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Volumn 81, Issue , 2015, Pages 340-348

The Ala86Gln mutant β-lactoglobulin has increased ligand binding and decreased immunoreactivity properties

Author keywords

Ala; Alanine; Allergy; CD; circular dichroism; Circular dichroism; CMA; Competitive ELISA; cow's milk allergy; electro spray ionization mass spectrometry; ELISA; enzyme linked immunosorbent assay; ESI MS; Gln; Glutamine; high performance liquid chromatography; HPLC; Ligand binding; Mutation; SDS PAGE; sodium dodecyl sulfate polyacrylamide gel electrophoresis; wild type; WT; Lactoglobulin; lactoglobulin; LG

Indexed keywords

ALANINE; ALANINE 86; BETA LACTOGLOBULIN; EPITOPE; GLUTAMINE; IMMUNOGLOBULIN E; LIGAND; LIPOCALIN; MUTANT PROTEIN; PALMITIC ACID; RECOMBINANT PROTEIN; RESVERATROL; RETINOL; SEROTONIN; UNCLASSIFIED DRUG; CODON; LACTOGLOBULIN; PROTEIN BINDING;

EID: 84955287328     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2015.08.013     Document Type: Article
Times cited : (17)

References (58)
  • 2
    • 34548228414 scopus 로고    scopus 로고
    • Food allergen detection methods and the challenge to protectfood-allergic consumers
    • A.J. van Hengel, Food allergen detection methods and the challenge to protectfood-allergic consumers, Anal. Bioanal. Chem. 389 (2007) 111-118.
    • (2007) Anal. Bioanal. Chem , vol.389 , pp. 111-118
    • van Hengel, A.J.1
  • 6
    • 0039565352 scopus 로고    scopus 로고
    • Food allergies and other food sensitivities
    • S.L. Taylor, S.L. Hefle, Food allergies and other food sensitivities, Food Technol.55 (2001) 68-84.
    • (2001) Food Technol , vol.55 , pp. 68-84
    • Taylor, S.L.1    Hefle, S.L.2
  • 7
    • 0033786028 scopus 로고    scopus 로고
    • The Melbourne milk allergy study-two decades ofclinical research
    • C. Hosking, R. Heine, D. Hill, The Melbourne milk allergy study-two decades ofclinical research, Am. Concr. Inst. 12 (2000) 198-205.
    • (2000) Am. Concr. Inst , vol.12 , pp. 198-205
    • Hosking, C.1    Heine, R.2    Hill, D.3
  • 9
    • 25844447622 scopus 로고    scopus 로고
    • Clinical course andprognosis of cow's milk allergy are dependent on milk-specific IgE status
    • K.M. Saarinen, A.S. Pelkonen, M.J. Mäkelä, E. Savilahti, Clinical course andprognosis of cow's milk allergy are dependent on milk-specific IgE status, J. Allergy Clin. Immunol. 116 (2005) 869-875.
    • (2005) J. Allergy Clin. Immunol , vol.116 , pp. 869-875
    • Saarinen, K.M.1    Pelkonen, A.S.2    Mäkelä, M.J.3    Savilahti, E.4
  • 11
    • 28244436213 scopus 로고    scopus 로고
    • Probiotics and allergy
    • E. Furrie, Probiotics and allergy, Proc. Nutr. Soc. 64 (2005) 465-469.
    • (2005) Proc. Nutr. Soc , vol.64 , pp. 465-469
    • Furrie, E.1
  • 12
    • 0034975020 scopus 로고    scopus 로고
    • Intestinalpermeability in children: variation with age and reliability in the diagnosis ofcow's milk allergy
    • N. Kalach, F. Rocchiccioli, D. Boissieu, P.H. Benhamou, C. Dupont, Intestinalpermeability in children: variation with age and reliability in the diagnosis ofcow's milk allergy, Acta Paediatr. 90 (2001) 499-504.
