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Volumn 8, Issue 8, 2013, Pages

Epitope Mapping and In Silico Characterization of Interactions between Der p 7 Allergen and MoAb WH9

Author keywords

[No Author keywords available]

Indexed keywords

D159A ALLERGEN; DER P 7 ALLERGEN; EPITOPE; HOUSE DUST ALLERGEN; HYDROGEN; I157A ALLERGEN; IMMUNOGLOBULIN E ANTIBODY; L158A ALLERGEN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY WH9; MUTANT PROTEIN; P160A ALLERGEN; S156A ALLERGEN; UNCLASSIFIED DRUG;

EID: 84881189967     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0071269     Document Type: Article
Times cited : (3)

References (35)
  • 1
    • 0027141028 scopus 로고
    • Molecular cloning of a house dust mite allergen with common antibody binding specificities with multiple components in mite extracts
    • Shen HD, Chua KY, Lin KL, Hsieh KH, Thomas WR, (1993) Molecular cloning of a house dust mite allergen with common antibody binding specificities with multiple components in mite extracts. Clin Exp Allergy 23: 934-940.
    • (1993) Clin Exp Allergy , vol.23 , pp. 934-940
    • Shen, H.D.1    Chua, K.Y.2    Lin, K.L.3    Hsieh, K.H.4    Thomas, W.R.5
  • 2
    • 0029069707 scopus 로고
    • Characterization of the house dust mite allergen Der p 7 by monoclonal antibodies
    • Shen HD, Chua KY, Lin WL, Hsieh KH, Thomas WR, (1995a) Characterization of the house dust mite allergen Der p 7 by monoclonal antibodies. Clin Exp Allergy 25: 416-422.
    • (1995) Clin Exp Allergy , vol.25 , pp. 416-422
    • Shen, H.D.1    Chua, K.Y.2    Lin, W.L.3    Hsieh, K.H.4    Thomas, W.R.5
  • 3
    • 0028973133 scopus 로고
    • Molecular cloning and immunological characterization of the house dust mite allergen Der f 7
    • Shen HD, CHua KY, Lin WL, Hsieh IM, Thomas WR, (1995b) Molecular cloning and immunological characterization of the house dust mite allergen Der f 7. Clin Exp Allergy 25: 1000-1006.
    • (1995) Clin Exp Allergy , vol.25 , pp. 1000-1006
    • Shen, H.D.1    Chua, K.Y.2    Lin, W.L.3    Hsieh, I.M.4    Thomas, W.R.5
  • 4
    • 0029914536 scopus 로고    scopus 로고
    • IgE and monoclonal antibody binding by the mite allergen Der p 7
    • Shen HD, Chua KY, Lin WL, Chen HL, Hsieh KH, et al. (1996) IgE and monoclonal antibody binding by the mite allergen Der p 7. Clin Exp Allergy 26: 308-315.
    • (1996) Clin Exp Allergy , vol.26 , pp. 308-315
    • Shen, H.D.1    Chua, K.Y.2    Lin, W.L.3    Chen, H.L.4    Hsieh, K.H.5
  • 5
    • 0030834372 scopus 로고    scopus 로고
    • Characterization of the allergen Der f 7 from house dust mite extracts by species-specific and cross-reactive monoclonal antibodies
    • Shen HD, Lin WL, Tsai LC, Tam MF, Chua KY, et al. (1997) Characterization of the allergen Der f 7 from house dust mite extracts by species-specific and cross-reactive monoclonal antibodies. Clin Exp Allergy 27: 824-832.
    • (1997) Clin Exp Allergy , vol.27 , pp. 824-832
    • Shen, H.D.1    Lin, W.L.2    Tsai, L.C.3    Tam, M.F.4    Chua, K.Y.5
  • 6
    • 79951942316 scopus 로고    scopus 로고
    • Homology modeling and monoclonal antibody binding of the Der f 7 dust mite allergen
    • Shen HD, Tam MF, Huang CH, Chou H, Tai HY, et al. (2011) Homology modeling and monoclonal antibody binding of the Der f 7 dust mite allergen. Immunol Cell Biol 89: 225-230.
    • (2011) Immunol Cell Biol , vol.89 , pp. 225-230
    • Shen, H.D.1    Tam, M.F.2    Huang, C.H.3    Chou, H.4    Tai, H.Y.5
  • 7
    • 77950301322 scopus 로고    scopus 로고
    • The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins
    • Mueller GA, Edwards LL, Aloor JJ, Aloor JJ, Fessler MB, et al. (2010) The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins. J Allergy Clin Immunol 125: 909-917.
