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Volumn 44, Issue 10, 2007, Pages 2781-2785

Major mountain cedar allergen, Jun a 1, contains conformational as well as linear IgE epitopes

Author keywords

Allergen structure; Cedar pollen hypersensitivity; Conformational epitopes; Cry j 1; IgE epitope; Jun a 1; Juniperus ashei; Mountain cedar; Protein denaturation

Indexed keywords

GUANIDINE; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E ANTIBODY; JUN A 1; POLLEN ANTIGEN; UNCLASSIFIED DRUG;

EID: 33846901166     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2005.12.001     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 13544259023 scopus 로고    scopus 로고
    • Crystal structure of Jun a 1, the major cedar pollen allergen from Juniperus ashei, reveals parallel beta-helical core
    • Czerwinski E.W., Midoro-Horiuti T., White M.A., Brooks E.G., and Goldblum R.M. Crystal structure of Jun a 1, the major cedar pollen allergen from Juniperus ashei, reveals parallel beta-helical core. J. Biol. Chem. 280 (2005) 3740-3746
    • (2005) J. Biol. Chem. , vol.280 , pp. 3740-3746
    • Czerwinski, E.W.1    Midoro-Horiuti, T.2    White, M.A.3    Brooks, E.G.4    Goldblum, R.M.5
  • 4
    • 0030443234 scopus 로고    scopus 로고
    • Molecular characterization of Bip 1, a monoclonal antibody that modulates IgE binding to birch pollen allergen, Bet v 1
    • Laffer S., Vangelista L., Steinberger P., Kraft D., Pastore A., and Valenta R. Molecular characterization of Bip 1, a monoclonal antibody that modulates IgE binding to birch pollen allergen, Bet v 1. J. Immunol. 157 (1996) 4953-4962
    • (1996) J. Immunol. , vol.157 , pp. 4953-4962
    • Laffer, S.1    Vangelista, L.2    Steinberger, P.3    Kraft, D.4    Pastore, A.5    Valenta, R.6
  • 5
    • 0037326488 scopus 로고    scopus 로고
    • Direct costs of allergic rhinitis in the United States: estimates from the 1996 Medical Expenditure Panel Survey
    • Law A.W., Reed S.D., Sundy J.S., and Schulman K.A. Direct costs of allergic rhinitis in the United States: estimates from the 1996 Medical Expenditure Panel Survey. J. Allergy Clin. Immunol. 111 (2003) 296-300
    • (2003) J. Allergy Clin. Immunol. , vol.111 , pp. 296-300
    • Law, A.W.1    Reed, S.D.2    Sundy, J.S.3    Schulman, K.A.4
  • 6
    • 0025117762 scopus 로고
    • Conformational stability of B cell epitopes on group I and group II Dermatophagoides spp. allergens. Effect of thermal and chemical denaturation on the binding of murine IgG and human IgE antibodies
    • Lombardero M., Heymann P.W., Platts-Mills T.A., Fox J.W., and Chapman M.D. Conformational stability of B cell epitopes on group I and group II Dermatophagoides spp. allergens. Effect of thermal and chemical denaturation on the binding of murine IgG and human IgE antibodies. J. Immunol. 144 (1990) 1353-1360
    • (1990) J. Immunol. , vol.144 , pp. 1353-1360
    • Lombardero, M.1    Heymann, P.W.2    Platts-Mills, T.A.3    Fox, J.W.4    Chapman, M.D.5
  • 7
    • 0004797905 scopus 로고
    • Evaluation of allergenicity of the extract of Japanese juniper pollen reacting to sera from asthmatic children-by the methods of enzyme-linked immunosorbent assay and immunoblotting
    • Midoro-Horiuti T. Evaluation of allergenicity of the extract of Japanese juniper pollen reacting to sera from asthmatic children-by the methods of enzyme-linked immunosorbent assay and immunoblotting. Jpn. J. Allergol. 41 (1992) 1459-1465
    • (1992) Jpn. J. Allergol. , vol.41 , pp. 1459-1465
    • Midoro-Horiuti, T.1
  • 8
    • 0032842409 scopus 로고    scopus 로고
    • Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1
    • Midoro-Horiuti T., Goldblum R.M., Kurosky A., Goetz D.W., and Brooks E.G. Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1. J. Allergy Clin. Immunol. 104 (1999) 608-612
