Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity

Clinical Immunology

Volumn 115, Issue 3, 2005, Pages 302-312

  Palmer, G William ^a   Dibbern Jr , Donald A ^a   Burks, A Wesley ^b   Bannon, Gary A ^c   Bock, S Allan ^d   Porterfield, Harry S ^a   McDermott, Robert A ^a   Dreskin, Stephen C ^a  

^a UNIVERSITY OF COLORADO   (United States)

^b DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c MONSANTO COMPANY   (United States)

^d NATIONAL JEWISH MEDICAL AND RESEARCH CENTER   (United States)

Author keywords

Allergens; Ara h 1; Ara h 2; IgE; Mast cells; Peanuts; RBL SX 38 cells

Indexed keywords

ALLERGEN; IMMUNOGLOBULIN E; PROTEIN DERIVATIVE;

ADOLESCENT; ADULT; ALLERGENICITY; ARTICLE; CELL ACTIVATION; CHILD; CLINICAL ARTICLE; CONTROLLED STUDY; CROSS LINKING; DEGRANULATION; HUMAN; IMMUNOBLOTTING; IMMUNOCHEMISTRY; IN VITRO STUDY; PEANUT ALLERGY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PURIFICATION;

ADOLESCENT; ADULT; ALLERGENS; ANIMALS; BASOPHILS; BIOLOGICAL ASSAY; CHILD; CHILD, PRESCHOOL; GLYCOPROTEINS; HUMANS; IMMUNOCHEMISTRY; IMMUNOGLOBULIN E; MIDDLE AGED; PEANUT HYPERSENSITIVITY; PLANT PROTEINS; RATS;

EID: 19044376267     PISSN: 15216616     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clim.2005.02.011     Document Type: Article

References (44)

