메뉴 건너뛰기




Volumn 63, Issue 1, 2006, Pages 235-242

Crystal structure at 1.45-Å resolution of the major allergen endo-β-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome

Author keywords

( )8 TIM barrel structure; Allergen; Catalytic groove; IgE binding epitopes; glucan

Indexed keywords

ALLERGEN; BETA 1,3 GLUCAN SYNTHETASE; GLUCAN; GLUCAN GLUCOSIDASE; GLUTAMIC ACID; GLYCOSIDASE; IMMUNOGLOBULIN E; PUSTULAN; TRISACCHARIDE; UNCLASSIFIED DRUG;

EID: 33645018648     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20876     Document Type: Article
Times cited : (44)

References (57)
  • 1
    • 0036863222 scopus 로고    scopus 로고
    • Clinical aspects of food allergy
    • Papageorgiou PS. Clinical aspects of food allergy. Biochem Soc Trans 2002;30:901-906.
    • (2002) Biochem Soc Trans , vol.30 , pp. 901-906
    • Papageorgiou, P.S.1
  • 5
    • 0036864268 scopus 로고    scopus 로고
    • Pathogenesis-related (PR)-proteins identified as allergens
    • Hoffmann-Sommergruber K. Pathogenesis-related (PR)-proteins identified as allergens. Biochem Soc Trans 2002;30:930-935.
    • (2002) Biochem Soc Trans , vol.30 , pp. 930-935
    • Hoffmann-Sommergruber, K.1
  • 7
    • 0029084994 scopus 로고
    • Prohevein from the rubber tree (Hevea brasiliensis) is a major latex allergen
    • Alenius H, Kalkkinen N, Lukka M, et al. Prohevein from the rubber tree (Hevea brasiliensis) is a major latex allergen. Clin Exp Allergy 1995;25:659-665.
    • (1995) Clin Exp Allergy , vol.25 , pp. 659-665
    • Alenius, H.1    Kalkkinen, N.2    Lukka, M.3
  • 8
    • 0036227247 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the Hevea brasiliensis allergen Hev b 11, a class I chitinase
    • O'Riordain G, Radauer C, Hoffmann-Sommergruber K, et al. Cloning and molecular characterization of the Hevea brasiliensis allergen Hev b 11, a class I chitinase. Clin Exp Allergy 2002;32:455-462.
    • (2002) Clin Exp Allergy , vol.32 , pp. 455-462
    • O'Riordain, G.1    Radauer, C.2    Hoffmann-Sommergruber, K.3
  • 9
    • 0031953751 scopus 로고    scopus 로고
    • Plant defense-related enzymes as latex allergens
    • Yagami T, Sato M, Nakamura A, et al. Plant defense-related enzymes as latex allergens. J Allergy Clin Immunol 1998;101:379-385.
    • (1998) J Allergy Clin Immunol , vol.101 , pp. 379-385
    • Yagami, T.1    Sato, M.2    Nakamura, A.3
  • 10
    • 33645023531 scopus 로고    scopus 로고
    • Hevea brasiliensis lipid transfer precursor protein mRNA, partial cs
    • Beezhold DH, Reschke GL, Hickey VL. Hevea brasiliensis lipid transfer precursor protein mRNA, partial cs. Accession AY057860. EMBL Database; 2001.
    • (2001) EMBL Database
    • Beezhold, D.H.1    Reschke, G.L.2    Hickey, V.L.3
  • 11
    • 0031251754 scopus 로고    scopus 로고
    • Differential gene expression in ripening banana fruit
    • Clendennen SK, May GD. Differential gene expression in ripening banana fruit. Plant Physiol 1997;115:463-469.
    • (1997) Plant Physiol , vol.115 , pp. 463-469
    • Clendennen, S.K.1    May, G.D.2
  • 12
    • 0033786158 scopus 로고    scopus 로고
    • Fruit-specific lectins from banana and plantain
    • Peumans WJ, Zhang W, Barre A, et al. Fruit-specific lectins from banana and plantain. Planta 2000;211:546-554.
    • (2000) Planta , vol.211 , pp. 546-554
    • Peumans, W.J.1    Zhang, W.2    Barre, A.3
  • 13
    • 0033651713 scopus 로고    scopus 로고
    • Purification and structural analysis of an abundant thaumatin-like protein from ripe banana fruit
    • Barre A, Peumans WJ, Menu-Bouaouiche L, et al. Purification and structural analysis of an abundant thaumatin-like protein from ripe banana fruit. Planta 2000;211:791-799.
    • (2000) Planta , vol.211 , pp. 791-799
    • Barre, A.1    Peumans, W.J.2    Menu-Bouaouiche, L.3
  • 14
    • 0033956457 scopus 로고    scopus 로고
    • Purification, characterization, and structural analysis of an abundant β-1,3-glucanase from banana fruit
    • Peumans WJ, Barre A, Derycke V, et al. Purification, characterization, and structural analysis of an abundant β-1,3-glucanase from banana fruit. Eur J Biochem 2000;267:1188-1195.
    • (2000) Eur J Biochem , vol.267 , pp. 1188-1195
    • Peumans, W.J.1    Barre, A.2    Derycke, V.3