    • (1999) J. Allergy Clin. Immunol. , vol.104 , pp. 608-612
    • Midoro-Horiuti, T.1    Goldblum, R.M.2    Kurosky, A.3    Goetz, D.W.4    Brooks, E.G.5
  • 10
    • 0034651647 scopus 로고    scopus 로고
    • Variable expression of pathogenesis-related protein allergen in mountain cedar (Juniperus ashei) pollen
    • Midoro-Horiuti T., Goldblum R.M., Kurosky A., Wood T.G., and Brooks E.G. Variable expression of pathogenesis-related protein allergen in mountain cedar (Juniperus ashei) pollen. J. Immunol. 164 (2000) 2188-2192
    • (2000) J. Immunol. , vol.164 , pp. 2188-2192
    • Midoro-Horiuti, T.1    Goldblum, R.M.2    Kurosky, A.3    Wood, T.G.4    Brooks, E.G.5
  • 13
    • 0037470521 scopus 로고    scopus 로고
    • Reduction of antigenicity and allergenicity of genetically modified egg white allergen, ovomucoid third domain
    • Mine Y., Sasaki E., and Zhang J.W. Reduction of antigenicity and allergenicity of genetically modified egg white allergen, ovomucoid third domain. Biochem. Biophys. Res. Commun. 302 (2003) 133-137
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 133-137
    • Mine, Y.1    Sasaki, E.2    Zhang, J.W.3
  • 14
    • 0344393658 scopus 로고    scopus 로고
    • Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure
    • Neudecker P., Lehmann K., Nerkamp J., Haase T., Wangorsch A., Fotisch K., Hoffmann S., Rosch P., Vieths S., and Scheurer S. Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure. Biochem. J. 376 (2003) 97-107
    • (2003) Biochem. J. , vol.376 , pp. 97-107
    • Neudecker, P.1    Lehmann, K.2    Nerkamp, J.3    Haase, T.4    Wangorsch, A.5    Fotisch, K.6    Hoffmann, S.7    Rosch, P.8    Vieths, S.9    Scheurer, S.10
  • 15
    • 0031692206 scopus 로고    scopus 로고
    • Analysis of the three-dimensional antigenic structure of giant ragweed allergen, Amb t 5
    • Rafnar T., Brummet M.E., Bassolino-Klimas D., Metzler W.J., and Marsh D.G. Analysis of the three-dimensional antigenic structure of giant ragweed allergen, Amb t 5. Mol. Immunol. 35 (1998) 459-467
    • (1998) Mol. Immunol. , vol.35 , pp. 459-467
    • Rafnar, T.1    Brummet, M.E.2    Bassolino-Klimas, D.3    Metzler, W.J.4    Marsh, D.G.5
  • 17
    • 3042798442 scopus 로고    scopus 로고
    • The increased prevalence of allergy and the hygiene hypothesis: missing immune deviation, reduced immune suppression, or both?
    • Romagnani S. The increased prevalence of allergy and the hygiene hypothesis: missing immune deviation, reduced immune suppression, or both?. Immunology 112 (2004) 352-363
    • (2004) Immunology , vol.112 , pp. 352-363
    • Romagnani, S.1
  • 18
    • 0029058322 scopus 로고
    • Basic and practical aspects of recombinant allergens
    • Scheiner O., and Kraft D. Basic and practical aspects of recombinant allergens. Allergy 50 (1995) 384-391
    • (1995) Allergy , vol.50 , pp. 384-391
    • Scheiner, O.1    Kraft, D.2
  • 19
    • 0035079256 scopus 로고    scopus 로고
    • Discontinuous IgE-binding epitopes contain multiple continuous epitope regions: results of an epitope mapping on recombinant Hol l 5, a major allergen from velvet grass pollen
    • Schramm G., Bufe A., Petersen A., Haas H., Merget R., Schlaak M., and Becker W.M. Discontinuous IgE-binding epitopes contain multiple continuous epitope regions: results of an epitope mapping on recombinant Hol l 5, a major allergen from velvet grass pollen. Clin. Exp. Allergy 31 (2001) 331-341
    • (2001) Clin. Exp. Allergy , vol.31 , pp. 331-341
    • Schramm, G.1    Bufe, A.2    Petersen, A.3    Haas, H.4    Merget, R.5    Schlaak, M.6    Becker, W.M.7
  • 20
    • 0029887345 scopus 로고    scopus 로고
