-472.
24. Maleki S.J., Viquez O., Jacks T., Dodo H., Champagne E.T., Chung S.Y., Landry S.J. The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function. J. Allergy Clin. Immunol. 2003, 112:190-195.
25. Mari A., Scala E., Palazzo P., Ridolfi S., Zennaro D., Carabella G. Bioinformatics applied to allergy: allergen databases, from collecting sequence information to data integration. The allergome platform as a model. Cell. Immunol. 2006, 244:97-100.
26. Maruyama N., Adachi M., Takahashi K., Yagasaki K., Kohno M., Takenaka Y., Okuda E., Nakagawa S., Mikami B., Utsumi S. Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers. Eur. J. Biochem. 2001, 268:3595-3604.
27. Maruyama N., Katsube T., Wada Y., Oh M.H., Barba De La Rosa A.P., Okuda E., Nakagawa S., Utsumi S. The roles of the N-linked glycans and extension regions of soybean beta-conglycinin in folding, assembly and structural features. Eur. J. Biochem. 1998, 258:854-862.
28. Maruyama Y., Maruyama N., Mikami B., Utsumi S. Structure of the core region of the soybean beta-conglycinin alpha' subunit. Acta Crystallogr. D: Biol. Crystallogr. 2004, 60:289-297.
29. Mills E.N., Jenkins J., Marigheto N., Belton P.S., Gunning A.P., Morris V.J. Allergens of the cupin superfamily. Biochem. Soc. Trans. 2002, 30:925-929.
30. Osterballe M., Hansen T.K., Mortz C.G., Host A., Bindslev-Jensen C. The prevalence of food hypersensitivity in an unselected population of children and adults. Pediatr. Allergy Immunol. 2005, 16:567-573.
31. Petrey D., Honig B. GRASP2: visualization, surface properties, and electrostatics of macromolecular structures and sequences. Methods Enzymol. 2003, 374:492-509.
32. Pomes A., Helm R.M., Bannon G.A., Burks A.W., Tsay A., Chapman M.D. Monitoring peanut allergen in food products by measuring Ara h 1. J. Allergy Clin. Immunol. 2003, 111:640-645.
33. Roberts G. Anaphylaxis to foods. Pediatr. Allergy Immunol. 2007, 18:543-548.
34. Rouge P., Culerrier R., Sabatier V., Granier C., Rance F., Barre A. Mapping and conformational analysis of IgE-binding epitopic regions on the molecular surface of the major Ara h 3 legumin allergen of peanut (Arachis hypogaea). Mol. Immunol. 2009, 46:1067-1075.
35. Sen M., Kopper R., Pons L., Abraham E.C., Burks A.W., Bannon G.A. Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J. Immunol. 2002, 169:882-887.
36. Shin D.S., Compadre C.M., Maleki S.J., Kopper R.A., Sampson H., Huang S.K., Burks A.W., Bannon G.A. Biochemical and structural analysis of the IgE binding sites on ara h1, an abundant and highly allergenic peanut protein. J. Biol. Chem. 1998, 273:13753-13759.
37. Shreffler W.G., Beyer K., Chu T.H., Burks A.W., Sampson H.A. Microarray immunoassay: association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes. J. Allergy Clin. Immunol. 2004, 113:776-782.
38. Sicherer S.H., Munoz-Furlong A., Burks A.W., Sampson H.A. Prevalence of peanut and tree nut allergy in the US determined by a random digit dial telephone survey. J. Allergy Clin. Immunol. 1999, 103:559-562.
39. Sicherer S.H., Munoz-Furlong A., Sampson H.A. Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: a 5-year follow-up study. J. Allergy Clin. Immunol. 2003, 112:1203-1207.
40. Skolnick H.S., Conover-Walker M.K., Koerner C.B., Sampson H.A., Burks W., Wood R.A. The natural history of peanut allergy. J. Allergy Clin. Immunol. 2001, 107:367-374.
41. Vagin A., Teplyakov A. Molecular replacement with MOLREP. Acta Crystallogr. D: Biol. Crystallogr. 2010, 66:22-25.
42. Vaguine A.A., Richelle J., Wodak S.J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D: Biol. Crystallogr. 1999, 55:191-205.
43. van Boxtel E.L., Koppelman S.J., van den Broek L.A., Gruppen H. Determination of pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated peanut allergen Ara h 1. J. Agric. Food Chem. 2008, 56:2223-2230.
44. van Boxtel E.L., van Beers M.M., Koppelman S.J., van den Broek L.A., Gruppen H. Allergen Ara h 1 occurs in peanuts as a large oligomer rather than as a trimer. J. Agric. Food Chem. 2006, 54:7180-7186.
45. Wichers H.J., De Beijer T., Savelkoul H.F., Van Amerongen A. The major peanut allergen Ara h 1 and its cleaved-off N-terminal peptide; possible implications for peanut allergen detection. J. Agric. Food Chem. 2004, 52:4903-4907.