메뉴 건너뛰기




Volumn 5, Issue 1, 1997, Pages 33-45

The molecular basis for allergen cross-reactivity: Crystal structure and IgE-epitope mapping of birch pollen profilin

Author keywords

actin; allergen; IgE; IgE epitopes; poly L proline; profilin

Indexed keywords

ACANTHAMOEBA; ANIMALIA; EUKARYOTA; MAMMALIA;

EID: 0031568307     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00164-0     Document Type: Article
Times cited : (210)

References (56)
  • 1
    • 12644256605 scopus 로고
    • Cold Spring Harbor Laboratory Press, USA
    • Valenta, R., et al., Scheiner, O. (1993). Vaccines 93. pp. 37-42. Cold Spring Harbor Laboratory Press, USA.
    • (1993) Vaccines 93 , pp. 37-42
    • Valenta, R.1    Scheiner, O.2
  • 2
    • 0026542305 scopus 로고
    • Profilins constitute a novel family of functional plant allergens
    • Valenta, R., et al., & Scheiner, O. (1992). Profilins constitute a novel family of functional plant allergens. J. Exp. Med. 175, 377-385.
    • (1992) J. Exp. Med. , vol.175 , pp. 377-385
    • Valenta, R.1    Scheiner, O.2
  • 3
    • 0025887036 scopus 로고
    • Identification of profilin as a novel pollen allergen: IgE autoreactivity in sensitized individuals
    • Valenta, R., et al., & Scheiner, O. (1991). Identification of profilin as a novel pollen allergen: IgE autoreactivity in sensitized individuals. Science 253, 557-559.
    • (1991) Science , vol.253 , pp. 557-559
    • Valenta, R.1    Scheiner, O.2
  • 4
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical analysis of mechanisms and functions
    • Pollard, T.D. & Copper, J.A. (1986). Actin and actin-binding proteins. A critical analysis of mechanisms and functions. Annu. Rev. Biochem. 55, 987-1035.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Copper, J.A.2
  • 5
    • 0019194944 scopus 로고
    • Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound nucleotide
    • Mockrin, S. & Korn, E. (1980). Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound nucleotide. Biochemistry 19, 5359-5362.
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mockrin, S.1    Korn, E.2
  • 6
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin β4 and profilin. A potential regulatory mechanism for actin polymerization in the cell
    • Goldschmidt-Clermont, P.J., Furman, M.I., Wachsstock, D., Safer, D., Nachmias, V.T. & Pollard, T.D. (1992). The control of actin nucleotide exchange by thymosin β4 and profilin. A potential regulatory mechanism for actin polymerization in the cell. Mol. Biol. Cell 3, 1015-1024.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.T.5    Pollard, T.D.6
  • 7
    • 0027163104 scopus 로고
    • Modulation of the interaction between G-actin and thymosin β4 by the ATP/ADP ratio: Possible implication in the regulation of actin dynamics
    • Carlier, M.-F., Jean, C., Rieger, K. J., Lenfant, M. & Pantaloni, D. (1993). Modulation of the interaction between G-actin and thymosin β4 by the ATP/ADP ratio: possible implication in the regulation of actin dynamics. Proc. Natl. Acad. Sci. USA 90, 5034-5038.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5034-5038
    • Carlier, M.-F.1    Jean, C.2    Rieger, K.J.3    Lenfant, M.4    Pantaloni, D.5
  • 8
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin β4
    • Pantaloni, D. & Carlier, M.-F. (1993). How profilin promotes actin filament assembly in the presence of thymosin β4. Cell 75, 1007-1013.
    • (1993) Cell , vol.75 , pp. 1007-1013
    • Pantaloni, D.1    Carlier, M.-F.2
  • 11
    • 0025517560 scopus 로고
