메뉴 건너뛰기




Volumn 137, Issue 5, 2016, Pages 1557-1565

IgE epitope proximity determines immune complex shape and effector cell activation capacity

Author keywords

allergen; Allergy; effector cells; IgE epitope; immune complex

Indexed keywords

EPITOPE; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E ANTIBODY; RECOMBINANT ALLERGEN; SCAFFOLD PROTEIN; ALLERGEN; ANTIGEN ANTIBODY COMPLEX; MYOGLOBIN; PHLPI PROTEIN, PHLEUM PRATENSE; PLANT PROTEIN; RECOMBINANT PROTEIN;

EID: 84960874036     PISSN: 00916749     EISSN: 10976825     Source Type: Journal    
DOI: 10.1016/j.jaci.2015.08.055     Document Type: Article
Times cited : (43)

References (40)
  • 1
    • 77953760056 scopus 로고    scopus 로고
    • Antibody-mediated modulation of immune responses
    • F. Nimmerjahn, and J.V. Ravetch Antibody-mediated modulation of immune responses Immunol Rev 236 2010 265 275
    • (2010) Immunol Rev , vol.236 , pp. 265-275
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 2
    • 0028816834 scopus 로고
    • Prevalence of atopy and pollinosis in the adult population of Switzerland (SAPALDIA study). Swiss Study on Air Pollution and Lung Diseases in Adults
    • B. Wüthrich, C. Schindler, P. Leuenberger, and U. Ackermann-Liebrich Prevalence of atopy and pollinosis in the adult population of Switzerland (SAPALDIA study). Swiss Study on Air Pollution and Lung Diseases in Adults Int Arch Allergy Immunol 106 1995 149 156
    • (1995) Int Arch Allergy Immunol , vol.106 , pp. 149-156
    • Wüthrich, B.1    Schindler, C.2    Leuenberger, P.3    Ackermann-Liebrich, U.4
  • 3
    • 84860655039 scopus 로고    scopus 로고
    • Innate and adaptive immune responses in asthma
    • S.T. Holgate Innate and adaptive immune responses in asthma Nat Med 18 2012 673 683
    • (2012) Nat Med , vol.18 , pp. 673-683
    • Holgate, S.T.1
  • 4
    • 1942499447 scopus 로고    scopus 로고
    • Time to draw breath: Asthma-susceptibility genes are identified
    • M. Wills-Karp, and S.L. Ewart Time to draw breath: Asthma-susceptibility genes are identified Nat Rev Genet 5 2004 376 387
    • (2004) Nat Rev Genet , vol.5 , pp. 376-387
    • Wills-Karp, M.1    Ewart, S.L.2
  • 5
    • 33846581108 scopus 로고    scopus 로고
    • Role of mast cells in allergic and non-allergic immune responses: Comparison of human and murine data
    • S.C. Bischoff Role of mast cells in allergic and non-allergic immune responses: comparison of human and murine data Nat Rev Immunol 7 2007 93 104
    • (2007) Nat Rev Immunol , vol.7 , pp. 93-104
    • Bischoff, S.C.1
  • 6
    • 0035546067 scopus 로고    scopus 로고
    • Eosinophils, allergy and parasites
    • D. Dombrowicz, and M. Capron Eosinophils, allergy and parasites Curr Opin Immunol 13 2001 716 720
    • (2001) Curr Opin Immunol , vol.13 , pp. 716-720
    • Dombrowicz, D.1    Capron, M.2
  • 7
    • 40049101678 scopus 로고    scopus 로고
    • IgE in allergy and asthma today
    • H.J. Gould, and B.J. Sutton IgE in allergy and asthma today Nat Rev Immunol 8 2008 205 217
    • (2008) Nat Rev Immunol , vol.8 , pp. 205-217
    • Gould, H.J.1    Sutton, B.J.2
  • 8
    • 84860668874 scopus 로고    scopus 로고
    • IgE and mast cells in allergic disease
    • S.J. Galli, and M. Tsai IgE and mast cells in allergic disease Nat Med 18 2012 693 704
    • (2012) Nat Med , vol.18 , pp. 693-704
    • Galli, S.J.1    Tsai, M.2
  • 9
    • 85014171655 scopus 로고
    • Experiments on anaphylaxis to azoproteins
    • K. Landsteiner Experiments on anaphylaxis to azoproteins J Exp Med 39 1924 631 637
    • (1924) J Exp Med , vol.39 , pp. 631-637
    • Landsteiner, K.1
  • 10
    • 0000452622 scopus 로고
