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Volumn 9, Issue 13, 2009, Pages 3507-3521

2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents

Author keywords

2 D DIGE; Arachis hypogaea; Food allergy; Proteome

Indexed keywords

FOOD ALLERGEN;

EID: 67651233459     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800938     Document Type: Article
Times cited : (51)

References (45)
  • 1
    • 0032856099 scopus 로고    scopus 로고
    • Specific immunoglobulin E to peanut, hazelnut and brazil nut in 731 patients: Similar patterns found at all ages
    • Pumphrey, R. S., Wilson, P. B., Faragher, E. B., Edwards, S. R., Specific immunoglobulin E to peanut, hazelnut and brazil nut in 731 patients: similar patterns found at all ages. Clin. Exp. Allergy 1999, 29, 1256-1259.
    • (1999) Clin. Exp. Allergy , vol.29 , pp. 1256-1259
    • Pumphrey, R.S.1    Wilson, P.B.2    Faragher, E.B.3    Edwards, S.R.4
  • 2
    • 0032565379 scopus 로고    scopus 로고
    • Resolution of peanut allergy: Case-control study
    • Hourihane, J. O., Roberts, S. A., Warner, J. O., Resolution of peanut allergy: case-control study. Br. Med. J. 1998, 316, 1271-1275.
    • (1998) Br. Med. J , vol.316 , pp. 1271-1275
    • Hourihane, J.O.1    Roberts, S.A.2    Warner, J.O.3
  • 4
    • 0026638876 scopus 로고
    • Fatal and nearfatal anaphylactic reactions to food in children and adolescents
    • Sampson, H. A., Mendelson, L., Rosen, J. P., Fatal and nearfatal anaphylactic reactions to food in children and adolescents. N. Engl. J. Med. 1992, 327, 380-384.
    • (1992) N. Engl. J. Med , vol.327 , pp. 380-384
    • Sampson, H.A.1    Mendelson, L.2    Rosen, J.P.3
  • 7
    • 0038681169 scopus 로고    scopus 로고
    • The natural progression of peanut allergy: Resolution and the possibility of recurrence
    • Fleischer, D. M., Conover-Walker, M. K., Christie, L., Burks, A. W. et al., The natural progression of peanut allergy: resolution and the possibility of recurrence. J. Allergy Clin. Immunol. 2003, 112, 183-189.
    • (2003) J. Allergy Clin. Immunol , vol.112 , pp. 183-189
    • Fleischer, D.M.1    Conover-Walker, M.K.2    Christie, L.3    Burks, A.W.4
  • 8
  • 9
    • 0037612518 scopus 로고    scopus 로고
    • Peanut allergy: An overview
    • Al-Muhsen, S., Clarke, A. E., Kagan, R. S., Peanut allergy: an overview. CMAJ. 2003, 168, 1279-1285.
    • (2003) CMAJ , vol.168 , pp. 1279-1285
    • Al-Muhsen, S.1    Clarke, A.E.2    Kagan, R.S.3
  • 10
    • 0026045826 scopus 로고
    • Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges
    • Burks, A. W., Williams, L. W., Helm, R. M., Connaughton, C. et al., 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.
    • (1991) J. Allergy Clin. Immunol , vol.88 , pp. 172-179
    • Burks, A.W.1    Williams, L.W.2    Helm, R.M.3    Connaughton, C.4
  • 11
    • 0038355287 scopus 로고    scopus 로고
    • Isolation and characterization of two complete Ara h 2 isoforms cDNA
    • Chatel, J. M., Bernard, H., Orson, F. M., Isolation and characterization of two complete Ara h 2 isoforms cDNA. Int. Arch. Allergy Immunol. 2003, 131, 14-18.