1. H.A. Sampson Update on food allergy J. Allergy Clin. Immunol. 113 2004 805 819 (quiz 820)
2. H.A. Sampson Food allergy JAMA 278 1997 1888 1894
3. R.S. Kagan, L. Joseph, C. Dufresne, K. Gray-Donald, E. Turnbull, Y.S. Pierre, and A.E. Clarke Prevalence of peanut allergy in primary-school children in Montreal, Canada J. Allergy Clin. Immunol. 112 2003 1223 1228
4. W. Burks, G.A. Bannon, S. Sicherer, and H.A. Sampson Peanut-induced anaphylactic reactions Int. Arch. Allergy Immunol. 119 1999 165 172
5. S.A. Bock, A. Munoz-Furlong, and H.A. Sampson Fatalities due to anaphylactic reactions to foods J. Allergy Clin. Immunol. 107 2001 191 193
6. J.B. Hourihane, S.A. Kilburn, J.A. Nordlee, S.L. Hefle, S.L. Taylor, and J.O. Warner An evaluation of the sensitivity of subjects with peanut allergy to very low doses of peanut protein: a randomized, double-blind, placebo-controlled food challenge study J. Allergy Clin. Immunol. 100 1997 596 600
7. J.O. Warner Peanut allergy: a major public health issue Pediatr. Allergy Immunol. 10 1999 14 20
8. D. Leung, H. Sampson, J. Yunginger, A. Burks, L. Schneider, C. Wortel, F. Davis, J. Hyun, and W. Shanahan Effect of anti-IgE therapy in patients with peanut allergy NEJM 348 2003 986 993
9. X.M. Li, K. Srivastava, A. Grishin, C.K. Huang, B. Schofield, W. Burks, and H.A. Sampson Persistent protective effect of heat-killed Escherichia coli producing "engineered," recombinant peanut proteins in a murine model of peanut allergy J. Allergy Clin. Immunol. 112 2003 159 167
10. X.M. Li, K. Srivastava, J.W. Huleatt, K. Bottomly, A.W. Burks, and H.A. Sampson Engineered recombinant peanut protein and heat-killed listeria monocytogenes coadministration protects against peanut-induced anaphylaxis in a murine model J. Immunol. 170 2003 3289 3295
11. L. Pons, U. Ponnappan, R.A. Hall, P. Simpson, G. Cockrell, C.M. West, H.A. Sampson, R.M. Helm, and A.W. Burks Soy immunotherapy for peanut-allergic mice: modulation of the peanut-allergic response J. Allergy Clin. Immunol. 114 2004 915 921
12. H.A. Sampson Adverse reactions to foods R.C.E. Middleton Jr. E.F. Ellis N.F. Adkinson Jr. J.W. Yunginger W.W. Busse Allergy, Principles and Practice vol. 2 1998 Mosby St. Louis 1162 1182
13. H.A. Sampson Clinical practice. Peanut allergy N. Engl. J. Med. 346 2002 1294 1299
14. W. Burks, H.A. Sampson, and G.A. Bannon Peanut allergens Allergy 53 1998 725 730
15. D.A. Moneret-Vautrin Modifications of allergenicity linked to food technologies Allerg. Immunol. (Paris) 30 1998 9 13
16. H.S. Nelson, J. Lahr, R. Rule, A. Bock, and D. Leung Treatment of anaphylactic sensitivity to peanuts by immunotherapy with injections of aqueous peanut extract J. Allergy Clin. Immunol. 99 1997 744 751
17. A.W. Burks, G. Cockrell, J.S. Stanley, R.M. Helm, and G.A. Bannon Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity J. Clin. Invest. 96 1995 1715 1721
18. J.S. Stanley, N. King, A.W. Burks, S.K. Huang, H. Sampson, G. Cockrell, R.M. Helm, C.M. West, and G.A. Bannon Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2 Arch. Biochem. Biophys. 342 1997 244 253
19. T. Kleber-Janke, R. Crameri, U. Appenzeller, M. Schlaak, and W.M. Becker Selective cloning of peanut allergens, including profilin and 2 S albumins, by phage display technology Int. Arch. Allergy Immunol. 119 1999 265 274
20. P. Rabjohn, E.M. Helm, J.S. Stanley, C.M. West, H.A. Sampson, A.W. Burks, and G.A. Bannon Molecular cloning and epitope analysis of the peanut allergen Ara h 3 J. Clin. Invest. 103 1999 535 542
21. L. Pons, C. Chery, A. Romano, F. Namour, M.C. Artesani, and J.L. Gueant The 18 kDa peanut oleosin is a candidate allergen for IgE-mediated reactions to peanuts Allergy 57 Suppl. 72 2002 88 93
22. D. Mittag, J. Akkerdaas, B.K. Ballmer-Weber, L. Vogel, M. Wensing, W.M. Becker, S.J. Koppelman, A.C. Knulst, A. Helbling, S.L. Hefle, R. Van Ree, and S. Vieths Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy J. Allergy Clin. Immunol. 114 2004 1410 1417
23. E.C. de Jong, M. Van Zijverden, S. Spanhaak, S.J. Koppelman, H. Pellegrom, and A.H. Penninks Identification and partial characterization of multiple major allergens in peanut proteins Clin. Exp. Allergy 28 1998 743 751
