Cloning and characterization of a novel peanut allergen Ara h 3 isoform displaying potentially decreased allergenicity

Plant Science

Volumn 172, Issue 2, 2007, Pages 345-353

  Kang, I H ^a   Gallo, M ^a  

^a Genetics Institute   (United States)

Author keywords

Ara h 1; Ara h 2; Ara h 3; Epitopes; Peanut allergens; Seed storage proteins

Indexed keywords

CLONING; DNA; FOOD PRODUCTS; IMMUNOLOGY; PROTEINS;

EPITOPES; HYPOALLERGENIC PEANUT; PEANUT ALLERGENS; SEED STORAGE PROTEINS;

ALLERGIES;

ALLERGIES; NUCLEIC ACIDS; PEANUTS; SEEDS;

ARA; ARACHIS HYPOGAEA;

EID: 33846074928     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2006.09.014     Document Type: Article

References (44)

1. Yocum M.W., and Khan D.A. Assessment of patients who have experienced anaphylaxis: a 3-year survey. Mayo Clin. Proc. 69 (1994) 16-23
2. Sicherer S.H., Munoz-Furlong A., Burks A.W., and Sampson H.A. Prevalence of peanut and tree nut allergy in the U.S. determined by a random digit dial telephone survey. J. Allergy Clin. Immunol. 103 (1999) 559-562
3. Sampson H.A. Managing peanut allergy. Br. Med. J. 312 (1996) 1050-1051
4. Burks A.W. Peanut allergy: a growing phenomenon. J. Clin. Invest. 111 (2003) 950-952
5. Koppelman S.J., Vlooswijk R.A., Knippels L.M., Hessing M., Knol E.F., Reijsen V.F.C., and Bruijnzeel-Koomen C.A. Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world. Allergy 56 (2001) 132-137
6. Clarke M.C., Kilburn S.A., Hourihane J.O., Dean K.R., Warner J.O., and Dean T.P. Serological characteristics of peanut allergy. Clin. Exp. Allergy 28 (1998) 1251-1257
7. Burks A.W., Sampson H.A., and Bannon G.A. Review Article Series II. Peanut allergens. Allergy 53 (1998) 725-730
8. Rabjohn P., Helm E.M., Stanley J.S., West C.M., Sampson H.A., Burks A.W., and Bannon G.A. Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J. Clin. Invest. 103 (1999) 535-542
9. Kleber-Janke T., Crameri R., Appenzeller U., Schlaak M., and Becker W.M. Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int. Arch. Allergy Immunol. 119 (1999) 265-274
10. Eigenmann P.A., Burks A.W., Bannon G.A., and Sampson H.A. Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies. J Allergy Clin. Immunol. 98 (1996) 969-978
11. Koppelman S.J., Knol E.F., Vlooswijk R.A.A., Wensing M., Knulst A.C., Hefle S.L., Gruppen H., and Piersma S. Peanut allergen Ara h 3: isolation from peanuts and biochemical characterization. Allergy 58 (2003) 1144-1151
12. Koppelman S.J., Bruijnzeel-Koomen C.A., Hessing M., and De Jong H.H. Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J. Biol. Chem. 274 (1999) 4770-4777
13. Boldt A., Fortunato D., Conti A., Petersen A., Ballmer-Weber B., Lepp U., Reese G., and 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 5 (2005) 675-686
14. Restani P., Ballabio C., Corsini E., Fiocchi A., Isoardi P., Magni C., Poiesi C., Terracciano L., and Duranti M. Identification of the basic subunit of Ara h 3 as the major allergen in a group of children allergic to peanuts. Ann. Allergy Asthma Immunol. 94 (2005) 262-266
15. Rogers S.O., and Bendich A.J. Extraction of DNA from milligram amounts of fresh, herbarium and mummified plant tissue. Plant Mol. Biol. 5 (1985) 69-76
16. Notredame C., Higgins D., and Heringa J. T-Coffee: a novel method for multiple sequence alignments. J. Mol. Biol. 302 (2000) 205-217
17. Huang X. On global sequence alignment. Comput. Appl. Biosci. 10 (1994) 227-235
18. Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
19. Adachi M., Takenaka Y., Gidamis A.B., Mikami B., and Utsumi S. Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol. 305 (2001) 291-305
20. Towbin H.K., Staehelin T.H., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 4350-4354
21. Xiang P., Beardslee T.A., Zeece M.G., Markwell J., and Sarath G G. Identification and analysis of a conserved immunoglobulin E-binding epitope in soybean G1a and G2a and peanut Ara h 3 glycinins. Arch. Biochem. Biophys. 408 (2002) 51-57
