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Volumn 89, Issue 2, 2011, Pages 225-230

Homology modeling and monoclonal antibody binding of the der f 7 dust mite allergen

Author keywords

BPI protein; Der f 7; Der p 7; epitope; modeling structure; odorant binding protein

Indexed keywords

BACTERICIDAL PERMEABILITY INCREASING PROTEIN; HOUSE DUST ALLERGEN; IMMUNOGLOBULIN E; MONOCLONAL ANTIBODY;

EID: 79951942316     PISSN: 08189641     EISSN: 14401711     Source Type: Journal    
DOI: 10.1038/icb.2010.77     Document Type: Article
Times cited : (16)

References (43)
  • 3
    • 42549101463 scopus 로고    scopus 로고
    • Characterization of der p 21, a new important allergen derived from the gut of house dust mites
    • Weghofer M, Dall'Antonia Y, Grote M, Stocklinger A, Kneidinger M, Balic N et al. Characterization of Der p 21, a new important allergen derived from the gut of house dust mites. Allergy 2008; 63: 758-767.
    • (2008) Allergy , vol.63 , pp. 758-767
    • Weghofer, M.1    Dall'Antonia, Y.2    Grote, M.3    Stocklinger, A.4    Kneidinger, M.5    Balic, N.6
  • 4
    • 33644843658 scopus 로고    scopus 로고
    • Comparison of purified Dermatophagoides pteronyssinus allergens and extract by two-dimensional immunoblotting and quantitative immunoglobulin E inhibitions
    • Weghofer M, Thomas WR, Pittner G, Horak F, Valenta R, Vrtala S. Comparison of purified Dermatophagoides pteronyssinus allergens and extract by two-dimensional immunoblotting and quantitative immunoglobulin E inhibitions. Clin Exp Allergy 2005; 35: 1384-1391.
    • (2005) Clin Exp Allergy , vol.35 , pp. 1384-1391
    • Weghofer, M.1    Thomas, W.R.2    Pittner, G.3    Horak, F.4    Valenta, R.5    Vrtala, S.6
  • 7
    • 53149097005 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structure and IgE epitopes of Blo t 5, a major dust mite allergen
    • Chan SL, Ong TC, Gao YF, Tiong YS, Wang de Y, Chew FT et al. Nuclear magnetic resonance structure and IgE epitopes of Blo t 5, a major dust mite allergen. J Immunol 2008; 181: 2586-2596.
    • (2008) J Immunol , vol.181 , pp. 2586-2596
    • Chan, S.L.1    Ong, T.C.2    Gao, Y.F.3    Tiong, Y.S.4    De Wang, Y.5    Chew, F.T.6
  • 8
    • 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, Chua KY et al. Roles of structure and structural dynamics in the antibody recognition of the allergen proteins: an NMR study on Blomia tropicalis major allergen. Structure 2008; 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    Chua, K.Y.6
  • 9
    • 0027141028 scopus 로고
    • Molecular cloning of a house dust mite allergen with common antibody binding specificities with multiple components in mite extracts
    • DOI 10.1111/j.1365-2222.1993.tb00278.x
    • Shen HD, Chua KY, Lin KL, Hsieh KH, Thomas WR. Molecular cloning of a house dust mite allergen with common antibody binding specificities with multiple components in mite extracts. Clin Exp Allergy 1993; 23: 934-940. (Pubitemid 24002187)
    • (1993) Clinical and Experimental Allergy , vol.23 , Issue.11 , pp. 934-940
    • Shen, H.-D.1    Chua, K.-Y.2    Lin, K.-L.3    Hsieh, K.-H.4    Thomas, W.R.5
  • 10
    • 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. Molecular cloning and immunological characterization of the house dust mite allergen Der f 7. Clin Exp Allergy 1995; 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
  • 11
    • 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. Characterization of the house dust mite allergen Der p 7 by monoclonal antibodies. Clin Exp Allergy 1995; 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
  • 14