    • (2010) J Allergy Clin Immunol , vol.125 , pp. 909-917
    • Mueller, G.A.1    Edwards, L.L.2    Aloor, J.J.3    Aloor, J.J.4    Fessler, M.B.5
  • 8
    • 84866065833 scopus 로고    scopus 로고
    • Crystal structure of Der f 7, a dust mite allergen from Dermatophagoides farinae
    • Tan KW, Jobichen C, Ong TC, Gao YF, Tiong YS, et al. (2012) Crystal structure of Der f 7, a dust mite allergen from Dermatophagoides farinae. PLoS One 7: e44850.
    • (2012) PLoS One , vol.7
    • Tan, K.W.1    Jobichen, C.2    Ong, T.C.3    Gao, Y.F.4    Tiong, Y.S.5
  • 9
    • 70450204938 scopus 로고    scopus 로고
    • Relevant B cell epitopes in allergic disease
    • Pomés A, (2010) Relevant B cell epitopes in allergic disease. Int Arch Allergy Immunol 152: 1-11.
    • (2010) Int Arch Allergy Immunol , vol.152 , pp. 1-11
    • Pomés, A.1
  • 10
    • 80051931126 scopus 로고    scopus 로고
    • Asp159 is a critical core amino acid of an IgE-binding and cross-reactive epitope of a dust mite allergen Der f 7
    • Chou H, Tam MF, Lee SS, Tang RB, Lin TH, et al. (2011) Asp159 is a critical core amino acid of an IgE-binding and cross-reactive epitope of a dust mite allergen Der f 7. Mol Immunol 48: 2130-2134.
    • (2011) Mol Immunol , vol.48 , pp. 2130-2134
    • Chou, H.1    Tam, M.F.2    Lee, S.S.3    Tang, R.B.4    Lin, T.H.5
  • 11
    • 77649272620 scopus 로고    scopus 로고
    • Rapid structural characterization of human antibody-antigen complexes through experimentally validated computational docking
    • Simonelli L, Beltramello M, Yudina Z, Macagno A, Calzolai L, et al. (2010) Rapid structural characterization of human antibody-antigen complexes through experimentally validated computational docking. J Mol Biol 396: 1491-1507.
    • (2010) J Mol Biol , vol.396 , pp. 1491-1507
    • Simonelli, L.1    Beltramello, M.2    Yudina, Z.3    Macagno, A.4    Calzolai, L.5
  • 12
    • 0033724387 scopus 로고    scopus 로고
    • Production and characterization of monoclonal antibodies to serine proteinase allergens in Penicillium and Aspergillus species
    • Lin WL, Chou H, Tam MF, Huang MH, Han SH, et al. (2000) Production and characterization of monoclonal antibodies to serine proteinase allergens in Penicillium and Aspergillus species. Clin Exp Allergy 30: 1653-1662.
    • (2000) Clin Exp Allergy , vol.30 , pp. 1653-1662
    • Lin, W.L.1    Chou, H.2    Tam, M.F.3    Huang, M.H.4    Han, S.H.5
  • 13
    • 0033971477 scopus 로고    scopus 로고
    • Kabat database and its applications: 30 years after the first variability plot
    • Johnson G, Wu TT, (2000) Kabat database and its applications: 30 years after the first variability plot. Nucleic Acids Res 28: 214-218.
    • (2000) Nucleic Acids Res , vol.28 , pp. 214-218
    • Johnson, G.1    Wu, T.T.2
  • 14
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 15
    • 0034436049 scopus 로고    scopus 로고
    • Mutual conformational adaptations in antigen and antibody upon complex formation between an Fab and HIV-1 capsid protein p24
    • Monaco-Malbet S, Berthet-Colominas C, Novelli A, Battaï N, Piga N, et al. (2000) Mutual conformational adaptations in antigen and antibody upon complex formation between an Fab and HIV-1 capsid protein p24. Structure 8: 1069-1077.
    • (2000) Structure , vol.8 , pp. 1069-1077
    • Monaco-Malbet, S.1    Berthet-Colominas, C.2    Novelli, A.3    Battaï, N.4    Piga, N.5
  • 16
    • 0037816292 scopus 로고    scopus 로고
    • The crystal structure of human angiogenin in complex with an antitumor neutralizing antibody
    • Chavali GB, Papageorgiou AC, Olson KA, Fett JW, Hu G, et al. (2003) The crystal structure of human angiogenin in complex with an antitumor neutralizing antibody. Structure 11: 875-885.