22. Burks A.W., Cockrell G., Stanley J.S., Helm R.M., and Bannon G.A. Recombinant peanut allergen Ara h I expression and IgE binding in pateients with peanut hypersensitivity. J. Clin. Invest. 96 (1995) 1715-1721
23. Stanley J.S., King N., Burks A.W., Huang S.K., Sampson H., Cockrell G., Helm R.M., West C.M., and Bannon G.A. 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
24. Chatel J.M., Song L., Bhogal B., and Orson F.M. Various factors (allergen nature, mouse strain, CpG/recombinant protein expressed) influence the immune response elicited by genetic immunization. Allergy 58 (2003) 641-647
25. Dodo H.W., Viquez O.M., Maleki S.J., and 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. 52 (2004) 1404-1409
26. Yamada K., Shimada T., Kondo M., Nishimura M., and Hhara-Nishimura I. Multiple functional proteins are produced by cleaving Asn-Gln bonds of a single precursor by vacuolar processing enzyme. J. Biol. Chem. 274 (1999) 2563-2570
27. Gruis D.F., Selinger D.A., Curran J.M., and Jung R. Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases. Plant Cell 14 (2002) 2863-2882
28. Gruis D., Schulze J., and Jung R. Storage protein accumulation in the absence of the vacuolar processing enzyme family of cysteine proteases. Plant Cell 16 (2004) 270-290
29. Piersma S.R., Gaspari M., Hefle S.L., and Koppelman S.J. Proteolytic processing of the peanut allergen Ara h 3. Mol. Nutr. Food Res. 49 (2005) 744-755
30. Dickinson C.D., Hussein E.H.A., and Nielsen N.C. Role of posttranslational cleavage in glycinin assembly. Plant Cell 1 (1989) 459-469
31. Scott M.P., Jung R., Muntz K., and Nielsen N.C. A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 658-662
32. Nielsen N.C., Dickinson C.D., Cho T.J., Thanh V.H., Scallon B.J., Fischer R.L., Sims T.L., Drews G.N., and Goldberg R.B. Characterization of the glycinin gene family in soybean. Plant Cell 1 (1989) 313-328
33. Jung R., Scott M.P., Nam Y.W., Beaman T.W., Bassuner R., Sallbach I., Muntz K., and Nielsen N.C. The role of proteolysis in the processing and assembly of 11S seed globulins. Plant Cell 10 (1998) 343-357
34. Domoney C., and Casey R. Measurement of gene number for seed storage proteins in Pisum. Nucleic Acids Res. 13 (1985) 687-699
35. Baumlein H., Wobus U., Pustell J., and Kafatos F.C. The legumin gene family: structure of a B type gene of Vicia faba and a possible legumin gene specific regulatory element. Nucleic Acids Res. 14 (1986) 2707-2720
36. Chlan C.A., Pyle J., Legocki A., and Dure III L. Developmental biochemistry of cottonseed embryogenesis and germination. XVIII. cDNA and amino acid sequences of the members of the storage protein families. Plant Mol. Biol. 7 (1986) 475-489
37. Beardslee T.A., Zeece M.G., Sarath G., and Markwell J.P. Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int. Arch. Allergy Immunol. 123 (2000) 299-307
38. Sims T.L., and Goldberg R.B. The glycinin Gy1 gene from soybean. Nucleic Acids Res. 17 (1989) 4386
39. Lycett G.W., Croy R.R., Shirsat A.H., and Boulter D. The complete nucleotide sequence of a legumin gene from pea (Pisum sativum L.). Nucleic Acids Res. 12 (1984) 4493-4506
40. Schlesier B., Bassuner R., Van Hai N., and Muntz K. The cDNA derived primary structure of two distinct legumin A subunit precursors from field bean (Vicia faba L.). Nucleic Acids Res. 18 (1990) 7146
41. Beyer K., Grishina G., Bardina L., Grishin A., and Sampson H.A. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. J. Allergy Clin. Immunol. 110 (2002) 517-523
42. Tai S.S., Wu L.S., Chen E.C., and Tzen J.T. Molecular cloning of 11S globulin and 2S albumin, the two major seed storage proteins in sesame. J. Agric. Food Chem. 47 (1999) 4932-4938
43. Okita T.W., Hwang Y.S., Hnilo J., Kim W.T., Aryan A.P., Larson R., and Krishnan H.B. Structure and expression of the rice glutelin multigene family. J. Biol Chem. 264 (1989) 12573-12581
44. Tanchak M.A., Giband M., Potier B., Schernthaner J.P., Dukiandjiev S., and Altosaar I. Genomic clones encoding 11S globulins in oats (Avena sativa L.). Genome 38 (1995) 627-634