메뉴 건너뛰기




Volumn 147, Issue 4, 2008, Pages 289-298

Mal d 2, the thaumatin-like allergen from apple, is highly resistant to gastrointestinal digestion and thermal processing

Author keywords

Allergenicity; Circular dichroism; Food allergen; Protein stability

Indexed keywords

FOOD ALLERGEN; IMMUNOGLOBULIN E; PROTEIN MAL D 2; THAUMATIN; UNCLASSIFIED DRUG;

EID: 56549103207     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000144036     Document Type: Article
Times cited : (60)

References (47)
  • 1
    • 0028289160 scopus 로고
    • Apple allergy: The IgE-binding potency of apple strains is related to the occurrence of the 18-kDa allergen
    • Vieths S, Jankiewicz A, Schoning B, Aulepp H: Apple allergy: the IgE-binding potency of apple strains is related to the occurrence of the 18-kDa allergen. Allergy 1994;49:262-271.
    • (1994) Allergy , vol.49 , pp. 262-271
    • Vieths, S.1    Jankiewicz, A.2    Schoning, B.3    Aulepp, H.4
  • 2
  • 5
    • 0029613725 scopus 로고
    • Characterization of apple 18 and 31 kDa allergens by microsequencing and evaluation of their content during storage and ripening
    • Hsieh LS, Moos M Jr, Lin Y: Characterization of apple 18 and 31 kDa allergens by microsequencing and evaluation of their content during storage and ripening. J Allergy Clin Immunol 1995;96:960-970.
    • (1995) J Allergy Clin Immunol , vol.96 , pp. 960-970
    • Hsieh, L.S.1    Moos Jr, M.2    Lin, Y.3
  • 6
    • 0034132311 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding a 31-kDa, pathogenesis-related 5/thaumatin-like (PR5/TL) protein abundantly expressed in apple fruit (Nalus domestica cv. Fuji)
    • Oh DH, Song KJ, Shin YU, Chung WI: Isolation of a cDNA encoding a 31-kDa, pathogenesis-related 5/thaumatin-like (PR5/TL) protein abundantly expressed in apple fruit (Nalus domestica cv. Fuji). Biosci Biotechnol Biochem 2000;64:355-362.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 355-362
    • Oh, D.H.1    Song, K.J.2    Shin, Y.U.3    Chung, W.I.4
  • 7
    • 0037716584 scopus 로고    scopus 로고
    • Plant-based heterologous expression of Mal d 2, a thaumatin-like protein and allergen of apple (Malus domestica) , and its characterization as an antifungal protein
    • Krebitz M, Wagner B, Ferreira F, Peterbauer C, Campillo N, Witty M, Kolarich D, Steinkellner H, Scheiner O, Breiteneder H: Plant-based heterologous expression of Mal d 2, a thaumatin-like protein and allergen of apple (Malus domestica) , and its characterization as an antifungal protein. J Mol Biol 2003;329:721-730.
    • (2003) J Mol Biol , vol.329 , pp. 721-730
    • Krebitz, M.1    Wagner, B.2    Ferreira, F.3    Peterbauer, C.4    Campillo, N.5    Witty, M.6    Kolarich, D.7    Steinkellner, H.8    Scheiner, O.9    Breiteneder, H.10
  • 9
    • 2342525840 scopus 로고    scopus 로고
    • A classification of plant food allergens
    • quiz 831
    • Breiteneder H, Radauer C: A classification of plant food allergens. J Allergy Clin Immunol 2004;113:821-830, quiz 831.
    • (2004) J Allergy Clin Immunol , vol.113 , pp. 821-830
    • Breiteneder, H.1    Radauer, C.2
  • 10
    • 0034651647 scopus 로고    scopus 로고
    • Variable expression of pathogenesis-related protein allergen in mountain cedar (Juniperus ashei) pollen
    • Midoro-Horiuti T, Goldblum RM, Kurosky A, Wood TG, Brooks EG: Variable expression of pathogenesis-related protein allergen in mountain cedar (Juniperus ashei) pollen. J Immunol 2000;164:2188-2192.
    • (2000) J Immunol , vol.164 , pp. 2188-2192
    • Midoro-Horiuti, T.1    Goldblum, R.M.2    Kurosky, A.3    Wood, T.G.4    Brooks, E.G.5
  • 11
    • 2342538399 scopus 로고    scopus 로고
    • Cloning and expression of a major allergen from Cupressus arizonica pollen, Cup a 3, a PR-5 protein expressed under polluted environment
    • Cortegano I, Civantos E, Aceituno E, del Moral A, Lopez E, Lombardero M, del Pozo V, Lahoz C: Cloning and expression of a major allergen from Cupressus arizonica pollen, Cup a 3, a PR-5 protein expressed under polluted environment. Allergy 2004;59:485-490.
    • (2004) Allergy , vol.59 , pp. 485-490
    • Cortegano, I.1    Civantos, E.2    Aceituno, E.3    del Moral, A.4    Lopez, E.5    Lombardero, M.6    del Pozo, V.7    Lahoz, C.8