  • 15
    • 0036802220 scopus 로고    scopus 로고
    • The abundant class III chitinase homolog in young developing banana fruits behaves as a transient vegetative storage protein and most probably serves as an important supply of amino acids for the synthesis of ripening-associated proteins
    • Peumans WJ, Proost P, Swennen RL, Van Damme EJM. The abundant class III chitinase homolog in young developing banana fruits behaves as a transient vegetative storage protein and most probably serves as an important supply of amino acids for the synthesis of ripening-associated proteins. Plant Physiol 2002;130:1063-1072.
    • (2002) Plant Physiol , vol.130 , pp. 1063-1072
    • Peumans, W.J.1    Proost, P.2    Swennen, R.L.3    Van Damme, E.J.M.4
  • 17
    • 0032488931 scopus 로고    scopus 로고
    • Crystal structure of barley 1,3-1,4-β-glucanase at 2.0-Å resolution and comparison with Bacillus 1,3-1,4-β-glucanase
    • Muller JJ, Thomsen KK, Heinemann U. Crystal structure of barley 1,3-1,4-β-glucanase at 2.0-Å resolution and comparison with Bacillus 1,3-1,4-β-glucanase. J Biol Chem 1998;273:3438-3446.
    • (1998) J Biol Chem , vol.273 , pp. 3438-3446
    • Muller, J.J.1    Thomsen, K.K.2    Heinemann, U.3
  • 18
    • 0028812262 scopus 로고
    • Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-beta-glucanase
    • Hahn M, Olsen O, Politz O, Borriss R, Heinemann U. Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-beta-glucanase. J Biol Chem 1995;270:3081-3088.
    • (1995) J Biol Chem , vol.270 , pp. 3081-3088
    • Hahn, M.1    Olsen, O.2    Politz, O.3    Borriss, R.4    Heinemann, U.5
  • 19
    • 0028841188 scopus 로고
    • Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanhydrolase at 1.8 Å resolution
    • Hahn M, Pons J, Planas A, Querol E, Heinemann U. Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanhydrolase at 1.8 Å resolution. FEBS Lett 1995;374:221-224.
    • (1995) FEBS Lett , vol.374 , pp. 221-224
    • Hahn, M.1    Pons, J.2    Planas, A.3    Querol, E.4    Heinemann, U.5
  • 20
    • 0344012467 scopus 로고    scopus 로고
    • The three-dimensional structures of two β-agarases
    • Allouch J, Jam M, Helbert W, et al. The three-dimensional structures of two β-agarases. J Biol Chem 2003;278:47171-47180.
    • (2003) J Biol Chem , vol.278 , pp. 47171-47180
    • Allouch, J.1    Jam, M.2    Helbert, W.3
  • 21
    • 1842554929 scopus 로고    scopus 로고
    • Parallel substrate binding sites in a β-agarase suggest a novel mode of action on double helical agarose
    • Allouch J, Helbert W, Henrissat B, Czjzek M. Parallel substrate binding sites in a β-agarase suggest a novel mode of action on double helical agarose. Structure 2004;12:623-632.
    • (2004) Structure , vol.12 , pp. 623-632
    • Allouch, J.1    Helbert, W.2    Henrissat, B.3    Czjzek, M.4
  • 22
    • 0033215006 scopus 로고    scopus 로고
    • Purification and properties of a basic endo-β1,6-glucanase (BGN16.1) from the antagonistic fungus Trichoderma harzianum
    • De la Cruz J, Llobell A. Purification and properties of a basic endo-β1,6-glucanase (BGN16.1) from the antagonistic fungus Trichoderma harzianum. Eur J Biochem 1999;265:145-151.
    • (1999) Eur J Biochem , vol.265 , pp. 145-151
    • De La Cruz, J.1    Llobell, A.2
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276A:307-326.
    • (1997) Methods Enzymol , vol.276 A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Cryst 1994;A50:157-163.
    • (1994) Acta Cryst , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 25
    • 16644364842 scopus 로고    scopus 로고
    • REFMAC5 dictionary: Organization of prior chemical knowledge and guidelines for its use
    • Vagin AA, Steiner RA, Lebedev AA, et al. REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use. Acta Cryst 2004;D60:2184-2195.
    • (2004) Acta Cryst , vol.D60 , pp. 2184-2195
    • Vagin, A.A.1    Steiner, R.A.2    Lebedev, A.A.3
  • 27
    • 0000243829 scopus 로고
    • PRO-CHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PRO-CHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993;26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 28
