메뉴 건너뛰기




Volumn 105, Issue 2 II, 2000, Pages 286-291

Purification and characterization of an 18-kd allergen of birch (Betula verrucosa) pollen: Identification as a cyclophilin

Author keywords

Allergen; Birch pollen; Chromatography; Cyclophilin; Peptidyl prolyl isomerase

Indexed keywords

CYCLOPHILIN; POLLEN ANTIGEN;

EID: 0033965967     PISSN: 00916749     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0091-6749(00)90078-2     Document Type: Article
Times cited : (54)

References (38)
  • 2
    • 0028893179 scopus 로고
    • Isoforms of Bet v 1, the major birch pollen allergen, analyzed by liquid chromatography, mass spectrometry, and cDNA cloning
    • Swoboda I, Jilek A, Ferreira F, Engel E, Hoffmann-Sommergruber K, Scheiner O, et al. Isoforms of Bet v 1, the major birch pollen allergen, analyzed by liquid chromatography, mass spectrometry, and cDNA cloning. J Biol Chem 1995;270:2607-13.
    • (1995) J Biol Chem , vol.270 , pp. 2607-2613
    • Swoboda, I.1    Jilek, A.2    Ferreira, F.3    Engel, E.4    Hoffmann-Sommergruber, K.5    Scheiner, O.6
  • 3
    • 0020619604 scopus 로고
    • Isolation and immunological characterization of the major allergen of birch pollen (Betula verrucosa)
    • Ipsen H, Løwenstein H. Isolation and immunological characterization of the major allergen of birch pollen (Betula verrucosa). J Allergy Clin Immunol 1983;72:150-9.
    • (1983) J Allergy Clin Immunol , vol.72 , pp. 150-159
    • Ipsen, H.1    Løwenstein, H.2
  • 4
    • 0024443144 scopus 로고
    • The gene coding for the major birch pollen allergen BetvI, is highly homologous to a pea disease resistance response gene
    • Breiteneder H, Pettenburger K, Bito A, Valenta R, Kraft D, Rumpold H, et al. The gene coding for the major birch pollen allergen BetvI, is highly homologous to a pea disease resistance response gene. EMBO J 1989;8:1935-8.
    • (1989) EMBO J , vol.8 , pp. 1935-1938
    • Breiteneder, H.1    Pettenburger, K.2    Bito, A.3    Valenta, R.4    Kraft, D.5    Rumpold, H.6
  • 5
    • 0029028998 scopus 로고
    • Identification of allergens in fruits and vegetables: IgE cross-reactivities with the important birch pollen allergens Bet v 1 and Bet v 2 (birch profilin)
    • Ebner C, Hirschwehr R, Bauer L, Breiteneder H, Valenta R, Ebner H, et al. Identification of allergens in fruits and vegetables: IgE cross-reactivities with the important birch pollen allergens Bet v 1 and Bet v 2 (birch profilin). J Allergy Clin Immunol 1995;95:962-9.
    • (1995) J Allergy Clin Immunol , vol.95 , pp. 962-969
    • Ebner, C.1    Hirschwehr, R.2    Bauer, L.3    Breiteneder, H.4    Valenta, R.5    Ebner, H.6
  • 7
    • 0029128357 scopus 로고
    • Cloning and sequencing of Mal d 1, the major allergen from apple (Malus domestica), and its immunological relationship to Bet v 1, the major birch pollen allergen
    • Vanek-Krebitz M, Hoffmann-Sommergruber K, Laimer da Camara Machado M, Susani M, Ebner C, Kraft D, et al. Cloning and sequencing of Mal d 1, the major allergen from apple (Malus domestica), and its immunological relationship to Bet v 1, the major birch pollen allergen. Biochem Biophys Res Commun 1995;214:538-51.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 538-551
    • Vanek-Krebitz, M.1    Hoffmann-Sommergruber, K.2    Laimer Da Camara Machado, M.3    Susani, M.4    Ebner, C.5    Kraft, D.6
  • 8
    • 0029067405 scopus 로고
    • Isolation and characterization of the 18-kDa major apple allergen and comparison with the major birch pollen allergen (Bet v I)