    • The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C
    • Machesky, L.M., Goldschmidt-Clermont, P.J. & Pollard, T.D. (1990). The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C. Cell Regul. 1, 937-950.
    • (1990) Cell Regul. , vol.1 , pp. 937-950
    • Machesky, L.M.1    Goldschmidt-Clermont, P.J.2    Pollard, T.D.3
  • 13
    • 0029097309 scopus 로고
    • Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin
    • Sohn, R.H., Chen, J., Koblan, K.S., Bray, P.F. & Goldschmidt-Clermont, P.J. (1995). Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin. J. Biol. Chem. 270, 21114-21120.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21114-21120
    • Sohn, R.H.1    Chen, J.2    Koblan, K.S.3    Bray, P.F.4    Goldschmidt-Clermont, P.J.5
  • 14
    • 0027965072 scopus 로고
    • X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates
    • Fedorov, A.A., Magnus, K.A., Graupe, M.H., Lattmam, E.E., Pollard, T.D. & Almo, S.C. (1994). X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates. Proc. Natl. Acad. Sci. USA 91, 8636-8640.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8636-8640
    • Fedorov, A.A.1    Magnus, K.A.2    Graupe, M.H.3    Lattmam, E.E.4    Pollard, T.D.5    Almo, S.C.6
  • 16
    • 0022409564 scopus 로고
    • Poly(L-proline)-binding proteins from chick embryos are a profilin and a profilactin
    • Tanaka, M. & Shibata, H. (1985) Poly(L-proline)-binding proteins from chick embryos are a profilin and a profilactin. Eur. J. Biochem. 151, 291-297.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 291-297
    • Tanaka, M.1    Shibata, H.2
  • 18
    • 0028153875 scopus 로고
    • Elucidation of the poly-L-proline binding site in Acanthamoeba profilin by NMR spectroscopy
    • Archer, S.J., Vinson, V.K., Pollard, T.D. & Torchia, D.A. (1994). Elucidation of the poly-L-proline binding site in Acanthamoeba profilin by NMR spectroscopy. FEBS Lett. 337, 145-151.
    • (1994) FEBS Lett. , vol.337 , pp. 145-151
    • Archer, S.J.1    Vinson, V.K.2    Pollard, T.D.3    Torchia, D.A.4
  • 19
    • 0028108647 scopus 로고
    • Identification of the poly-L-proline binding site on human profilin
    • W.J. Metzler, Bell, A.J., Ernst, E., Lavoie, T.B. & Mueller, L. (1994). Identification of the poly-L-proline binding site on human profilin. J. Biol. Chem. 269, 4620-4625.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4620-4625
    • Metzler, W.J.1    Bell, A.J.2    Ernst, E.3    Lavoie, T.B.4    Mueller, L.5
  • 20
    • 0027376752 scopus 로고
    • Mutagenesis of human profilin locates its poly(L-proline)-binding site to a hydrophobic patch of aromatic amino acids
    • Bjorkegren, C., Rozycki, M., Schutt, C.E., Lindberg, U. & Karlsson, R. (1993). Mutagenesis of human profilin locates its poly(L-proline)-binding site to a hydrophobic patch of aromatic amino acids. FEBS Lett. 333, 123-126.
    • (1993) FEBS Lett. , vol.333 , pp. 123-126
    • Bjorkegren, C.1    Rozycki, M.2    Schutt, C.E.3    Lindberg, U.4    Karlsson, R.5
  • 21
    • 0029025248 scopus 로고
    • The proline-rich focal adhesion and mircofilament protein VASP is a ligand for profilins
    • Reinhard, M., et al., & Walter, U. (1995). The proline-rich focal adhesion and mircofilament protein VASP is a ligand for profilins. EMBO J. 14, 1583-1589.
    • (1995) EMBO J. , vol.14 , pp. 1583-1589
    • Reinhard, M.1    Walter, U.2
  • 22
    • 0029157584 scopus 로고
    • Identification, purification and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP
    • M. Reinhard, Jouvenal, K., Tripier, D. & Walter, U. (1995). Identification, purification and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP. Proc. Natl. Acad. Sci. USA 92, 7956-7060.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7956-17060
    • Reinhard, M.1    Jouvenal, K.2    Tripier, D.3    Walter, U.4
  • 24
    • 0001099937 scopus 로고
    • Traitement statistique des arreurs daans la determination des structures crystallines
    • Luzzati, V. (1952). Traitement statistique des arreurs daans la determination des structures crystallines. Acta. Cryst. 5, 802-810.
    • (1952) Acta. Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 25
  • 26
    • 0014347799 scopus 로고
    • Stereochemical criteria for polypeptide and proteins. V. Conformation of a system of three link peptide units
    • Venkatachalam, C.M. (1968). Stereochemical criteria for polypeptide and proteins. V. Conformation of a system of three link peptide units. Biopolymers 6, 1425-1436.
    • (1968) Biopolymers , vol.6 , pp. 1425-1436
    • Venkatachalam, C.M.1
  • 27
    • 0020485895 scopus 로고
    • Orthogonal packing of β-pleated sheets in proteins
    • Chothia, C. & Janin, J. (1982). Orthogonal packing of β-pleated sheets in proteins. Biochemistry 21, 3955-3065.
    • (1982) Biochemistry , vol.21 , pp. 3955-13065
    • Chothia, C.1    Janin, J.2
  • 28
    • 0028348081 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins
    • Murzin, A.G., Lesk, A.M. & Chothia, C. (1994). Principles determining the structure of β-sheet barrels in proteins. J. Mol. Biol. 236, 1369-1381.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1369-1381
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 30
    • 0027731196 scopus 로고
    • 15N NMR assignments and global folding pattern
    • 15N NMR assignments and global folding pattern. Biochemistry 32, 13818-13829.
    • (1993) Biochemistry , vol.32 , pp. 13818-13829
    • Metzler, W.J.1    Mueller, L.2
  • 31
    • 0028109193 scopus 로고
    • Crystallization and structure determination of bovine profilin at 2.0 Å resolution
    • Cedergren-Zeppezauer, E.S., et al., & Schutt, C.E. (1994). Crystallization and structure determination of bovine profilin at 2.0 Å resolution. J. Mol. Biol. 249, 459-475.
    • (1994) J. Mol. Biol. , vol.249 , pp. 459-475
    • Cedergren-Zeppezauer, E.S.1    Schutt, C.E.2
  • 32
    • 0016743427 scopus 로고
    • A comparison of the heme binding pocket in globins and cytochrome β5
    • Rossmann, M.G. & Argos, P. (1975). A comparison of the heme binding pocket in globins and cytochrome β5. J. Biol. Chem. 250, 7525-7532.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7525-7532
    • Rossmann, M.G.1    Argos, P.2
  • 33
    • 10544242206 scopus 로고    scopus 로고
    • Molecular and structural analysis of a continuous birch profilin epitope defined by a monoclonal antibody
    • Wiedemann, P., et al., & Valenta, R. (1996). Molecular and structural analysis of a continuous birch profilin epitope defined by a monoclonal antibody. J. Biol. Chem. 271, 29915-29921.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29915-29921
    • Wiedemann, P.1    Valenta, R.2
  • 34
    • 0024363256 scopus 로고
    • Acanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin
    • Vandekerckhove, J.S., Kaiser, D.A. & Pollard, T.D. (1989). Acanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin. J. Cell Biol. 109, 619-626.
    • (1989) J. Cell Biol. , vol.109 , pp. 619-626
    • Vandekerckhove, J.S.1    Kaiser, D.A.2    Pollard, T.D.3
  • 36
    • 0026705211 scopus 로고