    • (2003) Int. Arch. Allergy Immunol , vol.131 , pp. 14-18
    • Chatel, J.M.1    Bernard, H.2    Orson, F.M.3
  • 12
    • 0033557358 scopus 로고    scopus 로고
    • Molecular cloning and epitope analysis of the peanut allergen Ara h 3
    • Rabjohn, P., Helm, E. M., Stanley, J. S., West, C. M. et al., Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J. Clin. Invest 1999, 103, 535-542.
    • (1999) J. Clin. Invest , vol.103 , pp. 535-542
    • Rabjohn, P.1    Helm, E.M.2    Stanley, J.S.3    West, C.M.4
  • 15
    • 15444378641 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis and Western-blotting analyses with anti Ara h 3 basic subunit IgG evidence the crossreacting polypeptides of Arachis hypogaea, Glycine max, and Lupinus albus seed proteomes
    • Magni, C., Ballabio, C., Restani, P., Sironi, E. et al., Two-dimensional electrophoresis and Western-blotting analyses with anti Ara h 3 basic subunit IgG evidence the crossreacting polypeptides of Arachis hypogaea, Glycine max, and Lupinus albus seed proteomes. J. Agric. Food Chem. 2005, 53, 2275-2281.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 2275-2281
    • Magni, C.1    Ballabio, C.2    Restani, P.3    Sironi, E.4
  • 16
    • 0032812397 scopus 로고    scopus 로고
    • Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology
    • Kleber-Janke, T., Crameri, R., Appenzeller, U., Schlaak, M. et al., Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int. Arch. Allergy Immunol. 1999, 119, 265-274.
    • (1999) Int. Arch. Allergy Immunol , vol.119 , pp. 265-274
    • Kleber-Janke, T.1    Crameri, R.2    Appenzeller, U.3    Schlaak, M.4
  • 17
    • 0035947021 scopus 로고    scopus 로고
    • Patient-tailored cloning of allergens by phage display: Peanut (Arachis hypogaea) profilin, a food allergen derived from a rare mRNA
    • Kleber-Janke, T., Crameri, R., Scheurer, S., Vieths, S. et al., Patient-tailored cloning of allergens by phage display: peanut (Arachis hypogaea) profilin, a food allergen derived from a rare mRNA. J. Chromatogr. B Biomed. Sci. Appl. 2001, 756, 295-305.
    • (2001) J. Chromatogr. B Biomed. Sci. Appl , vol.756 , pp. 295-305
    • Kleber-Janke, T.1    Crameri, R.2    Scheurer, S.3    Vieths, S.4
  • 18
    • 33646249121 scopus 로고    scopus 로고
    • Structure and stability of 2S albumin-type peanut allergens: Implications for the severity of peanut allergic reactions
    • Lehmann, K., Schweimer, K., Reese, G., Randow, S. et al., Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Biochem. J. 2006, 395, 463-472.
    • (2006) Biochem. J , vol.395 , pp. 463-472
    • Lehmann, K.1    Schweimer, K.2    Reese, G.3    Randow, S.4
  • 19
    • 8744286502 scopus 로고    scopus 로고
    • Isolation and characterization of natural Ara h 6: Evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat
    • Suhr, M., Wicklein, D., Lepp, U., Becker, W. M., Isolation and characterization of natural Ara h 6: evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat. Mol. Nutr. Food Res. 2004, 48, 390-399.
    • (2004) Mol. Nutr. Food Res , vol.48 , pp. 390-399
    • Suhr, M.1    Wicklein, D.2    Lepp, U.3    Becker, W.M.4
  • 20
    • 44649090661 scopus 로고    scopus 로고
    • Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform
    • Riecken, S., Lindner, B., Petersen, A., Jappe, U. et al., Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform. Biol. Chem. 2008, 389, 415-423.
    • (2008) Biol. Chem , vol.389 , pp. 415-423
    • Riecken, S.1    Lindner, B.2    Petersen, A.3    Jappe, U.4
  • 21
    • 9644262438 scopus 로고    scopus 로고
    • Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy
    • Mittag, D., Akkerdaas, J., Ballmer-Weber, B. K., Vogel, L. et al., 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. 2004, 114, 1410-1417.