    • (2001) Acta Paediatr , vol.90 , pp. 499-504
    • Kalach, N.1    Rocchiccioli, F.2    Boissieu, D.3    Benhamou, P.H.4    Dupont, C.5
  • 13
    • 0032199537 scopus 로고    scopus 로고
    • Cow's milk allergens
    • J.M. Wal, Cow's milk allergens, Allergy 53 (1998) 1013-1022.
    • (1998) Allergy , vol.53 , pp. 1013-1022
    • Wal, J.M.1
  • 15
    • 84948991919 scopus 로고    scopus 로고
    • β-Lactoglobulin
    • L. Sawyer, β-Lactoglobulin, Adv. Dairy Chem. (2013) 211-259.
    • (2013) Adv. Dairy Chem , pp. 211-259
    • Sawyer, L.1
  • 16
    • 8644235852 scopus 로고    scopus 로고
    • Bovine milk allergenicity
    • J.M. Wal, Bovine milk allergenicity, Ann. Allergy Asthma Immunol. 93 (2004) S2-S11.
    • (2004) Ann. Allergy Asthma Immunol , vol.93 , pp. S2-S11
    • Wal, J.M.1
  • 18
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying pH-induced dissociation of theβ-lactoglobulin dimer
    • S. Uhrínová, M.H. Smith, G.B. Jameson, D. Uhrín, L. Sawyer, P.N. Barlow, Structural changes accompanying pH-induced dissociation of theβ-lactoglobulin dimer, Biochemistry 39 (2000) 3565-3574.
    • (2000) Biochemistry , vol.39 , pp. 3565-3574
    • Uhrínová, S.1    Smith, M.H.2    Jameson, G.B.3    Uhrín, D.4    Sawyer, L.5    Barlow, P.N.6
  • 19
    • 0000048540 scopus 로고
    • Purification of β-lactoglobulin: isolation ofgenetic variants and influence of purification method on secondary structure
    • S. Ebeler, L. Phillips, J. Kinsella, Purification of β-lactoglobulin: isolation ofgenetic variants and influence of purification method on secondary structure, Milchwissenschaft 45 (1990) 694-698.
    • (1990) Milchwissenschaft , vol.45 , pp. 694-698
    • Ebeler, S.1    Phillips, L.2    Kinsella, J.3
  • 22
    • 4243120936 scopus 로고    scopus 로고
    • β-Lactoglobulin: binding properties, structure, and function
    • G. Kontopidis, C. Holt, L. Sawyer, β-Lactoglobulin: binding properties, structure, and function, J. Dairy Sci. 87 (2004) 785-796.
    • (2004) J. Dairy Sci , vol.87 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 23
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin withresveratrol and its biological implications
    • L. Liang, H.A. Tajmir-Riahi, M. Subirade, Interaction of β-lactoglobulin withresveratrol and its biological implications, Biomacromolecules 9 (2007) 50-56.
    • (2007) Biomacromolecules , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 24
    • 84857059676 scopus 로고    scopus 로고
    • Study of the acid and thermal stability ofβ-lactoglobulin-ligand complexes using fluorescence quenching
    • L. Liang, M. Subirade, Study of the acid and thermal stability ofβ-lactoglobulin-ligand complexes using fluorescence quenching, Food Chem.132 (2012) 2023-2029.
    • (2012) Food Chem , vol.132 , pp. 2023-2029
    • Liang, L.1    Subirade, M.2
  • 26
    • 84906276492 scopus 로고    scopus 로고
    • Bovineβ-lactoglobulin/fatty acid complexes: binding, structural, and biologicalproperties
    • S. Le Maux, S. Bouhallab, L. Giblin, A. Brodkorb, T. Croguennec, Bovineβ-lactoglobulin/fatty acid complexes: binding, structural, and biologicalproperties, Dairy Sci. Technol. 94 (2014) 409-426.