    • Vieths S, Janek K, Aulepp H, Petersen A. Isolation and characterization of the 18-kDa major apple allergen and comparison with the major birch pollen allergen (Bet v I). Allergy 1995;50:421-30.
    • (1995) Allergy , vol.50 , pp. 421-430
    • Vieths, S.1    Janek, K.2    Aulepp, H.3    Petersen, A.4
  • 9
    • 0025887036 scopus 로고
    • Identification of profilin as a novel pollen allergen: IgE autore-activity in sensitized individuals
    • Valenta R, Duchêne M, Pettenburger K, Sillaber C, Valent P, Bettelheim P, et al. Identification of profilin as a novel pollen allergen: IgE autore-activity in sensitized individuals. Science 1991;253:557-60.
    • (1991) Science , vol.253 , pp. 557-560
    • Valenta, R.1    Duchêne, M.2    Pettenburger, K.3    Sillaber, C.4    Valent, P.5    Bettelheim, P.6
  • 10
    • 0030662265 scopus 로고    scopus 로고
    • Immunological and biological properties of Bet v 4, a novel birch pollen allergen with two EF-hand calcium-binding domains
    • Engel E, Richter K, Obermeyer G, Briza P, Kungl AJ, Simon B, et al. Immunological and biological properties of Bet v 4, a novel birch pollen allergen with two EF-hand calcium-binding domains. J Biol Chem 1997;272:28630-7.
    • (1997) J Biol Chem , vol.272 , pp. 28630-28637
    • Engel, E.1    Richter, K.2    Obermeyer, G.3    Briza, P.4    Kungl, A.J.5    Simon, B.6
  • 12
    • 0031955511 scopus 로고    scopus 로고
    • Characterization of a new IgE-binding 35-kDa protein from birch pollen with cross-reacting homologues in various plant foods
    • Vieths S, Frank E, Scheurer S, Meyer HE, Hrazdina G, Haustein D. Characterization of a new IgE-binding 35-kDa protein from birch pollen with cross-reacting homologues in various plant foods. Scand J Immunol 1998;47:263-72.
    • (1998) Scand J Immunol , vol.47 , pp. 263-272
    • Vieths, S.1    Frank, E.2    Scheurer, S.3    Meyer, H.E.4    Hrazdina, G.5    Haustein, D.6
  • 13
    • 0029013684 scopus 로고
    • Influence of the pH of the extraction medium on the composition of birch (Betula verrucosa) pollen extracts
    • Cadot P, Lejoly M, Van Hoeyveld EM, Stevens EAM. Influence of the pH of the extraction medium on the composition of birch (Betula verrucosa) pollen extracts. Allergy 1995;50:431-7.
    • (1995) Allergy , vol.50 , pp. 431-437
    • Cadot, P.1    Lejoly, M.2    Van Hoeyveld, E.M.3    Stevens, E.A.M.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0021689983 scopus 로고
    • Conformational specificity of chymotrypsin toward proline-containing substrates
    • Fischer G, Bang H, Berger E, Schellenberger A. Conformational specificity of chymotrypsin toward proline-containing substrates. Biochim Biophys Acta 1984;791:87-97.
    • (1984) Biochim Biophys Acta , vol.791 , pp. 87-97
    • Fischer, G.1    Bang, H.2    Berger, E.3    Schellenberger, A.4
  • 16
    • 0025599920 scopus 로고
    • Structure and expres sion of cytosolic cyclophilin/peptidyl-prolyl cis-trans isomerase of higher plants and production of active tomato cyclophilin in Escherichia coli
    • Gasser CS, Gunning DA, Budelier KA, Brown SM. Structure and expres sion of cytosolic cyclophilin/peptidyl-prolyl cis-trans isomerase of higher plants and production of active tomato cyclophilin in Escherichia coli. Proc Natl Acad Sci U S A 1990;87:9519-23.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 9519-9523
    • Gasser, C.S.1    Gunning, D.A.2    Budelier, K.A.3    Brown, S.M.4