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. Molscript: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 1991;24:946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
    • Esnouf RM, An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J Mol Graphics 1997;15:132-134.
    • (1997) J Mol Graphics , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 30
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt EA, Bacon DJ. Raster3D photorealistic molecular graphics. Methods Enzymol 1997;277:505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 32
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999;15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 33
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tool
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tool. Nucleic Acids Res 1997;15:4876-4882.
    • (1997) Nucleic Acids Res , vol.15 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 34
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse aminoacid sequences
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP. Hydrophobic cluster analysis: an efficient new way to compare and analyse aminoacid sequences. FEBS Lett 1987;224:149-155.
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 35
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-293.
    • (1991) Proteins , vol.11 , pp. 281-293
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 36
    • 0023280069 scopus 로고
    • Calculation of electrostatic potential in an enzyme active site
    • Gilson MK, Honing BH. Calculation of electrostatic potential in an enzyme active site. Nature 1987;330:84-86.
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.K.1    Honing, B.H.2
  • 37
    • 0036137241 scopus 로고    scopus 로고
    • ProPred: Prediction of HLA-DR binding sites
    • Singh H, Raghava GPS. ProPred: prediction of HLA-DR binding sites. Bioinformatics 2001;17:1236-1237.
    • (2001) Bioinformatics , vol.17 , pp. 1236-1237
    • Singh, H.1    Raghava, G.P.S.2
  • 38
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982;157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 39
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins
    • Karplus PA, Schulz GE. Prediction of chain flexibility in proteins. Naturwissenschaften 1985;72:212-213.
    • (1985) Naturwissenschaften , vol.72 , pp. 212-213
    • Karplus, P.A.1    Schulz, G.E.2
  • 40
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971;55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 41
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp TP, Woods KR. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 1981;78:3824-3828.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3824-3828
    • Hopp, T.P.1    Woods, K.R.2
  • 42
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B, Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr Opin Struct Biol 1997;7:637-644.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 43
    • 0028956984 scopus 로고
    • β-glycosidase, β-galactosidase, family a cellulases, family F xylanases and two barley glucanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven
    • Jenkins J, Leggio LL, Harris G, Pickersgill R. β-Glycosidase, β-galactosidase, family A cellulases, family F xylanases and two barley glucanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven. FEBS Lett 1995;362:281-285.
    • (1995) FEBS Lett , vol.362 , pp. 281-285
    • Jenkins, J.1    Leggio, L.L.2    Harris, G.3    Pickersgill, R.4
  • 44
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA 1995;92:7090-7094.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 45
    • 0037168470 scopus 로고    scopus 로고
    • Aspergillus aculeatus β-1,4-galactanase: Substrate recognition and relations to other glycoside hydrolases in clan GH-A
    • Ryttersgaard C, Lo Leggio L, Coutinho PM, Henrissat B, Larsen S. Aspergillus aculeatus β-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A. Biochemistry 2002;41:15135-15143.
    • (2002) Biochemistry , vol.41 , pp. 15135-15143
    • Ryttersgaard, C.1    Lo Leggio, L.2    Coutinho, P.M.3    Henrissat, B.4    Larsen, S.5
  • 46
    • 0032566284 scopus 로고    scopus 로고
    • Snapshots along an enzymatic reaction coordinate: Analysis of a retaining beta-glycoside hydrolase