    • (2014) Dairy Sci. Technol , vol.94 , pp. 409-426
    • Le Maux, S.1    Bouhallab, S.2    Giblin, L.3    Brodkorb, A.4    Croguennec, T.5
  • 27
    • 84878398368 scopus 로고    scopus 로고
    • Binding of curcumin to β-lactoglobulin and its effecton antioxidant characteristics of curcumin
    • M. Li, Y. Ma, M.O. Ngadi, Binding of curcumin to β-lactoglobulin and its effecton antioxidant characteristics of curcumin, Food Chem. 141 (2013) 1504-1511.
    • (2013) Food Chem , vol.141 , pp. 1504-1511
    • Li, M.1    Ma, Y.2    Ngadi, M.O.3
  • 28
    • 84862756974 scopus 로고    scopus 로고
    • Binding of a perfluorinated surfactant to β-lactoglobulin in aqueous solutions
    • C. Schwieger, M.H. Ropers, Binding of a perfluorinated surfactant to β-lactoglobulin in aqueous solutions, Food Hydrocolloids 30 (2013) 241-248.
    • (2013) Food Hydrocolloids , vol.30 , pp. 241-248
    • Schwieger, C.1    Ropers, M.H.2
  • 29
    • 84901456941 scopus 로고    scopus 로고
    • Binding interaction of a prospectivechemotherapeutic antibacterial drug with β-lactoglobulin: results andchallenges
    • B.K. Paul, N. Ghosh, S. Mukherjee, Binding interaction of a prospectivechemotherapeutic antibacterial drug with β-lactoglobulin: results andchallenges, Langmuir 30 (2014) 5921-5929.
    • (2014) Langmuir , vol.30 , pp. 5921-5929
    • Paul, B.K.1    Ghosh, N.2    Mukherjee, S.3
  • 30
  • 31
    • 0034039993 scopus 로고    scopus 로고
    • Ligand-binding proteins: their potential forapplication in systems for controlled delivery and uptake of ligands
    • F.A. De Wolf, G.M. Brett, Ligand-binding proteins: their potential forapplication in systems for controlled delivery and uptake of ligands, Pharmacol. Rev. 52 (2000) 207-236.
    • (2000) Pharmacol. Rev , vol.52 , pp. 207-236
    • De Wolf, F.A.1    Brett, G.M.2
  • 34
    • 0018956182 scopus 로고
    • Milk hypersensitivity:RAST studies using new antigens generated by pepsin hydrolysis ofbeta-lactoglobulin
    • H. Schwartz, L. Nerurkar, J. Spies, R. Scanlon, J. Bellanti, Milk hypersensitivity:RAST studies using new antigens generated by pepsin hydrolysis ofbeta-lactoglobulin, Ann. Allergy Asthma Immunol. 45 (1980) 242-245.
    • (1980) Ann. Allergy Asthma Immunol , vol.45 , pp. 242-245
    • Schwartz, H.1    Nerurkar, L.2    Spies, J.3    Scanlon, R.4    Bellanti, J.5
  • 35
    • 0036980003 scopus 로고    scopus 로고
    • Frequency of cow's milk allergy in childhood
    • A. Høst, Frequency of cow's milk allergy in childhood, Ann. Allergy AsthmaImmunol. 89 (2002) 33-37.
    • (2002) Ann. Allergy AsthmaImmunol , vol.89 , pp. 33-37
    • Høst, A.1
  • 37
    • 84908143975 scopus 로고    scopus 로고
    • Lactobacillus delbrueckii subsp. bulgaricus CRL 454 cleaves allergenic peptides of β-lactoglobulin
    • M. Pescuma, E.M. Hébert, T. Haertlé, J.M. Chobert, F. Mozzi, G. Font de Valdez, Lactobacillus delbrueckii subsp. bulgaricus CRL 454 cleaves allergenic peptides of β-lactoglobulin, Food Chem. 170 (2015) 407-414.