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993; 234: 779-815. (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 15
    • 0030760314 scopus 로고    scopus 로고
    • Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution
    • Beamer LJ, Carroll SF, Eisenberg D. Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. Science 1997; 276: 1861-1864.
    • (1997) Science , vol.276 , pp. 1861-1864
    • Beamer, L.J.1    Carroll, S.F.2    Eisenberg, D.3
  • 16
    • 0032007337 scopus 로고    scopus 로고
    • Role of the bactericidal/permeability-increasing protein in host defence
    • DOI 10.1016/S0952-7915(98)80030-7
    • Elsbach P, Weiss J. Role of the bactericidal/permeability-increasing protein in host defense. Curr Opin Immunol 1998; 10: 45-49. (Pubitemid 28112078)
    • (1998) Current Opinion in Immunology , vol.10 , Issue.1 , pp. 45-49
    • Elsbach, P.1    Weiss, J.2
  • 17
    • 0023525873 scopus 로고
    • 2-terminal fragment carries all the antibacterial activities of the human neutrophil 60-kDa bactericidal/permeability-increasing protein
    • Ooi CE, Weiss J, Elsbach P, Frangione B, Mannion B. A 25-kDa NH2-terminal fragment carries all the antibacterial activities of the human neutrophil 60-kDa bactericidal/permeability-increasing protein. J Biol Chem 1987; 262: 14891-14894. (Pubitemid 17160164)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.31 , pp. 14891-14894
    • Ooi, C.E.1    Weiss, J.2    Elsbach, P.3    Frangione, B.4    Mannion, B.5
  • 18
    • 0025883775 scopus 로고
    • Endotoxin-neutralizing properties of the 25kD N-terminal fragment and a newly isolated 30kD C-terminal fragment of the 55-60kD bactericidal/ permeability-increasing protein of human neutrophils
    • Ooi CE, Weiss J, Doerfler ME, Elsbach P. Endotoxin-neutralizing properties of the 25kD N-terminal fragment and a newly isolated 30kD C-terminal fragment of the 55-60kD bactericidal/permeability-increasing protein of human neutrophils. J Exp Med 1991; 174: 649-655.
    • (1991) J Exp Med , vol.174 , pp. 649-655
    • Ooi, C.E.1    Weiss, J.2    Doerfler, M.E.3    Elsbach, P.4
  • 19
    • 0030885521 scopus 로고    scopus 로고
    • An opsonic function of the neutrophil bactericidal/permeability- increasing protein depends on both its N- and C-terminal domains
    • Iovine NM, Elsbach P, Weiss J. An opsonic function of the neutrophil bactericidal/permeability-increasing protein depends on both its N- and C-terminal domains. Proc Natl Acad Sci USA 1997; 94: 10973-10978.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10973-10978
    • Iovine, N.M.1    Elsbach, P.2    Weiss, J.3
  • 20
    • 0029054796 scopus 로고
    • Plasma lipid transfer proteins
    • Tall A. Plasma lipid transfer proteins. Annu Rev Biochem 1995; 64: 235-257.
    • (1995) Annu Rev Biochem , vol.64 , pp. 235-257
    • Tall, A.1
  • 21
    • 53849117421 scopus 로고    scopus 로고
    • Bactericidal/permeability-increasing protein (BPI) and BPI homologs at mucosal sites
    • Canny G, Levy O. Bactericidal/permeability-increasing protein (BPI) and BPI homologs at mucosal sites. Trends Immunol 2008; 29: 541-547.
    • (2008) Trends Immunol , vol.29 , pp. 541-547
    • Canny, G.1    Levy, O.2
  • 22
    • 0031564630 scopus 로고    scopus 로고
    • A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence
    • DOI 10.1006/jmbi.1997.0924
    • Rice DW, Eisenberg D. A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence. J Mol Biol 1997; 267: 1026-1038. (Pubitemid 27192670)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.4 , pp. 1026-1038
    • Rice, D.W.1    Eisenberg, D.2
  • 23
    • 40649091053 scopus 로고    scopus 로고
    • Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins
    • Kolodziejczyk R, Bujacz G, Jakob M, Ozyhar A, Jaskolski M, Kochman M. Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins. J Mol Biol 2008; 377: 870-881.
    • (2008) J Mol Biol , vol.377 , pp. 870-881
    • Kolodziejczyk, R.1    Bujacz, G.2    Jakob, M.3    Ozyhar, A.4    Jaskolski, M.5    Kochman, M.6
  • 24
    • 69249222581 scopus 로고    scopus 로고
    • Characterisation and expression of SPLUNC2, the human orthologue of rodent parotid secretory protein
    • Bingle L, Barnes FA, Lunn H, Musa M, Webster S, Douglas CW et al. Characterisation and expression of SPLUNC2, the human orthologue of rodent parotid secretory protein. Histochem Cell Biol 2009; 132: 339-349.
    • (2009) Histochem Cell Biol , vol.132 , pp. 339-349
    • Bingle, L.1    Barnes, F.A.2    Lunn, H.3    Musa, M.4    Webster, S.5    Douglas, C.W.6
  • 26
    • 59049100417 scopus 로고    scopus 로고
    • Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein
    • Trompette A, Divanovic S, Visintin A, Blanchard C, Hegde RS, Madan R et al. Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein. Nature 2009; 457: 585-588.
    • (2009) Nature , vol.457 , pp. 585-588
    • Trompette, A.1    Divanovic, S.2    Visintin, A.3    Blanchard, C.4    Hegde, R.S.5    Madan, R.6
  • 27
    • 11144293555 scopus 로고    scopus 로고
    • Molecular and structural analysis of IgE-binding epitopes of Pen ch 13, an alkaline serine protease major allergen from Penicillium chrysogenum
    • Lai HY, Tam MF, Chou H, Lee SS, Tai HY, Shen HD. Molecular and structural analysis of IgE-binding epitopes of Pen ch 13, an alkaline serine protease major allergen from Penicillium chrysogenum. Clin Exp Allergy 2004; 34: 1926-1933.
    • (2004) Clin Exp Allergy , vol.34 , pp. 1926-1933
    • Lai, H.Y.1    Tam, M.F.2    Chou, H.3    Lee, S.S.4    Tai, H.Y.5    Shen, H.D.6
  • 29
    • 59349114360 scopus 로고    scopus 로고
    • Crystal structures of mite allergens der f 1 and der p 1 reveal differences in surface-exposed residues that may influence antibody binding
    • Chruszcz M, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W et al. Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding. J Mol Biol 2009; 386: 520-530.
    • (2009) J Mol Biol , vol.386 , pp. 520-530
    • Chruszcz, M.1    Chapman, M.D.2    Vailes, L.D.3    Stura, E.A.4    Saint-Remy, J.M.5    Minor, W.6
  • 30
    • 33744491534 scopus 로고    scopus 로고
    • Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: Structural analysis of an allergenic hyaluronidase from wasp venom
    • Skov LK, Seppälä U, Coen JJ, Crickmore N, King TP, Monsalve R et al. Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural analysis of an allergenic hyaluronidase from wasp venom. Acta Crystallogr D Biol Crystallogr 2006; 62: 595-604.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 595-604
    • Skov, L.K.1    Seppälä, U.2    Coen, J.J.3    Crickmore, N.4    King, T.P.5    Monsalve, R.6
  • 31
    • 0035937834 scopus 로고    scopus 로고
    • Hydrogen exchange nuclear magnetic resonance spectroscopy mapping of antibody epitopes on the house dust mite allergen der p 2
    • Mueller GA, Smith AM, Chapman MD, Rule GS, Benjamin DC. Hydrogen exchange nuclear magnetic resonance spectroscopy mapping of antibody epitopes on the house dust mite allergen Der p 2. J Biol Chem 2001; 276: 9359-9365.
    • (2001) J Biol Chem , vol.276 , pp. 9359-9365
    • Mueller, G.A.1    Smith, A.M.2    Chapman, M.D.3    Rule, G.S.4    Benjamin, D.C.5
  • 32