    • Identification and characterization of the major allergens of velvet grass (Holcus lanatus), Hol l 1 and Hol l 5
    • Schramm G., Petersen A., Bufe A., Schlaak M., and Becker W.M. Identification and characterization of the major allergens of velvet grass (Holcus lanatus), Hol l 1 and Hol l 5. Int. Arch. Allergy Immunol. 110 (1996) 354-363
    • (1996) Int. Arch. Allergy Immunol. , vol.110 , pp. 354-363
    • Schramm, G.1    Petersen, A.2    Bufe, A.3    Schlaak, M.4    Becker, W.M.5
  • 22
    • 0029999352 scopus 로고    scopus 로고
    • Reduction in IgE binding to allergen variants generated by site-directed mutagenesis: contribution of disulfide bonds to the antigenic structure of the major house dust mite allergen Der p 2
    • Smith A.M., and Chapman M.D. Reduction in IgE binding to allergen variants generated by site-directed mutagenesis: contribution of disulfide bonds to the antigenic structure of the major house dust mite allergen Der p 2. Mol. Immunol. 33 (1996) 399-405
    • (1996) Mol. Immunol. , vol.33 , pp. 399-405
    • Smith, A.M.1    Chapman, M.D.2
  • 26
    • 0033571728 scopus 로고    scopus 로고
    • Molecular, immunological, and structural characterization of Phl p 6, a major allergen and P-particle-associated protein from Timothy grass (Phleum pratense) pollen
    • Vrtala S., Fischer S., Grote M., Vangelista L., Pastore A., Sperr W.R., Valent P., Reichelt R., Kraft D., and Valenta R. Molecular, immunological, and structural characterization of Phl p 6, a major allergen and P-particle-associated protein from Timothy grass (Phleum pratense) pollen. J. Immunol. 163 (1999) 5489-5496
    • (1999) J. Immunol. , vol.163 , pp. 5489-5496
    • Vrtala, S.1    Fischer, S.2    Grote, M.3    Vangelista, L.4    Pastore, A.5    Sperr, W.R.6    Valent, P.7    Reichelt, R.8    Kraft, D.9    Valenta, R.10
  • 27
    • 0030937231 scopus 로고    scopus 로고
    • Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy
    • Vrtala S., Hirtenlehner K., Vangelista L., Pastore A., Eichler H.G., Sperr W.R., Valent P., Ebner C., Kraft D., and Valenta R. Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy. J. Clin. Invest. 99 (1997) 1673-1681
    • (1997) J. Clin. Invest. , vol.99 , pp. 1673-1681
    • Vrtala, S.1    Hirtenlehner, K.2    Vangelista, L.3    Pastore, A.4    Eichler, H.G.5    Sperr, W.R.6    Valent, P.7    Ebner, C.8    Kraft, D.9    Valenta, R.10
  • 28
    • 0346093659 scopus 로고    scopus 로고
    • Effect of cysteine mutagenesis on human IgE reactivity of recombinants forms of the major rye grass pollen allergen Lol p 1
    • Weerd N.D., Bhalla P.L., and Singh M.B. Effect of cysteine mutagenesis on human IgE reactivity of recombinants forms of the major rye grass pollen allergen Lol p 1. Allergol. Int. 52 (2003) 183-190
    • (2003) Allergol. Int. , vol.52 , pp. 183-190
    • Weerd, N.D.1    Bhalla, P.L.2    Singh, M.B.3
  • 29
    • 12744253736 scopus 로고    scopus 로고
    • Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen
    • Wiche R., Gubesch M., Konig H., Fotisch K., Hoffmann A., Wangorsch A., Scheurer S., and Vieths S. Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen. Biochem. J. 385 (2005) 319-327
    • (2005) Biochem. J. , vol.385 , pp. 319-327
    • Wiche, R.1    Gubesch, M.2    Konig, H.3    Fotisch, K.4    Hoffmann, A.5    Wangorsch, A.6    Scheurer, S.7    Vieths, S.8
  • 30
    • 0033648607 scopus 로고    scopus 로고
    • Structural thermodynamics of a random coil protein in guanidine hydrochloride
    • Yang M., Ferreon A.C., and Bolen D.W. Structural thermodynamics of a random coil protein in guanidine hydrochloride. Proteins Suppl. 4 (2000) 44-49
    • (2000) Proteins Suppl. , vol.4 , pp. 44-49
    • Yang, M.1    Ferreon, A.C.2    Bolen, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.