    • (2004) J. Allergy Clin. Immunol , vol.114 , pp. 1410-1417
    • Mittag, D.1    Akkerdaas, J.2    Ballmer-Weber, B.K.3    Vogel, L.4
  • 22
    • 37749014992 scopus 로고    scopus 로고
    • Alleviating peanut allergy using genetic engineering: The silencing of the immunodominant allergen Ara h 2 leads to its significant reduction and a decrease in peanut allergenicity
    • Dodo, H. W., Konan, K. N., Chen, F. C., Egnin, M. et al., Alleviating peanut allergy using genetic engineering: the silencing of the immunodominant allergen Ara h 2 leads to its significant reduction and a decrease in peanut allergenicity. Plant Biotechnol. J. 2008, 6, 135-145.
    • (2008) Plant Biotechnol. J , vol.6 , pp. 135-145
    • Dodo, H.W.1    Konan, K.N.2    Chen, F.C.3    Egnin, M.4
  • 23
    • 58549103468 scopus 로고    scopus 로고
    • Reduction of IgE binding and nonpromotion of Aspergillus flavus fungal growth by simultaneously silencing Ara h 2 and Ara h 6 in peanut
    • Chu, Y., Faustinelli, P., Ramos, M. L., Hajduch, M. et al., Reduction of IgE binding and nonpromotion of Aspergillus flavus fungal growth by simultaneously silencing Ara h 2 and Ara h 6 in peanut. J. Agric. Food Chem. 2008, 56, 11225-11233.
    • (2008) J. Agric. Food Chem , vol.56 , pp. 11225-11233
    • Chu, Y.1    Faustinelli, P.2    Ramos, M.L.3    Hajduch, M.4
  • 24
    • 33750340111 scopus 로고    scopus 로고
    • Storage protein profiles in Spanish and runner market type peanuts and potential markers
    • Liang, X. Q., Luo, M., Holbrook, C. C., Guo, B. Z., Storage protein profiles in Spanish and runner market type peanuts and potential markers. BMC. Plant Biol. 2006, 6, 24
    • (2006) BMC. Plant Biol , vol.6 , pp. 24
    • Liang, X.Q.1    Luo, M.2    Holbrook, C.C.3    Guo, B.Z.4
  • 25
    • 55249092087 scopus 로고    scopus 로고
    • Proteomic screening points to the potential importance of Ara h 3 basic subunit in allergenicity of peanut
    • Guo, B., Liang, X., Chung, S. Y., Maleki, S. J., Proteomic screening points to the potential importance of Ara h 3 basic subunit in allergenicity of peanut. Inflamm. Allergy Drug Targets 2008, 7, 163-166.
    • (2008) Inflamm. Allergy Drug Targets , vol.7 , pp. 163-166
    • Guo, B.1    Liang, X.2    Chung, S.Y.3    Maleki, S.J.4
  • 26
    • 14644394893 scopus 로고    scopus 로고
    • 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
    • Boldt, A., Fortunato, D., Conti, A., Petersen, A. et al., 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.
    • (2005) Proteomics , vol.5 , pp. 675-686
    • Boldt, A.1    Fortunato, D.2    Conti, A.3    Petersen, A.4
  • 27
    • 67651230213 scopus 로고    scopus 로고
    • Becker, W. M., Purification of the natural peanut allergen Ara h 1. in: Holgate, S., Marone, G., Ring, J. (Eds.), Cellular and Molecular Targets in Allergy and Clinical Immunology, Hogrefe, Goettingen 2007, pp. 70-72.
    • Becker, W. M., Purification of the natural peanut allergen Ara h 1. in: Holgate, S., Marone, G., Ring, J. (Eds.), Cellular and Molecular Targets in Allergy and Clinical Immunology, Hogrefe, Goettingen 2007, pp. 70-72.