    • 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, Spangfort MD et al. 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 2000; 165: 331-338. (Pubitemid 30429524)
    • (2000) Journal of Immunology , vol.165 , Issue.1 , pp. 331-338
    • Mirza, O.1    Henriksen, A.2    Ipsen, H.3    Larsen, J.N.4    Wissenbach, M.5    Spangfort, M.D.6    Gajhede, M.7
  • 33
    • 33646941045 scopus 로고    scopus 로고
    • Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1: Importance for allergenic activity
    • Flicker S, Steinberger P, Ball T, Krauth MT, Verdino P, Valent P et al. Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1: importance for allergenic activity. J Allergy Clin Immunol 2006; 117: 1336-1343.
    • (2006) J Allergy Clin Immunol , vol.117 , pp. 1336-1343
    • Flicker, S.1    Steinberger, P.2    Ball, T.3    Krauth, M.T.4    Verdino, P.5    Valent, P.6
  • 34
    • 68949157033 scopus 로고    scopus 로고
    • Immunochemical characterisation of structure and allergenicity of peanut 2S albumins using different formats of immunoassays
    • Bernard H, Drumare MF, Guillon B, Paty E, Scheinmann P, Wal JM. Immunochemical characterisation of structure and allergenicity of peanut 2S albumins using different formats of immunoassays. Anal Bioanal Chem 2009; 395: 139-146.
    • (2009) Anal Bioanal Chem , vol.395 , pp. 139-146
    • Bernard, H.1    Drumare, M.F.2    Guillon, B.3    Paty, E.4    Scheinmann, P.5    Wal, J.M.6
  • 35
    • 0021238906 scopus 로고
    • Antigenic regions defined by monoclonal antibodies correspond to structural domains of avian lysozyme
    • Smith-Gill SJ, Lavoie TB, Mainhart CR. Antigenic regions defined by monoclonal antibodies correspond to structural domains of avian lysozyme. J Immunol 1984; 133: 384-393. (Pubitemid 14082063)
    • (1984) Journal of Immunology , vol.133 , Issue.1 , pp. 384-393
    • Smith-Gill, S.J.1    Lavoie, T.B.2    Mainhart, C.R.3
  • 36
    • 0035958621 scopus 로고    scopus 로고
    • A novel grass pollen allergen mimotope identified by phage display peptide library inhibits allergen-human IgE antibody interaction
    • DOI 10.1016/S0014-5793(01)02661-8, PII S0014579301026618
    • Suphioglu C, Schappi G, Kenrick J, Levy D, Davies JM, O'Hehir RE. A novel grass pollen allergen mimotope identified by phage display peptide library inhibits allergen-human IgE antibody interaction. FEBS Lett 2001; 502: 46-52. (Pubitemid 32722058)
    • (2001) FEBS Letters , vol.502 , Issue.1-2 , pp. 46-52
    • Suphioglu, C.1    Schappi, G.2    Kenrick, J.3    Levy, D.4    Davies, J.M.5    O'Hehir, R.E.6
  • 38
    • 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, Wunschmann S, Kepley CL et al. Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody. J Biol Chem 2008; 283: 22806-22814.
    • (2008) J Biol Chem , vol.283 , pp. 22806-22814
    • Li, M.1    Gustchina, A.2    Alexandratos, J.3    Wlodawer, A.4    Wunschmann, S.5    Kepley, C.L.6
  • 40
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley LA, Sternberg MJ. Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 2009; 4: 363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 42
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: 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
  • 43
    • 0036495004 scopus 로고    scopus 로고
    • Getting the most from PSI-BLAST
    • DOI 10.1016/S0968-0004(01)02039-4, PII S0968000401020394
    • Jones DT, Swindells MB. Getting the most from psi-BLAST. Trends Biochem Sci 2002; 27: 161-164. (Pubitemid 34219327)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.3 , pp. 161-164
    • Jones, D.T.1    Swindells, M.B.2


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