  • 18
    • 0037949470 scopus 로고    scopus 로고
    • Heterologous expression in Nicotiana benthamiana of Cap a 1, a thaumatin-like protein and major allergen from bell pepper (Capsicum annuum)
    • Fuchs HC, Hoffmann-Sommergruber K, Wagner B, Krebitz M, Scheiner O, Breiteneder H: Heterologous expression in Nicotiana benthamiana of Cap a 1, a thaumatin-like protein and major allergen from bell pepper (Capsicum annuum). J Allergy Clin Immunol 2002;109:S134.
    • (2002) J Allergy Clin Immunol , vol.109
    • Fuchs, H.C.1    Hoffmann-Sommergruber, K.2    Wagner, B.3    Krebitz, M.4    Scheiner, O.5    Breiteneder, H.6
  • 19
    • 2342578126 scopus 로고    scopus 로고
    • Thaumatin-like proteins - a new family of pollen and fruit allergens
    • Breiteneder H: Thaumatin-like proteins - a new family of pollen and fruit allergens. Allergy 2004;59:479-481.
    • (2004) Allergy , vol.59 , pp. 479-481
    • Breiteneder, H.1
  • 20
    • 33745614616 scopus 로고    scopus 로고
    • Shatters RG Jr, Boykin LM, Lapointe SL, Hunter WB, Weathersbee AA 3rd: Phylogenetic and structural relationships of the PR5 gene family reveal an ancient multigene family conserved in plants and select animal taxa. J Mol Evol 2006;63:12-29.
    • Shatters RG Jr, Boykin LM, Lapointe SL, Hunter WB, Weathersbee AA 3rd: Phylogenetic and structural relationships of the PR5 gene family reveal an ancient multigene family conserved in plants and select animal taxa. J Mol Evol 2006;63:12-29.
  • 21
    • 0027096460 scopus 로고
    • Crystal structure of a sweet tasting protein thaumatin I, at 1.65 A resolution
    • Ogata CM, Gordon PF, de Vos AM, Kim SH: Crystal structure of a sweet tasting protein thaumatin I, at 1.65 A resolution. J Mol Biol 1992;228:893-908.
    • (1992) J Mol Biol , vol.228 , pp. 893-908
    • Ogata, C.M.1    Gordon, P.F.2    de Vos, A.M.3    Kim, S.H.4
  • 23
    • 0015494327 scopus 로고
    • Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth
    • van der Wel H, Loeve K: Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth. Eur J Biochem 1972;31:221-225.
    • (1972) Eur J Biochem , vol.31 , pp. 221-225
    • van der Wel, H.1    Loeve, K.2
  • 24
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • Astwood JD, Leach JN, Fuchs RL: Stability of food allergens to digestion in vitro. Nat Biotechnol 1996;14:1269-1273.
    • (1996) Nat Biotechnol , vol.14 , pp. 1269-1273
    • Astwood, J.D.1    Leach, J.N.2    Fuchs, R.L.3
  • 25
    • 12544254069 scopus 로고    scopus 로고
    • Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion
    • Moreno FJ, Mellon FA, Wickham MS, Bottrill AR, Mills EN: Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion. FEBS J 2005;272:341-352.
    • (2005) FEBS J , vol.272 , pp. 341-352
    • Moreno, F.J.1    Mellon, F.A.2    Wickham, M.S.3    Bottrill, A.R.4    Mills, E.N.5
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: 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
  • 29
    • 0036816556 scopus 로고    scopus 로고
    • Glycosylation of proteins in plants and invertebrates
    • Wilson IB: Glycosylation of proteins in plants and invertebrates. Curr Opin Struct Biol 2002;12:569-577.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 569-577
    • Wilson, I.B.1
  • 30
    • 0037145909 scopus 로고    scopus 로고
    • Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid - a comparative study
    • Fu TJ, Abbott UR, Hatzos C: Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid - a comparative study. J Agric Food Chem 2002;50:7154-7160.
    • (2002) J Agric Food Chem , vol.50 , pp. 7154-7160
    • Fu, T.J.1    Abbott, U.R.2    Hatzos, C.3
  • 32
    • 0035116853 scopus 로고    scopus 로고
    • Structure-sweetness relationship in thaumatin: Importance of lysine residues
    • Kaneko R, Kitabatake N: Structure-sweetness relationship in thaumatin: importance of lysine residues. Chem Senses 2001;26:167-177.
    • (2001) Chem Senses , vol.26 , pp. 167-177
    • Kaneko, R.1    Kitabatake, N.2
  • 33
    • 0015908718 scopus 로고
    • Spectrometric investigation of thaumatin I and II, two sweet-tasting proteins from Thaumatococcus daniellii Benth