24. M.C. Clarke, S.A. Kilburn, J.O. Hourihane, K.R. Dean, J.O. Warner, and T.P. Dean Serological characteristics of peanut allergy Clin. Exp. Allergy 28 1998 1251 1257
25. G.W. Palmer, D.A. Dibbern, A.W. Burks, G.A. Bannon, S.A. Bock, H.S. Porterfield, R.A. McDermott, and S.C. Dreskin Ara h 2 is greater than 50 times more potent than Ara h 1 in a functional assay of peanut protein allergenicity, a difference not appreciated with immunoblots J. Allergy Clin. Immunol. 109 2002 S300
26. S.J. Koppelman, M. Wensing, M. Ertmann, A.C. Knulst, and E.F. Knol 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 34 2004 583 590
27. T.W. Wiegand, P.B. Williams, S.C. Dreskin, M.H. Jouvin, J.P. Kinet, and D. Tasset High-affinity oligonucleotide ligands to human IgE inhibit binding to Fc epsilon receptor I J. Immunol. 157 1996 221 230
28. D.J. Dibbern, G. Palmer, P. Williams, S. Bock, and S. Dreskin RBL cells expressing human FcεRI are a sensitive tool for exploring functional IgE-allergen interactions J. Immunol. Methods 274 2003 37 45
29. H.A. Sampson Utility of food specific IgE concentrations in predicting symptomatic food allergy J. Allergy Clin. Immunol. 107 2001 891 896
30. H.J. Schuurman, J. Cheng, and T. Lam Pathology of xenograft rejection: a commentary Xenotransplantation 10 2003 293 299
31. A.W. Burks, L.W. Williams, R.M. Helm, C. Connaughton, G. Cockrell, and T. O'Brien Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges J. Allergy Clin. Immunol. 88 1991 172 179
32. A.W. Burks, L.W. Williams, C. Connaughton, G. Cockrell, T.J. O'Brien, and R.M. Helm 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. 90 1992 962 969
33. D.W. MacGlashan Jr., S.P. Peters, J. Warner, and L.M. Lichtenstein Characteristics of human basophil sulfidopeptide leukotriene release: releasability defined as the ability of the basophil to respond to dimeric cross-links J. Immunol. 136 1986 2231 2239
34. D.W. MacGlashan Jr. Releasability of human basophils: cellular sensitivity and maximal histamine release are independent variables J. Allergy Clin. Immunol. 91 1993 605 615
35. Z. Peng, A.B. Becker, and F.E. Simons Binding properties of protein A and protein G for human IgE Int. Arch. Allergy Immunol. 104 1994 204 206
36. A. Bufe, K. Gehlhar, G. Schramm, M. Schlaak, and W.M. Becker Allergenic activity of a major grass pollen allergen is elevated in the presence of nasal secretion Am. J. Respir. Crit. Care Med. 157 1998 1269 1276
37. E. Sten, P.S. Skov, S.B. Andersen, A.M. Torp, A. Olesen, U. Bindslev-Jensen, L.K. Poulsen, and C. Bindslev-Jensen A comparative study of the allergenic potency of wild-type and glyphosate-tolerant gene-modified soybean cultivars APMIS 112 2004 21 28
38. B. Bohle, A. Breitwieser, B. Zwolfer, B. Jahn-Schmid, M. Sara, U.B. Sleytr, and C. Ebner A novel approach to specific allergy treatment: the recombinant fusion protein of a bacterial cell surface (S-layer) protein and the major birch pollen allergen Bet v 1 (rSbsC-Bet v 1) combines reduced allergenicity with immunomodulating capacity J. Immunol. 172 2004 6642 6648
39. A.C. Drew, N.P. Eusebius, L. Kenins, H.D. de Silva, C. Suphioglu, J.M. Rolland, and E. O'Hehir R Hypoallergenic variants of the major latex allergen Hev b 6.01 retaining human T lymphocyte reactivity J. Immunol. 173 2004 5872 5879
40. E.R. Tovey, and B.A. Baldo Comparison by electroblotting of IgE-binding components in extracts of house dust mite bodies and spent mite culture J. Allergy Clin. Immunol. 79 1987 93 102
41. J.D. Astwood, J.N. Leach, and R.L. Fuchs Stability of food allergens to digestion in vitro Nat. Biotechnol. 14 1996 1269 1273
42. M. Sen, R. Kopper, L. Pons, E.C. Abraham, A.W. Burks, and G.A. Bannon Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes J. Immunol. 169 2002 882 887
43. S.J. Maleki, R.A. Kopper, D.S. Shin, C.W. Park, C.M. Compadre, H. Sampson, A.W. Burks, and G.A. Bannon Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation J. Immunol. 164 2000 5844 5849
44. H. Ali, D. Collado-Escobar, and M. Beaven The rise in concentration of free Ca2+ and of pH provides sequential, synergistic signals for secretion in antigen-stimulated rat basophilic leukemia (RBL-2H3) cells J. Immunol. 143 1989 2626 2633