메뉴 건너뛰기




Volumn 63, Issue 41, 2015, Pages 9150-9158

Structural and Functional Characterization of the Hazelnut Allergen Cor a 8

Author keywords

allergen; food allergy; hazelnut; nonspecific lipid transfer protein; protein crystallization

Indexed keywords

ALLERGENS; COVALENT BONDS; CRYSTAL STRUCTURE; EPITOPES; FRUITS; MOLECULAR DYNAMICS;

EID: 84945312371     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/acs.jafc.5b03534     Document Type: Article
Times cited : (36)

References (55)
  • 2
    • 84903955619 scopus 로고    scopus 로고
    • Prevalence of common food allergies in Europe: A systematic review and meta-analysis
    • Nwaru, B. I.; Hickstein, L.; Panesar, S. S.; Roberts, G.; Muraro, A.; Sheikh, A. Prevalence of common food allergies in Europe: a systematic review and meta-analysis Allergy 2014, 69, 992-1007 10.1111/all.12423
    • (2014) Allergy , vol.69 , pp. 992-1007
    • Nwaru, B.I.1    Hickstein, L.2    Panesar, S.S.3    Roberts, G.4    Muraro, A.5    Sheikh, A.6
  • 5
    • 77952744759 scopus 로고    scopus 로고
    • US prevalence of self-reported peanut, tree nut, and sesame allergy: 11-year follow-up
    • Sicherer, S. H.; Munoz-Furlong, A.; Godbold, J. H.; Sampson, H. A. US prevalence of self-reported peanut, tree nut, and sesame allergy: 11-year follow-up J. Allergy Clin. Immunol. 2010, 125, 1322-1326 10.1016/j.jaci.2010.03.029
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. 1322-1326
    • Sicherer, S.H.1    Munoz-Furlong, A.2    Godbold, J.H.3    Sampson, H.A.4
  • 15
    • 38649137238 scopus 로고    scopus 로고
    • The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs)
    • Yeats, T. H.; Rose, J. K. The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs) Protein Sci. 2008, 17, 191-198 10.1110/ps.073300108
    • (2008) Protein Sci. , vol.17 , pp. 191-198
    • Yeats, T.H.1    Rose, J.K.2
  • 17
    • 0033853295 scopus 로고    scopus 로고
    • Structure, biological and technological functions of lipid transfer proteins and indolines, the major lipid binding proteins from cereal kernels
    • Douliez, J. P.; Michon, T.; Elmorjani, K.; Marion, D. Structure, biological and technological functions of lipid transfer proteins and indolines, the major lipid binding proteins from cereal kernels J. Cereal Sci. 2000, 32, 1-20 10.1006/jcrs.2000.0315
    • (2000) J. Cereal Sci. , vol.32 , pp. 1-20
    • Douliez, J.P.1    Michon, T.2    Elmorjani, K.3    Marion, D.4
  • 18
    • 0021402150 scopus 로고
    • Purification and characterization of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts
    • Kader, J. C.; Julienne, M.; Vergnolle, C. Purification and characterization of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts Eur. J. Biochem. 1984, 139, 411-416 10.1111/j.1432-1033.1984.tb08020.x
    • (1984) Eur. J. Biochem. , vol.139 , pp. 411-416
    • Kader, J.C.1    Julienne, M.2    Vergnolle, C.3
  • 19
    • 0041522376 scopus 로고    scopus 로고
    • Protein stability and plasticity of the hydrophobic cavity in wheat ns-LTP
    • Sy, D.; Le Gravier, Y.; Goodfellow, J.; Vovelle, F. Protein stability and plasticity of the hydrophobic cavity in wheat ns-LTP J. Biomol. Struct. Dyn. 2003, 21, 15-29 10.1080/07391102.2003.10506902
    • (2003) J. Biomol. Struct. Dyn. , vol.21 , pp. 15-29
    • Sy, D.1    Le Gravier, Y.2    Goodfellow, J.3    Vovelle, F.4
  • 21
    • 0035910388 scopus 로고    scopus 로고
    • Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases
    • Lindorff-Larsen, K.; Winther, J. R. Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases FEBS Lett. 2001, 488, 145-148 10.1016/S0014-5793(00)02424-8
    • (2001) FEBS Lett. , vol.488 , pp. 145-148
    • Lindorff-Larsen, K.1    Winther, J.R.2
  • 22
    • 0033769815 scopus 로고    scopus 로고
    • Lipid-transfer proteins as potential plant panallergens: Cross-reactivity among proteins of Artemisia pollen, Castanea nut and Rosaceae fruits, with different IgE-binding capacities