    • Studies on the mechanisms of hypersensitivity phenomena, IX: Histamine release from human leukocytes by ragweed pollen antigen
    • L.M. Lichtenstein, and A.G. Osler Studies on the mechanisms of hypersensitivity phenomena, IX: histamine release from human leukocytes by ragweed pollen antigen J Exp Med 120 1964 507 530
    • (1964) J Exp Med , vol.120 , pp. 507-530
    • Lichtenstein, L.M.1    Osler, A.G.2
  • 11
    • 0000457253 scopus 로고
    • Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation
    • D.M. Segal, J.D. Taurog, and H. Metzger Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation Proc Natl Acad Sci U S A 74 1977 2993 2997
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 2993-2997
    • Segal, D.M.1    Taurog, J.D.2    Metzger, H.3
  • 12
    • 0018908824 scopus 로고
    • Larger oligomers of IgE are more effective than dimers in stimulating rat basophilic leukemia cells
    • C. Fewtrell, and H. Metzger Larger oligomers of IgE are more effective than dimers in stimulating rat basophilic leukemia cells J Immunol 125 1980 701 710
    • (1980) J Immunol , vol.125 , pp. 701-710
    • Fewtrell, C.1    Metzger, H.2
  • 13
    • 0019850122 scopus 로고
    • Qualitative characteristics of histamine release from human basophils by covalently cross-linked IgE
    • A. Kagey-Sobotka, M. Dembo, B. Goldstein, H. Metzger, and L.M. Lichtenstein Qualitative characteristics of histamine release from human basophils by covalently cross-linked IgE J Immunol 127 1981 2285 2291
    • (1981) J Immunol , vol.127 , pp. 2285-2291
    • Kagey-Sobotka, A.1    Dembo, M.2    Goldstein, B.3    Metzger, H.4    Lichtenstein, L.M.5
  • 14
    • 0019792538 scopus 로고
    • IgE-mediated histamine release from human basophils: Differences between antigen E- and anti-IgE-induced secretion
    • G. Marone, A. Kagey-Sobotka, and L.M. Lichtenstein IgE-mediated histamine release from human basophils: differences between antigen E- and anti-IgE-induced secretion Int Arch Allergy Appl Immunol 65 1981 339 348
    • (1981) Int Arch Allergy Appl Immunol , vol.65 , pp. 339-348
    • Marone, G.1    Kagey-Sobotka, A.2    Lichtenstein, L.M.3
  • 17
    • 0026567279 scopus 로고
    • IgE binding structures of the major house dust mite allergen der p I
    • W.K. Greene, and W.R. Thomas IgE binding structures of the major house dust mite allergen Der p I Mol Immunol 29 1992 257 262
    • (1992) Mol Immunol , vol.29 , pp. 257-262
    • Greene, W.K.1    Thomas, W.R.2
  • 18
    • 0027939421 scopus 로고
    • Isolation of an immunodominant IgE hapten from an epitope expression cDNA library: Dissection of the allergic effector reaction
    • T. Ball, S. Vrtala, W.R. Sperr, P. Valent, M. Susani, D. Kraft, and et al. Isolation of an immunodominant IgE hapten from an epitope expression cDNA library: dissection of the allergic effector reaction J Biol Chem 269 1994 28323 28328
    • (1994) J Biol Chem , vol.269 , pp. 28323-28328
    • Ball, T.1    Vrtala, S.2    Sperr, W.R.3    Valent, P.4    Susani, M.5    Kraft, D.6
  • 19
    • 0031568307 scopus 로고    scopus 로고
    • The molecular basis for allergen cross-reactivity: Crystal structure and IgE-epitope mapping of birch pollen profilin
    • A.A. Fedorov, T. Ball, N.M. Mahoney, R. Valenta, and S.C. Almo The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilin Structure 5 1997 33 45
    • (1997) Structure , vol.5 , pp. 33-45
    • Fedorov, A.A.1    Ball, T.2    Mahoney, N.M.3    Valenta, R.4    Almo, S.C.5
  • 20
    • 0032577580 scopus 로고    scopus 로고
    • Biochemical and structural analysis of the IgE binding sites on Ara h1, an abundant and highly allergenic peanut protein