    • (2015) Food Chem , vol.170 , pp. 407-414
    • Pescuma, M.1    Hébert, E.M.2    Haertlé, T.3    Chobert, J.M.4    Mozzi, F.5    Font de Valdez, G.6
  • 39
    • 84904420876 scopus 로고    scopus 로고
    • Antigenicity and conformationalchanges of β-lactoglobulin by dynamic high pressure microfluidizationcombining with glycation treatment
    • J. Zhong, Y. Tu, W. Liu, Y. Xu, C. Liu, R. Dun, Antigenicity and conformationalchanges of β-lactoglobulin by dynamic high pressure microfluidizationcombining with glycation treatment, J. Dairy Sci. 97 (2014) 4695-4702.
    • (2014) J. Dairy Sci , vol.97 , pp. 4695-4702
    • Zhong, J.1    Tu, Y.2    Liu, W.3    Xu, Y.4    Liu, C.5    Dun, R.6
  • 42
    • 27144547578 scopus 로고    scopus 로고
    • Molecular design of allergy vaccines
    • B. Linhart, R. Valenta, Molecular design of allergy vaccines, Curr. Opin.Immunol. 17 (2005) 646-655.
    • (2005) Curr. Opin.Immunol , vol.17 , pp. 646-655
    • Linhart, B.1    Valenta, R.2
  • 44
    • 0036598404 scopus 로고    scopus 로고
    • The future of antigen-specific immunotherapy of allergy
    • R. Valenta, The future of antigen-specific immunotherapy of allergy, Nat. Rev.Immunol. 2 (2002) 446-453.
    • (2002) Nat. Rev.Immunol , vol.2 , pp. 446-453
    • Valenta, R.1
  • 46
    • 15544382364 scopus 로고    scopus 로고
    • Multiple-mutation at a potential ligand-binding region decreasedallergenicity of a mite allergen Der f 2 without disrupting global structure
    • T. Nakazawa, T. Takai, H. Hatanaka, E. Mizuuchi, T. Nagamune, K. Okumura, H. Ogawa, Multiple-mutation at a potential ligand-binding region decreasedallergenicity of a mite allergen Der f 2 without disrupting global structure, FEBS Lett. 579 (2005) 1988-1994.
    • (2005) FEBS Lett , vol.579 , pp. 1988-1994
    • Nakazawa, T.1    Takai, T.2    Hatanaka, H.3    Mizuuchi, E.4    Nagamune, T.5    Okumura, K.6    Ogawa, H.7
  • 47
    • 84987300635 scopus 로고
    • Preparation of β-lactoglobulin andp-lactoglobulin-free proteins from whey retentate by NaCI salting out at lowpH
    • P. Mailliart, B. Ribadeau-Dumas, Preparation of β-lactoglobulin andp-lactoglobulin-free proteins from whey retentate by NaCI salting out at lowpH, J. Food Sci. 53 (1988) 743-745.
    • (1988) J. Food Sci , vol.53 , pp. 743-745
    • Mailliart, P.1    Ribadeau-Dumas, B.2
  • 48
    • 0033778182 scopus 로고    scopus 로고
    • New insight on β-lactoglobulin bindingsites by 1-anilinonaphthalene-8-sulfonate fluorescence decay
    • M. Collini, L. D'Alfonso, G. Baldini, New insight on β-lactoglobulin bindingsites by 1-anilinonaphthalene-8-sulfonate fluorescence decay, Protein Sci. 9 (2000) 1968-1974.
    • (2000) Protein Sci , vol.9 , pp. 1968-1974
    • Collini, M.1    D'Alfonso, L.2    Baldini, G.3
  • 50
    • 0008824744 scopus 로고    scopus 로고
    • Expression ofrecombinant wild-type and mutant β-lactoglobulins in the yeast Pichiapastoris
    • C. Wilson, L. Quarrie, G.J. Allan, D.J. Flint, L. Sawyer, C. Holt, Expression ofrecombinant wild-type and mutant β-lactoglobulins in the yeast Pichiapastoris, Int. J. Food Sci. Technol. 34 (1999) 445-450.