  • 28
    • 48949087726 scopus 로고    scopus 로고
    • 2-D DIGE analyses of enriched secretory lysosomes reveal heterogeneous profiles of functionally relevant proteins in leukemic and activated human NK cells
    • Schmidt, H., Gelhaus, C., Nebendahl, M., Lettau, M. et al., 2-D DIGE analyses of enriched secretory lysosomes reveal heterogeneous profiles of functionally relevant proteins in leukemic and activated human NK cells. Proteomics 2008, 8, 2911-2925.
    • (2008) Proteomics , vol.8 , pp. 2911-2925
    • Schmidt, H.1    Gelhaus, C.2    Nebendahl, M.3    Lettau, M.4
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 1979, 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 31
    • 0030957650 scopus 로고    scopus 로고
    • Improvement of the solubilization of proteins in twodimensional electrophoresis with immobilized pH gradients
    • Rabilloud, T., Adessi, C., Giraudel, A., Lunardi, J., Improvement of the solubilization of proteins in twodimensional electrophoresis with immobilized pH gradients. Electrophoresis 1997, 18, 307-316.
    • (1997) Electrophoresis , vol.18 , pp. 307-316
    • Rabilloud, T.1    Adessi, C.2    Giraudel, A.3    Lunardi, J.4
  • 32
    • 0035289178 scopus 로고    scopus 로고
    • Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology
    • Tonge, R., Shaw, J., Middleton, B., Rowlinson, R. et al., Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 2001, 1, 377-396.
    • (2001) Proteomics , vol.1 , pp. 377-396
    • Tonge, R.1    Shaw, J.2    Middleton, B.3    Rowlinson, R.4
  • 33
    • 27744559511 scopus 로고    scopus 로고
    • towards a proteomic analysis of Plasmodium falciparum
    • Fractionation and identification of proteins by 2-DE and MS
    • Gelhaus, C., Fritsch, J., Krause, E., Leippe, M., Fractionation and identification of proteins by 2-DE and MS: towards a proteomic analysis of Plasmodium falciparum. Proteomics. 2005, 5, 4213-4222.
    • (2005) Proteomics , vol.5 , pp. 4213-4222
    • Gelhaus, C.1    Fritsch, J.2    Krause, E.3    Leippe, M.4
  • 34
    • 0024311923 scopus 로고
    • The natural history of peanut allergy
    • Bock, S. A., Atkins, F. M., The natural history of peanut allergy. J. Allergy Clin. Immunol. 1989, 83, 900-904.
    • (1989) J. Allergy Clin. Immunol , vol.83 , pp. 900-904
    • Bock, S.A.1    Atkins, F.M.2
  • 35
    • 49349130487 scopus 로고
    • Legumin and vicilin, storage proteins of legume seeds
    • Derbyshire, E., Wright, D. J., Boulter, D., Legumin and vicilin, storage proteins of legume seeds. Phytochemistry 1976, 15, 3-24.
    • (1976) Phytochemistry , vol.15 , pp. 3-24
    • Derbyshire, E.1    Wright, D.J.2    Boulter, D.3
  • 36
    • 0030942818 scopus 로고    scopus 로고
    • Characterization of Ara h 1 by two-dimensional electrophoresis immunoblot and recombinant techniques: New digestion experiments with peanuts imitating the gastrointestinal tract
    • Becker, W. M., Characterization of Ara h 1 by two-dimensional electrophoresis immunoblot and recombinant techniques: new digestion experiments with peanuts imitating the gastrointestinal tract. Int. Arch. Allergy Immunol. 1997, 113, 118-121.
    • (1997) Int. Arch. Allergy Immunol , vol.113 , pp. 118-121
    • Becker, W.M.1
  • 37
    • 0035020401 scopus 로고    scopus 로고
    • Effects of cooking methods on peanut allergenicity
    • Beyer, K., Morrow, E., Li, X. M., Bardina, L. et al., Effects of cooking methods on peanut allergenicity. J. Allergy Clin. Immunol. 2001, 107, 1077-1081.