    • D.S. Shin, C.M. Compadre, S.J. Maleki, R.A. Kopper, H. Sampson, S.K. Huang, and et al. Biochemical and structural analysis of the IgE binding sites on Ara h1, an abundant and highly allergenic peanut protein J Biol Chem 273 1998 13753 13759
    • (1998) J Biol Chem , vol.273 , pp. 13753-13759
    • Shin, D.S.1    Compadre, C.M.2    Maleki, S.J.3    Kopper, R.A.4    Sampson, H.5    Huang, S.K.6
  • 21
    • 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
    • S. Flicker, P. Steinberger, T. Ball, M.T. Krauth, P. Verdino, P. Valent, and 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 117 2006 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
  • 22
    • 61449212919 scopus 로고    scopus 로고
    • High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X-ray crystallography
    • S. Padavattan, S. Flicker, T. Schirmer, C. Madritsch, S. Randow, G. Reese, and et al. High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X-ray crystallography J Immunol 182 2009 2141 2151
    • (2009) J Immunol , vol.182 , pp. 2141-2151
    • Padavattan, S.1    Flicker, S.2    Schirmer, T.3    Madritsch, C.4    Randow, S.5    Reese, G.6
  • 24
    • 84880104666 scopus 로고    scopus 로고
    • Phl p 1-specific human monoclonal IgE and design of a hypoallergenic group 1 grass pollen allergen fragment
    • M. Levin, F. Rydnert, E. Källström, L.W. Tan, P.J. Wormald, M. Lindstedt, and et al. Phl p 1-specific human monoclonal IgE and design of a hypoallergenic group 1 grass pollen allergen fragment J Immunol 191 2013 551 560
    • (2013) J Immunol , vol.191 , pp. 551-560
    • Levin, M.1    Rydnert, F.2    Källström, E.3    Tan, L.W.4    Wormald, P.J.5    Lindstedt, M.6
  • 25
    • 0035464780 scopus 로고    scopus 로고
    • Nonanaphylactic synthetic peptides derived from B cell epitopes of the major grass pollen allergen, Phl p 1, for allergy vaccination
    • M. Focke, V. Mahler, T. Ball, W.R. Sperr, Y. Majlesi, P. Valent, and et al. Nonanaphylactic synthetic peptides derived from B cell epitopes of the major grass pollen allergen, Phl p 1, for allergy vaccination FASEB J 15 2001 2042 2044
    • (2001) FASEB J , vol.15 , pp. 2042-2044
    • Focke, M.1    Mahler, V.2    Ball, T.3    Sperr, W.R.4    Majlesi, Y.5    Valent, P.6
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0025887036 scopus 로고
    • Identification of profilin as a novel pollen allergen: IgE autoreactivity in sensitized individuals
    • R. Valenta, M. Duchene, K. Pettenburger, C. Sillaber, P. Valent, P. Bettelheim, and et al. Identification of profilin as a novel pollen allergen: IgE autoreactivity in sensitized individuals Science 253 1991 557 560
    • (1991) Science , vol.253 , pp. 557-560
    • Valenta, R.1    Duchene, M.2    Pettenburger, K.3    Sillaber, C.4    Valent, P.5    Bettelheim, P.6
  • 28
    • 0030270610 scopus 로고    scopus 로고
    • Negative-stain immunoelectron-microscopic analysis of small macromolecules of immunologic significance
    • K.H. Roux Negative-stain immunoelectron-microscopic analysis of small macromolecules of immunologic significance Methods 10 1996 247 256
    • (1996) Methods , vol.10 , pp. 247-256
    • Roux, K.H.1
  • 29
    • 0015857512 scopus 로고
    • Basophilic leukaemia in the albino rat and a demonstration of the basopoietin
    • E. Eccleston, B.J. Leonard, J.S. Lowe, and H.J. Welford Basophilic leukaemia in the albino rat and a demonstration of the basopoietin Nat New Biol 244 1973 73 76
    • (1973) Nat New Biol , vol.244 , pp. 73-76
    • Eccleston, E.1    Leonard, B.J.2    Lowe, J.S.3    Welford, H.J.4
  • 31
    • 0023910427 scopus 로고
    • Horse heart metmyoglobin: A 2.8-A resolution three-dimensional structure determination