    • (1999) Int. J. Food Sci. Technol , vol.34 , pp. 445-450
    • Wilson, C.1    Quarrie, L.2    Allan, G.J.3    Flint, D.J.4    Sawyer, L.5    Holt, C.6
  • 51
    • 0017075905 scopus 로고
    • Binding affinities of retinoland related compounds to retinol binding proteins
    • U. Cogan, M. Kopelman, S. Mokady, M. Shinitzky, Binding affinities of retinoland related compounds to retinol binding proteins, Eur. J. Biochem. 65 (1976) 71-78.
    • (1976) Eur. J. Biochem , vol.65 , pp. 71-78
    • Cogan, U.1    Kopelman, M.2    Mokady, S.3    Shinitzky, M.4
  • 52
    • 7944227678 scopus 로고    scopus 로고
    • Study of the interactionbetween monoammonium glycyrrhizinate and bovine serum albumin
    • Y.-J. Hu, Y. Liu, J.-B. Wang, X.-H. Xiao, S.-S. Qu, Study of the interactionbetween monoammonium glycyrrhizinate and bovine serum albumin, J.Pharm. Biomed. Anal. 36 (2004) 915-919.
    • (2004) J.Pharm. Biomed. Anal , vol.36 , pp. 915-919
    • Hu, Y.-J.1    Liu, Y.2    Wang, J.-B.3    Xiao, X.-H.4    Qu, S.-S.5
  • 53
    • 0031227534 scopus 로고    scopus 로고
    • Productionand epitopic characterization of monoclonal antibodies against bovine β-lactoglobulin
    • A. Venien, D. Levieux, C. Astier, L. Briand, J.M. Chobert, T. Haertle, Productionand epitopic characterization of monoclonal antibodies against bovine β-lactoglobulin, J. Dairy Sci. 80 (1997) 1977-1987.
    • (1997) J. Dairy Sci , vol.80 , pp. 1977-1987
    • Venien, A.1    Levieux, D.2    Astier, C.3    Briand, L.4    Chobert, J.M.5    Haertle, T.6
  • 54
    • 0031424642 scopus 로고    scopus 로고
    • High-level expression of bovine beta-lactoglobulin in Pichia pastoris andcharacterization of its physical properties
    • T.-R. Kim, Y. Goto, N. Hirota, K. Kuwata, H. Denton, S.-Y. Wu, L. Sawyer, C.A. Batt, High-level expression of bovine beta-lactoglobulin in Pichia pastoris andcharacterization of its physical properties, Protein Eng. 10 (1997) 1339-1345.
    • (1997) Protein Eng , vol.10 , pp. 1339-1345
    • Kim, T.-R.1    Goto, Y.2    Hirota, N.3    Kuwata, K.4    Denton, H.5    Wu, S.-Y.6    Sawyer, L.7    Batt, C.A.8
  • 55
    • 77952531665 scopus 로고    scopus 로고
    • β-Lactoglobulin/folic acid complexes: formation, characterization, and biological implication
    • L. Liang, M. Subirade, β-Lactoglobulin/folic acid complexes: formation, characterization, and biological implication, J. Phys. Chem. B 114 (2010) 6707-6712.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6707-6712
    • Liang, L.1    Subirade, M.2
  • 57
    • 84877080943 scopus 로고    scopus 로고
    • Interactions of β-lactoglobulin variants A and B with vitamin A. Competitivebinding of retinoids and carotenoids
    • A. Mensi, Y. Choiset, H. Rabesona, T. Haertlé, P. Borel, J.M. Chobert, Interactions of β-lactoglobulin variants A and B with vitamin A. Competitivebinding of retinoids and carotenoids, J. Agric. Food Chem. 61 (2013) 4114-4119.
    • (2013) J. Agric. Food Chem , vol.61 , pp. 4114-4119
    • Mensi, A.1    Choiset, Y.2    Rabesona, H.3    Haertlé, T.4    Borel, P.5    Chobert, J.M.6


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