    • Davies GJ, Dauter M, Brzozowski AM, et al. Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase. Biochemistry 1998;37:11707-11713.
    • (1998) Biochemistry , vol.37 , pp. 11707-11713
    • Davies, G.J.1    Dauter, M.2    Brzozowski, A.M.3
  • 47
    • 0035040572 scopus 로고    scopus 로고
    • Characterization and expression of β-1,3-glucanase genes in peach
    • Thimmapuram J, Ko TS, Korban SS. Characterization and expression of β-1,3-glucanase genes in peach. Mol Genet Genomics 2001;265:469-479.
    • (2001) Mol Genet Genomics , vol.265 , pp. 469-479
    • Thimmapuram, J.1    Ko, T.S.2    Korban, S.S.3
  • 50
    • 0037865396 scopus 로고    scopus 로고
    • Mapping the conformational itinerary of beta-glycosidases by X-ray crystallography
    • Davies GJ, Ducros VM, Varrot A, Zechel DL. Mapping the conformational itinerary of beta-glycosidases by X-ray crystallography. Biochem Soc Trans 2003;31:523-527.
    • (2003) Biochem Soc Trans , vol.31 , pp. 523-527
    • Davies, G.J.1    Ducros, V.M.2    Varrot, A.3    Zechel, D.L.4
  • 51
    • 0033928258 scopus 로고    scopus 로고
    • Molecular and biochemical classification of plant-derived food allergens
    • Breiteneder H, Ebner C. Molecular and biochemical classification of plant-derived food allergens. J Allergy Clin Immunol 2000;106:27-36.
    • (2000) J Allergy Clin Immunol , vol.106 , pp. 27-36
    • Breiteneder, H.1    Ebner, C.2
  • 52
    • 0033955250 scopus 로고    scopus 로고
    • Male flower-specific expression of genes for polygalacturonase, pectin methylesterase and β-1,3-glucanase in a dioecious willow (Salix gilgiana Seemen)
    • Futamura N, Mori H, Kouchi H, Shinohara K. Male flower-specific expression of genes for polygalacturonase, pectin methylesterase and β-1,3-glucanase in a dioecious willow (Salix gilgiana Seemen). Plant Cell Physiol 2000;41:16-26.
    • (2000) Plant Cell Physiol , vol.41 , pp. 16-26
    • Futamura, N.1    Mori, H.2    Kouchi, H.3    Shinohara, K.4
  • 53
    • 0035958872 scopus 로고    scopus 로고
    • Ole e 9, a major olive pollen allergen is a 1,3-β-glucanase
    • Huecas S, Villalba M, Rodriguez R. Ole e 9, a major olive pollen allergen is a 1,3-β-glucanase. J Biol Chem 2001;276:27959-27966.
    • (2001) J Biol Chem , vol.276 , pp. 27959-27966
    • Huecas, S.1    Villalba, M.2    Rodriguez, R.3
  • 54
    • 17144416056 scopus 로고    scopus 로고
    • 1,3-β-glucanases as candidates in latex-pollen-vegetable food cross-reactivity
    • Palomares O, Villalba M, Quiralte J, Polo F, Rodriguez R. 1,3-β-Glucanases as candidates in latex-pollen-vegetable food cross-reactivity. Clin Exp Allergy 2005;35:345-351.
    • (2005) Clin Exp Allergy , vol.35 , pp. 345-351
    • Palomares, O.1    Villalba, M.2    Quiralte, J.3    Polo, F.4    Rodriguez, R.5
  • 55
    • 0029379568 scopus 로고
    • Beta-1,3-glucanase is highly-expressed in laticifers of Hevea brasiliensis
    • Chye ML, Cheung KY. Beta-1,3-glucanase is highly-expressed in laticifers of Hevea brasiliensis. Plant Mol Biol 1995;29:397-402.
    • (1995) Plant Mol Biol , vol.29 , pp. 397-402
    • Chye, M.L.1    Cheung, K.Y.2
  • 56
    • 0036673739 scopus 로고    scopus 로고
    • Allergies to cross-reactive plant proteins. Latex-fruit syndrome is comparable with pollen-food allergy syndrome
    • Yagami T. Allergies to cross-reactive plant proteins. Latex-fruit syndrome is comparable with pollen-food allergy syndrome. Int Arch Allergy Immunol 2002;128:271-279.
    • (2002) Int Arch Allergy Immunol , vol.128 , pp. 271-279
    • Yagami, T.1
  • 57
    • 0026954685 scopus 로고
    • Differential accumulation of mRNAs encoding extracellular and intracellular PR proteins in tomato induced by virulent and avirulent races of Cladosporium fulvum
    • Van Kan JA, Joosten MH, Wagemakers CA, Van den Berg-Velthuis GC, De Wit PJ. Differential accumulation of mRNAs encoding extracellular and intracellular PR proteins in tomato induced by virulent and avirulent races of Cladosporium fulvum. Plant Mol Biol 1992;20:513-527.
    • (1992) Plant Mol Biol , vol.20 , pp. 513-527
    • Van Kan, J.A.1    Joosten, M.H.2    Wagemakers, C.A.3    Van Den Berg-Velthuis, G.C.4    De Wit, P.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.