    • (2003) Structure , vol.11 , pp. 875-885
    • Chavali, G.B.1    Papageorgiou, A.C.2    Olson, K.A.3    Fett, J.W.4    Hu, G.5
  • 17
    • 84875472032 scopus 로고    scopus 로고
    • Structure of a human IgA1 Fab fragment at 1.55 Å resolution: potential effect of the constant domains on antigen-affinity modulation
    • Correa A, Trajtenberg F, Obal G, Pritsch O, Dighiero G, et al. (2013) Structure of a human IgA1 Fab fragment at 1.55 Å resolution: potential effect of the constant domains on antigen-affinity modulation. ActaCrystallogr D Biol Crystallogr 69: 388-397.
    • (2013) ActaCrystallogr D Biol Crystallogr , vol.69 , pp. 388-397
    • Correa, A.1    Trajtenberg, F.2    Obal, G.3    Pritsch, O.4    Dighiero, G.5
  • 18
    • 0029878720 scopus 로고    scopus 로고
    • VMD. Visual molecular dynamics
    • Humphrey W, Dalke A, Schulten K, (1996) VMD. Visual molecular dynamics. J Mol Graph 14: 33-28, 33-38, 27-28.
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 19
    • 80052903046 scopus 로고    scopus 로고
    • Accelerating Protein Docking in ZDOCK Using an Advanced 3D Convolution Library
    • Pierce BG, Hourai Y, Weng Z, (2011) Accelerating Protein Docking in ZDOCK Using an Advanced 3D Convolution Library. PLoS One 6: e24657.
    • (2011) PLoS One , vol.6
    • Pierce, B.G.1    Hourai, Y.2    Weng, Z.3
  • 21
    • 34047171268 scopus 로고    scopus 로고
    • Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab
    • Padavattan S, Schirmer T, Schmidt M, Akdis C, Valenta R, et al. (2007) Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab. J Mol Biol 368: 742-752.
    • (2007) J Mol Biol , vol.368 , pp. 742-752
    • Padavattan, S.1    Schirmer, T.2    Schmidt, M.3    Akdis, C.4    Valenta, R.5
  • 22
    • 35748953107 scopus 로고    scopus 로고
    • Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen
    • Niemi M, Jylhä S, Laukkanen ML, Söderlund H, Mäkinen-Kiljunen S, et al. (2007) Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen. Structure 15: 1413-1421.
    • (2007) Structure , vol.15 , pp. 1413-1421
    • Niemi, M.1    Jylhä, S.2    Laukkanen, M.L.3    Söderlund, H.4    Mäkinen-Kiljunen, S.5
  • 24
    • 0033711628 scopus 로고    scopus 로고
    • Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities
    • Xu JL, Davis MM, (2000) Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities. Immunity 13: 37-45.
    • (2000) Immunity , vol.13 , pp. 37-45
    • Xu, J.L.1    Davis, M.M.2
  • 25
    • 84857711026 scopus 로고    scopus 로고
    • Molecular determinants for antibody binding on group 1 house dust mite allergens
    • Chruszcz M, Pomés A, Glesner J, Vailes LD, Osinski T, et al. (2012) Molecular determinants for antibody binding on group 1 house dust mite allergens. J Biol Chem 287: 7388-7398.
    • (2012) J Biol Chem , vol.287 , pp. 7388-7398
    • Chruszcz, M.1    Pomés, A.2    Glesner, J.3    Vailes, L.D.4    Osinski, T.5
  • 26
  • 27
    • 53049108650 scopus 로고    scopus 로고
    • Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody
    • Li M, Gustchina A, Alexandratos J, Wlodawer A, Wünschmann S, et al. (2008) Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody. J Biol Chem 283: 22806-22814.
    • (2008) J Biol Chem , vol.283 , pp. 22806-22814
    • Li, M.1    Gustchina, A.2    Alexandratos, J.3    Wlodawer, A.4    Wünschmann, S.5
  • 28
    • 33645794229 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structure-based epitope mapping and modulation of dust mite group 13 allergen as a hypoallergen
    • Chan SL, Ong ST, Ong SY, Chew FT, Mok YK, (2006) Nuclear magnetic resonance structure-based epitope mapping and modulation of dust mite group 13 allergen as a hypoallergen. J Immunol 176: 4852-4860.