    • Diaz-Perales, A.; Lombardero, M.; Sanchez-Monge, R.; Garcia-Selles, F. J.; Pernas, M.; Fernandez-Rivas, M.; Barber, D.; Salcedo, G. Lipid-transfer proteins as potential plant panallergens: cross-reactivity among proteins of Artemisia pollen, Castanea nut and Rosaceae fruits, with different IgE-binding capacities Clin. Exp. Allergy 2000, 30, 1403-1410 10.1046/j.1365-2222.2000.00909.x
    • (2000) Clin. Exp. Allergy , vol.30 , pp. 1403-1410
    • Diaz-Perales, A.1    Lombardero, M.2    Sanchez-Monge, R.3    Garcia-Selles, F.J.4    Pernas, M.5    Fernandez-Rivas, M.6    Barber, D.7    Salcedo, G.8
  • 23
    • 77953592164 scopus 로고    scopus 로고
    • Comparison of IgE-binding capacity, cross-reactivity and biological potency of allergenic non-specific lipid transfer proteins from peach, cherry and hazelnut
    • Hartz, C.; Lauer, I.; del Mar San Miguel Moncin, M.; Cistero-Bahima, A.; Foetisch, K.; Lidholm, J.; Vieths, S.; Scheurer, S. Comparison of IgE-binding capacity, cross-reactivity and biological potency of allergenic non-specific lipid transfer proteins from peach, cherry and hazelnut Int. Arch. Allergy Immunol. 2010, 153, 335-346 10.1159/000316344
    • (2010) Int. Arch. Allergy Immunol. , vol.153 , pp. 335-346
    • Hartz, C.1    Lauer, I.2    Del Mar San Miguel Moncin, M.3    Cistero-Bahima, A.4    Foetisch, K.5    Lidholm, J.6    Vieths, S.7    Scheurer, S.8
  • 24
    • 84903129709 scopus 로고    scopus 로고
    • Cross-reactivity among non-specific lipid-transfer proteins from food and pollen allergenic sources
    • Morales, M.; Lopez-Matas, M. A.; Moya, R.; Carnes, J. Cross-reactivity among non-specific lipid-transfer proteins from food and pollen allergenic sources Food Chem. 2014, 165, 397-402 10.1016/j.foodchem.2014.05.101
    • (2014) Food Chem. , vol.165 , pp. 397-402
    • Morales, M.1    Lopez-Matas, M.A.2    Moya, R.3    Carnes, J.4
  • 25
    • 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, 276, 307-326 10.1016/S0076-6879(97)76066-X
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • Minor, W.; Cymborowski, M.; Otwinowski, Z.; Chruszcz, M. HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes Acta Crystallogr., Sect. D: Biol. Crystallogr. 2006, 62, 859-866 10.1107/S0907444906019949
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 27
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A.; Teplyakov, A. MOLREP: an automated program for molecular replacement J. Appl. Crystallogr. 1997, 30, 1022-1025 10.1107/S0021889897006766
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. The Buccaneer software for automated model building. 1. Tracing protein chains Acta Crystallogr., Sect. D: Biol. Crystallogr. 2006, 62, 1002-1011 10.1107/S0907444906022116
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 31
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A.; Morris, R.; Lamzin, V. S. Automated protein model building combined with iterative structure refinement Nat. Struct. Biol. 1999, 6, 458-463 10.1038/8263
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 37
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent treatment of internal and surface residues in empirical pK(a) predictions
    • Olsson, M. H. M.; Sondergaard, C. R.; Rostkowski, M.; Jensen, J. H. PROPKA3: consistent treatment of internal and surface residues in empirical pK(a) predictions J. Chem. Theory Comput. 2011, 7, 525-537 10.1021/ct100578z
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Sondergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 40
    • 84884192184 scopus 로고    scopus 로고
    • Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald
    • Salomon-Ferrer, R.; Gotz, A. W.; Poole, D.; Le Grand, S.; Walker, R. C. Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald J. Chem. Theory Comput. 2013, 9, 3878-3888 10.1021/ct400314y
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 3878-3888
    • Salomon-Ferrer, R.1    Gotz, A.W.2    Poole, D.3    Le Grand, S.4    Walker, R.C.5
  • 41
    • 2942539614 scopus 로고    scopus 로고