    • (2001) J. Allergy Clin. Immunol , vol.107 , pp. 1077-1081
    • Beyer, K.1    Morrow, E.2    Li, X.M.3    Bardina, L.4
  • 38
    • 34247107662 scopus 로고    scopus 로고
    • Effect of CyDye minimum labeling in differential gel electrophoresis on the reliability of protein identification
    • Hrebicek, T., Durrschmid, K., Auer, N., Bayer, K. et al., Effect of CyDye minimum labeling in differential gel electrophoresis on the reliability of protein identification. Electrophoresis 2007, 28, 1161-1169.
    • (2007) Electrophoresis , vol.28 , pp. 1161-1169
    • Hrebicek, T.1    Durrschmid, K.2    Auer, N.3    Bayer, K.4
  • 39
    • 3242762842 scopus 로고    scopus 로고
    • The major peanut allergen Ara h 1 and its cleavedoff N-terminal peptide; possible implications for peanut allergen detection
    • Wichers, H. J., De, B. T., Savelkoul, H. F., Van, A. A., The major peanut allergen Ara h 1 and its cleavedoff N-terminal peptide; possible implications for peanut allergen detection. J. Agric. Food Chem. 2004, 52, 4903-4907.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 4903-4907
    • Wichers, H.J.1    De, B.T.2    Savelkoul, H.F.3    Van, A.A.4
  • 40
    • 56749131953 scopus 로고    scopus 로고
    • Purification and characterisation of a panel of peanut allergens suitable for use in allergy diagnosis
    • Marsh, J., Rigby, N., Wellner, K., Reese, G. et al., Purification and characterisation of a panel of peanut allergens suitable for use in allergy diagnosis. Mol. Nutr. Food Res. 2008, 52, S272-S285.
    • (2008) Mol. Nutr. Food Res , vol.52
    • Marsh, J.1    Rigby, N.2    Wellner, K.3    Reese, G.4
  • 41
    • 0344393676 scopus 로고    scopus 로고
    • Serological characteristics of peanut allergy in children
    • Bernard, H., Paty, E., Mondoulet, L., Burks, A. W. et al., Serological characteristics of peanut allergy in children. Allergy 2003, 58, 1285-1292.
    • (2003) Allergy , vol.58 , pp. 1285-1292
    • Bernard, H.1    Paty, E.2    Mondoulet, L.3    Burks, A.W.4
  • 43
    • 2042449746 scopus 로고    scopus 로고
    • 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
    • Koppelman, S. J., Wensing, M., Ertmann, M., Knulst, A. C. et al., 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 2004, 34, 583-590.
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 583-590
    • Koppelman, S.J.1    Wensing, M.2    Ertmann, M.3    Knulst, A.C.4
  • 44
    • 19044376267 scopus 로고    scopus 로고
    • Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity
    • Palmer, G. W., Dibbern, D. A., Jr., Burks, A. W., Bannon, G. A. et al., Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity. Clin. Immunol. 2005, 115, 302-312.
    • (2005) Clin. Immunol , vol.115 , pp. 302-312
    • Palmer, G.W.1    Dibbern Jr., D.A.2    Burks, A.W.3    Bannon, G.A.4
  • 45
    • 36749011988 scopus 로고    scopus 로고
    • Identification of a new natural Ara h 6 isoform and of its proteolytic product as major allergens in peanut
    • Bernard, H., Mondoulet, L., Drumare, M. F., Paty, E. et al., Identification of a new natural Ara h 6 isoform and of its proteolytic product as major allergens in peanut. J. Agric. Food Chem. 2007, 55, 9663-9669.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 9663-9669
    • Bernard, H.1    Mondoulet, L.2    Drumare, M.F.3    Paty, E.4


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