    • (2006) J Immunol , vol.176 , pp. 4852-4860
    • Chan, S.L.1    Ong, S.T.2    Ong, S.Y.3    Chew, F.T.4    Mok, Y.K.5
  • 29
    • 37549013725 scopus 로고    scopus 로고
    • Roles of structure and structural dynamics in the antibody recognition of the allergen proteins: an NMR study on Blomia tropicalis major allergen
    • Naik MT, Chang CF, Kuo IC, Kung CC, Yi FC, et al. (2008) Roles of structure and structural dynamics in the antibody recognition of the allergen proteins: an NMR study on Blomia tropicalis major allergen. Structure 16: 125-136.
    • (2008) Structure , vol.16 , pp. 125-136
    • Naik, M.T.1    Chang, C.F.2    Kuo, I.C.3    Kung, C.C.4    Yi, F.C.5
  • 30
    • 79960301160 scopus 로고    scopus 로고
    • Mechanisms of allergen-antibody interaction of cockroach allergen Bla g 2 with monoclonal antibodies that inhibit IgE antibody binding
    • Glesner J, Wünschmann S, Li M, Wlodawer A, Himly M, et al. (2011) Mechanisms of allergen-antibody interaction of cockroach allergen Bla g 2 with monoclonal antibodies that inhibit IgE antibody binding. PLoS One 6: e22223.
    • (2011) PLoS One , vol.6
    • Glesner, J.1    Wünschmann, S.2    Li, M.3    Wlodawer, A.4    Himly, M.5
  • 31
    • 0034235234 scopus 로고    scopus 로고
    • Dominant epitopes and allergic cross-reactivity: complex formation between a Fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen Bet v 1
    • Mirza O, Henriksen A, Ipsen H, Larsen JN, Wissenbach M, et al. (2000) Dominant epitopes and allergic cross-reactivity: complex formation between a Fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen Bet v 1. J Immunol 165: 331-338.
    • (2000) J Immunol , vol.165 , pp. 331-338
    • Mirza, O.1    Henriksen, A.2    Ipsen, H.3    Larsen, J.N.4    Wissenbach, M.5
  • 32
    • 79955549894 scopus 로고    scopus 로고
    • Mapping of conformational IgE epitopes with peptide-specific monoclonal antibodies reveals simultaneous binding of different IgE antibodies to a surface patch on the major birch pollen allergen, Bet v 1
    • Gieras A, Cejka P, Blatt K, Focke-Tejkl M, Linhart B, et al. (2011) Mapping of conformational IgE epitopes with peptide-specific monoclonal antibodies reveals simultaneous binding of different IgE antibodies to a surface patch on the major birch pollen allergen, Bet v 1. J Immunol 186: 5333-5344.
    • (2011) J Immunol , vol.186 , pp. 5333-5344
    • Gieras, A.1    Cejka, P.2    Blatt, K.3    Focke-Tejkl, M.4    Linhart, B.5
  • 33
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Sundberg EJ, Mariuzza RA, (2002) Molecular recognition in antibody-antigen complexes. Adv Protein Chem 61: 119-160.
    • (2002) Adv Protein Chem , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 34
    • 79959973530 scopus 로고    scopus 로고
    • Epitope mapping and structural analysis of the anti-Der p 1 monoclonal antibody: insight into therapeutic potential
    • Dai YC, Chuang WJ, Chua KY, Shieh CC, Wang JY, (2011) Epitope mapping and structural analysis of the anti-Der p 1 monoclonal antibody: insight into therapeutic potential. J Mol Med (Berl) 89: 701-712.
    • (2011) J Mol Med (Berl) , vol.89 , pp. 701-712
    • Dai, Y.C.1    Chuang, W.J.2    Chua, K.Y.3    Shieh, C.C.4    Wang, J.Y.5
  • 35
    • 0141958643 scopus 로고    scopus 로고
    • Renaissance of the blocking antibody concept in type I allergy
    • Flicker S, Valenta R, (2003) Renaissance of the blocking antibody concept in type I allergy. Int Arch Allergy Immunol 132: 13-24.
    • (2003) Int Arch Allergy Immunol , vol.132 , pp. 13-24
    • Flicker, S.1    Valenta, R.2


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