    • S.V. Evans, and G.D. Brayer Horse heart metmyoglobin: A 2.8-A resolution three-dimensional structure determination J Biol Chem 263 1988 4263 4268
    • (1988) J Biol Chem , vol.263 , pp. 4263-4268
    • Evans, S.V.1    Brayer, G.D.2
  • 32
    • 0032532015 scopus 로고    scopus 로고
    • Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry
    • K.H. Roux, L. Strelets, O.H. Brekke, I. Sandlie, and T.E. Michaelsen Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry J Immunol 161 1998 4083 4090
    • (1998) J Immunol , vol.161 , pp. 4083-4090
    • Roux, K.H.1    Strelets, L.2    Brekke, O.H.3    Sandlie, I.4    Michaelsen, T.E.5
  • 33
    • 1042286444 scopus 로고    scopus 로고
    • Do mouse models of allergic asthma mimic clinical disease?
    • M.M. Epstein Do mouse models of allergic asthma mimic clinical disease? Int Arch Allergy Immunol 133 2004 84 100
    • (2004) Int Arch Allergy Immunol , vol.133 , pp. 84-100
    • Epstein, M.M.1
  • 34
    • 0014202658 scopus 로고
    • Electron microscopy of an antibody-hapten complex
    • R.C. Valentine, and N.M. Green Electron microscopy of an antibody-hapten complex J Mol Biol 27 1967 615 617
    • (1967) J Mol Biol , vol.27 , pp. 615-617
    • Valentine, R.C.1    Green, N.M.2
  • 35
    • 0023369233 scopus 로고
    • Construction of an extended three-dimensional idiotope map by electron microscopic analysis of idiotope-anti-idiotope complexes
    • K.H. Roux, W.J. Monafo, J.M. Davie, and N.S. Greenspan Construction of an extended three-dimensional idiotope map by electron microscopic analysis of idiotope-anti-idiotope complexes Proc Natl Acad Sci U S A 84 1987 4984 4988
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 4984-4988
    • Roux, K.H.1    Monafo, W.J.2    Davie, J.M.3    Greenspan, N.S.4
  • 36
    • 0025302266 scopus 로고
    • A nanosecond fluorescence depolarization study on the segmental flexibility of receptor-bound immunoglobulin E
    • D. Holowka, T. Wensel, and B. Baird A nanosecond fluorescence depolarization study on the segmental flexibility of receptor-bound immunoglobulin E Biochemistry 29 1990 4607 4612
    • (1990) Biochemistry , vol.29 , pp. 4607-4612
    • Holowka, D.1    Wensel, T.2    Baird, B.3
  • 37
    • 0035109363 scopus 로고    scopus 로고
    • Recombinant allergen molecules: Tools to study effector cell activation
    • R. Valenta, and D. Kraft Recombinant allergen molecules: tools to study effector cell activation Immunol Rev 179 2001 119 127
    • (2001) Immunol Rev , vol.179 , pp. 119-127
    • Valenta, R.1    Kraft, D.2
  • 38
    • 84864002906 scopus 로고    scopus 로고
    • The complexity of allergic patients' IgE repertoire correlates with serum concentration of allergen-specific IgE
    • N. Willumsen, J. Holm, L.H. Christensen, P.A. Würtzen, and K. Lund The complexity of allergic patients' IgE repertoire correlates with serum concentration of allergen-specific IgE Clin Exp Allergy 42 2012 1227 1236
    • (2012) Clin Exp Allergy , vol.42 , pp. 1227-1236
    • Willumsen, N.1    Holm, J.2    Christensen, L.H.3    Würtzen, P.A.4    Lund, K.5
  • 39
    • 0015576658 scopus 로고
    • IgE antibody measurements in ragweed hay fever: Relationship to clinical severity and the results of immunotherapy
    • L.M. Lichtenstein, K. Ishizaka, P.S. Norman, A.K. Sobotka, and B.M. Hill IgE antibody measurements in ragweed hay fever: relationship to clinical severity and the results of immunotherapy J Clin Invest 52 1973 472 482
    • (1973) J Clin Invest , vol.52 , pp. 472-482
    • Lichtenstein, L.M.1    Ishizaka, K.2    Norman, P.S.3    Sobotka, A.K.4    Hill, B.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.