    • Korver O, van Gorkom M, van der Wel H: Spectrometric investigation of thaumatin I and II, two sweet-tasting proteins from Thaumatococcus daniellii Benth. Eur J Biochem 1973;35:554-558.
    • (1973) Eur J Biochem , vol.35 , pp. 554-558
    • Korver, O.1    van Gorkom, M.2    van der Wel, H.3
  • 34
    • 0030021265 scopus 로고    scopus 로고
    • The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family
    • Batalia MA, Monzingo AF, Ernst S, Roberts W, Robertus JD: The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family. Nat Struct Biol 1996;3:19-23.
    • (1996) Nat Struct Biol , vol.3 , pp. 19-23
    • Batalia, M.A.1    Monzingo, A.F.2    Ernst, S.3    Roberts, W.4    Robertus, J.D.5
  • 36
    • 33846567968 scopus 로고    scopus 로고
    • Gastrointestinal digestion of food allergens: Effect on their allergenicity
    • Moreno FJ: Gastrointestinal digestion of food allergens: effect on their allergenicity. Biomed Pharmacother 2007;61:50-60.
    • (2007) Biomed Pharmacother , vol.61 , pp. 50-60
    • Moreno, F.J.1
  • 38
    • 0032745308 scopus 로고    scopus 로고
    • The amino acidic substitution of cysteine 167 by serine (C167S) in BstVI restriction endonuclease of Bacillus stearothermophilus V affects its conformation and thermostability
    • Loyola C, Saavedra C, Gomez I, Vasquez C: The amino acidic substitution of cysteine 167 by serine (C167S) in BstVI restriction endonuclease of Bacillus stearothermophilus V affects its conformation and thermostability. Biochimie 1999;81:261-266.
    • (1999) Biochimie , vol.81 , pp. 261-266
    • Loyola, C.1    Saavedra, C.2    Gomez, I.3    Vasquez, C.4
  • 39
    • 0032532007 scopus 로고    scopus 로고
    • Susceptibility towards intramolecular disulphidebond formation affects conformational stability and folding of human basic fibroblast growth factor
    • Estape D, van den Heuvel J, Rinas U: Susceptibility towards intramolecular disulphidebond formation affects conformational stability and folding of human basic fibroblast growth factor. Biochem J 1998;335:343-349.
    • (1998) Biochem J , vol.335 , pp. 343-349
    • Estape, D.1    van den Heuvel, J.2    Rinas, U.3
  • 40
    • 0028985861 scopus 로고
    • Conformational constraints in protein degradation by the 20S proteasome
    • Wenzel T, Baumeister W: Conformational constraints in protein degradation by the 20S proteasome. Nat Struct Biol 1995;2:199-204.
    • (1995) Nat Struct Biol , vol.2 , pp. 199-204
    • Wenzel, T.1    Baumeister, W.2
  • 41
    • 25144519047 scopus 로고    scopus 로고
    • Thermostability and in vitro digestibility of a purified major allergen 2S albumin (Ses i 1) from white sesame seeds (Sesamum indicum L.)
    • Moreno FJ, Maldonado BM, Wellner N, Mills EN: Thermostability and in vitro digestibility of a purified major allergen 2S albumin (Ses i 1) from white sesame seeds (Sesamum indicum L.). Biochim Biophys Acta 2005;1752:142-153.
    • (2005) Biochim Biophys Acta , vol.1752 , pp. 142-153
    • Moreno, F.J.1    Maldonado, B.M.2    Wellner, N.3    Mills, E.N.4
  • 43
    • 0023644668 scopus 로고
    • Thermal destruction processes in proteins involving cystine residues
    • Volkin DB, Klibanov AM: Thermal destruction processes in proteins involving cystine residues. J Biol Chem 1987;262:2945-2950.
    • (1987) J Biol Chem , vol.262 , pp. 2945-2950
    • Volkin, D.B.1    Klibanov, A.M.2
  • 44
    • 0033371883 scopus 로고    scopus 로고
    • Heat-induced formation of intermolecular disulfide linkages between thaumatin molecules that do not contain cysteine residues
    • Kaneko R, Kitabatake N: Heat-induced formation of intermolecular disulfide linkages between thaumatin molecules that do not contain cysteine residues. J Agric Food Chem 1999;47:4950-4955.
    • (1999) J Agric Food Chem , vol.47 , pp. 4950-4955
    • Kaneko, R.1    Kitabatake, N.2
  • 45
    • 0025351555 scopus 로고
    • Epitopes on protein antigens: Misconceptions and realities
    • Laver WG, Air GM, Webster RG, Smith-Gill SJ: Epitopes on protein antigens: misconceptions and realities. Cell 1990;61:553-556.
    • (1990) Cell , vol.61 , pp. 553-556
    • Laver, W.G.1    Air, G.M.2    Webster, R.G.3    Smith-Gill, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.