  • 17
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Schreiber S. Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 1991;251:283-7.
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.1
  • 18
    • 0029816659 scopus 로고    scopus 로고
    • Cellular functions of immunophilins
    • Marks A. Cellular functions of immunophilins. Physiol Rev 1996;76:631-49.
    • (1996) Physiol Rev , vol.76 , pp. 631-649
    • Marks, A.1
  • 19
    • 0031944241 scopus 로고    scopus 로고
    • Peptidylprolyl cis-trans-isomerases from plant organelles
    • Mattoo AK. Peptidylprolyl cis-trans-isomerases from plant organelles. Methods Enzymol 1998;290:84-100.
    • (1998) Methods Enzymol , vol.290 , pp. 84-100
    • Mattoo, A.K.1
  • 20
    • 0027996970 scopus 로고
    • The nucleotide and deduced amino acid sequences of a peptidyl-prolyl cis-trans isomerase from Arabidopsis thaliana
    • Hayman GT, Miernyk JA. The nucleotide and deduced amino acid sequences of a peptidyl-prolyl cis-trans isomerase from Arabidopsis thaliana. Biochim Biophys Acta 1994;1219:536-8.
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 536-538
    • Hayman, G.T.1    Miernyk, J.A.2
  • 22
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 1989;337:476-8.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 23
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi N, Hayano T, Suzuki M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 1989;337:473-5.
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 24
    • 0026799384 scopus 로고
    • Plant organelles contain distinct peptidylprolyl cis-trans isomerases
    • Breiman A, Fawcett TW, Ghirardi ML, Mattoo AK. Plant organelles contain distinct peptidylprolyl cis-trans isomerases. J Biol Chem 1992;267:21293-6.
    • (1992) J Biol Chem , vol.267 , pp. 21293-21296
    • Breiman, A.1    Fawcett, T.W.2    Ghirardi, M.L.3    Mattoo, A.K.4
  • 25
    • 0028363956 scopus 로고
    • Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana
    • Lippuner V, Chou IT, Varian Scott S, Ettinger WF, Theg SM, Gasser CS. Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana. J Biol Chem 1994;269:7863-8.
    • (1994) J Biol Chem , vol.269 , pp. 7863-7868
    • Lippuner, V.1    Chou, I.T.2    Varian Scott, S.3    Ettinger, W.F.4    Theg, S.M.5    Gasser, C.S.6
  • 26
    • 0029919194 scopus 로고    scopus 로고
    • Purification and characterization of cytosolic and microsomal cyclophilins from maize (Zea mays)
    • Sheldon PS, Venis MA. Purification and characterization of cytosolic and microsomal cyclophilins from maize (Zea mays). Biochem J 1996;315:965-9.
    • (1996) Biochem J , vol.315 , pp. 965-969
    • Sheldon, P.S.1    Venis, M.A.2
  • 27
    • 0031456116 scopus 로고    scopus 로고
    • Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins
    • Chou IT, Gasser CS. Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins. Plant Mol Biol 1997;35:873-92.
    • (1997) Plant Mol Biol , vol.35 , pp. 873-892
    • Chou, I.T.1    Gasser, C.S.2
  • 28
    • 0028158402 scopus 로고
    • Light-regulated, tissue-specific immunophilins in a higher plant
    • Luan S, Albers MW, Schreiber SL. Light-regulated, tissue-specific immunophilins in a higher plant. Proc Natl Acad Sci U S A 1994;91:984-8.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 984-988
    • Luan, S.1    Albers, M.W.2    Schreiber, S.L.3
  • 29
    • 0026499641 scopus 로고
    • Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase
    • Freskgard P-O, Bergenhem N, Jonsson B-H, Svensson M, Carlsson U. Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science 1992;258:466-8.
    • (1992) Science , vol.258 , pp. 466-468
    • Freskgard, P.-O.1    Bergenhem, N.2    Jonsson, B.-H.3    Svensson, M.4    Carlsson, U.5
  • 30
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker EK, Colley NJ, Zuker CS. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J 1994;13:4886-95.
    • (1994) EMBO J , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 31
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin a and FKBP-FK506 complexes
    • Liu J, Farmer J, Lane W, Friedman J, Weissman I, Schreiber S. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 1991;66:807-15.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.2    Lane, W.3    Friedman, J.4    Weissman, I.5    Schreiber, S.6
  • 32
    • 0028534732 scopus 로고
    • Bean cyclophilin gene expression during plant development and stress conditions
    • Marivet J, Margis-Pinheiro M, Frendo P, Burkard G. Bean cyclophilin gene expression during plant development and stress conditions. Plant Mol Biol 1994;26:1181-9.
    • (1994) Plant Mol Biol , vol.26 , pp. 1181-1189
    • Marivet, J.1    Margis-Pinheiro, M.2    Frendo, P.3    Burkard, G.4
  • 33
    • 0040439865 scopus 로고    scopus 로고
    • Stress-induced expression of cyclophilins in proembryonic masses of Digitalis lanata does not protect against freezing/thawing stress
    • Kullertz G, Liebau A, Rucknagel P, Schierhorn A, Diettrich B, Fischer G, et al. Stress-induced expression of cyclophilins in proembryonic masses of Digitalis lanata does not protect against freezing/thawing stress. Planta 1999;208:599-605.
    • (1999) Planta , vol.208 , pp. 599-605
    • Kullertz, G.1    Liebau, A.2    Rucknagel, P.3    Schierhorn, A.4    Diettrich, B.5    Fischer, G.6
  • 35
    • 0029014156 scopus 로고
    • Identification of the allergen Psi c 2 from the basidiomycete Psilocibe cubensis as a fungal cyclophilin
    • Homer WE, Reese G, Lehrer SB. Identification of the allergen Psi c 2 from the basidiomycete Psilocibe cubensis as a fungal cyclophilin. Int Arch Allergy Immunol 1995;107:298-300.
    • (1995) Int Arch Allergy Immunol , vol.107 , pp. 298-300
    • Homer, W.E.1    Reese, G.2    Lehrer, S.B.3
  • 36
    • 0032606057 scopus 로고    scopus 로고
    • Epidemiology and molecular basis of the involvement of Aspergillus fumigatus in allergic diseases
    • Brakhage AA, Jahn B, Schmidt A. editors. Basel: Karger
    • Crameri R. Epidemiology and molecular basis of the involvement of Aspergillus fumigatus in allergic diseases. In: Brakhage AA, Jahn B, Schmidt A. editors. Contributions in microbiology. Vol 2. Basel: Karger; 1999. p 44-56.
    • (1999) Contributions in Microbiology , vol.2 , pp. 44-56
    • Crameri, R.1
  • 38
    • 0033507180 scopus 로고    scopus 로고
    • Selective cloning of allergens from the skin colonizing yeast Malassezia furfur by phage surface display technology
    • Lindborg M, Magnusson CGM, Zargari A, Schmidt M, Scheynius A, Crameri R, et al. Selective cloning of allergens from the skin colonizing yeast Malassezia furfur by phage surface display technology. J Invest Dermatol 1999;113:156-61.
    • (1999) J Invest Dermatol , vol.113 , pp. 156-161
    • Lindborg, M.1    Magnusson, C.G.M.2    Zargari, A.3    Schmidt, M.4    Scheynius, A.5    Crameri, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.