    • MmLib Python toolkit for manipulating annotated structural models of biological macromolecules
    • Painter, J.; Merritt, E. A. mmLib Python toolkit for manipulating annotated structural models of biological macromolecules J. Appl. Crystallogr. 2004, 37, 174-178 10.1107/S0021889803025639
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 174-178
    • Painter, J.1    Merritt, E.A.2
  • 42
    • 23844520061 scopus 로고    scopus 로고
    • A molecular viewer for the analysis of TLS rigid-body motion in macromolecules
    • Painter, J.; Merritt, E. A. A molecular viewer for the analysis of TLS rigid-body motion in macromolecules Acta Crystallogr., Sect. D: Biol. Crystallogr. 2005, 61, 465-471 10.1107/S0907444905001897
    • (2005) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.61 , pp. 465-471
    • Painter, J.1    Merritt, E.A.2
  • 43
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E.; Henrick, K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr., Sect. D: Biol. Crystallogr. 2004, 60, 2256-2268 10.1107/S0907444904026460
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E.; Henrick, K. Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 2007, 372, 774-797 10.1016/j.jmb.2007.05.022
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 47
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L.; Rosenstrom, P. Dali server: conservation mapping in 3D Nucleic Acids Res. 2010, 38, W545-549 10.1093/nar/gkq366
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-549
    • Holm, L.1    Rosenstrom, P.2
  • 48
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H.; Erez, E.; Martz, E.; Pupko, T.; Ben-Tal, N. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res. 2010, 38, W529-533 10.1093/nar/gkq399
    • (2010) Nucleic Acids Res. , vol.38 , pp. W529-533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 50
    • 77953592164 scopus 로고    scopus 로고
    • Comparison of IgE-binding capacity, cross-reactivity and biological potency of allergenic non-specific lipid transfer proteins from peach, cherry and hazelnut
    • Hartz, C.; Lauer, I.; del Mar San Miguel Moncin, M.; Cistero-Bahima, A.; Foetisch, K.; Lidholm, J.; Vieths, S.; Scheurer, S. Comparison of IgE-binding capacity, cross-reactivity and biological potency of allergenic non-specific lipid transfer proteins from peach, cherry and hazelnut Int. Arch. Allergy Immunol. 2010, 153, 335-346 10.1159/000316344
    • (2010) Int. Arch. Allergy Immunol. , vol.153 , pp. 335-346
    • Hartz, C.1    Lauer, I.2    Del Mar San Miguel Moncin, M.3    Cistero-Bahima, A.4    Foetisch, K.5    Lidholm, J.6    Vieths, S.7    Scheurer, S.8
  • 51
    • 84903129709 scopus 로고    scopus 로고
    • Cross-reactivity among non-specific lipid-transfer proteins from food and pollen allergenic sources
    • Morales, M.; Lopez-Matas, M. A.; Moya, R.; Carnes, J. Cross-reactivity among non-specific lipid-transfer proteins from food and pollen allergenic sources Food Chem. 2014, 165, 397-402 10.1016/j.foodchem.2014.05.101
    • (2014) Food Chem. , vol.165 , pp. 397-402
    • Morales, M.1    Lopez-Matas, M.A.2    Moya, R.3    Carnes, J.4
  • 52
    • 0042011224 scopus 로고    scopus 로고
    • Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals
    • Kantardjieff, K. A.; Rupp, B. Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals Protein Sci. 2003, 12, 1865-1871 10.1110/ps.0350503
    • (2003) Protein Sci. , vol.12 , pp. 1865-1871
    • Kantardjieff, K.A.1    Rupp, B.2
  • 55
    • 37049037250 scopus 로고    scopus 로고
    • Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity
    • Borges, J. P.; Barre, A.; Culerrier, R.; Granier, C.; Didier, A.; Rouge, P. Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity Biochem. Biophys. Res. Commun. 2008, 365, 685-690 10.1016/j.bbrc.2007.11.046
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 685-690
    • Borges, J.P.1    Barre, A.2    Culerrier, R.3    Granier, C.4    Didier, A.5    Rouge, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.