    • Proton resonance assignments and three-dimensional solution structure of the ragweed allergen Amb a V by nuclear magnetic resonance spectroscopy
    • Metzler, W.J., Valentine, K., Roebber, M., Marsh, D.G., & Mueller, L. (1992). Proton resonance assignments and three-dimensional solution structure of the ragweed allergen Amb a V by nuclear magnetic resonance spectroscopy. Biochemistry 31, 8697-8705.
    • (1992) Biochemistry , vol.31 , pp. 8697-8705
    • Metzler, W.J.1    Valentine, K.2    Roebber, M.3    Marsh, D.G.4    Mueller, L.5
  • 37
    • 0028280829 scopus 로고
    • Immunologic and molecular characterization of Amb p V allergens from Ambrosia psilostachya pollen
    • Ghosh, B., et al., & Marsh, D.G. (1994). Immunologic and molecular characterization of Amb p V allergens from Ambrosia psilostachya pollen. J. Immunol. 152, 2882-2889.
    • (1994) J. Immunol. , vol.152 , pp. 2882-2889
    • Ghosh, B.1    Marsh, D.G.2
  • 38
    • 0027449093 scopus 로고
    • Molecular characterization of PhI p II, a major timothy grass (Phleum pratense) pollen allergen
    • Dolecek, C., et al., & Valenta, R. (1993). Molecular characterization of PhI p II, a major timothy grass (Phleum pratense) pollen allergen. FEBS Lett. 335, 299-304.
    • (1993) FEBS Lett. , vol.335 , pp. 299-304
    • Dolecek, C.1    Valenta, R.2
  • 39
    • 0029870704 scopus 로고    scopus 로고
    • Immunologic characterization of purified recombinant timothy grass pollen (Phleum pretense) allergens (PhI p 1, PhI p 2, PhI p 5)
    • Vrtala, S., et al., & Valenta, R. (1996). Immunologic characterization of purified recombinant timothy grass pollen (Phleum pretense) allergens (PhI p 1, PhI p 2, PhI p 5). J. Allergy Clin. Immunol. 97, 781-787.
    • (1996) J. Allergy Clin. Immunol. , vol.97 , pp. 781-787
    • Vrtala, S.1    Valenta, R.2
  • 40
    • 0027364291 scopus 로고
    • Identification of profilin as an actin-binding protein in higher plants
    • Valenta, R., et al., & Scheiner, O. (1993). Identification of profilin as an actin-binding protein in higher plants. J. Biol. Chem. 268, 22777-23781.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22777-23781
    • Valenta, R.1    Scheiner, O.2
  • 41
    • 0023877882 scopus 로고
    • Sequence analysis of cDNA coding for a major house dust mite allergen, der p 1. Homology with cysteine proteases
    • Chua, K.Y., et al., & Turner, K.J. (1988). Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1. Homology with cysteine proteases. J. Exp. Med. 167, 175-182.
    • (1988) J. Exp. Med. , vol.167 , pp. 175-182
    • Chua, K.Y.1    Turner, K.J.2
  • 42
    • 0028818335 scopus 로고
    • A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: Inate protection by proteases
    • Hewitt, C.R., Brown, A.P., Hart, B.J. & Pritchard, D.I. (1995). A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: inate protection by proteases. J. Exp. Med. 182, 1537-1544.
    • (1995) J. Exp. Med. , vol.182 , pp. 1537-1544
    • Hewitt, C.R.1    Brown, A.P.2    Hart, B.J.3    Pritchard, D.I.4
  • 43
    • 0028913520 scopus 로고
    • Major allergen PhI p Vb in timothy grass is a novel pollen RNase
    • Bufe, A., Schramm, G., Keown, M.B., Schlaak, M. & Becker, W.M. (1995). Major allergen PhI p Vb in timothy grass is a novel pollen RNase. FEBS Lett. 363, 6-12.
    • (1995) FEBS Lett. , vol.363 , pp. 6-12
    • Bufe, A.1    Schramm, G.2    Keown, M.B.3    Schlaak, M.4    Becker, W.M.5
  • 45
    • 0027431127 scopus 로고
    • Properties of tree and grass pollen allergens: Reinvestigation of the linkage between solubility and allergenicity
    • Vrtala, S., et al., & Valenta, R. (1993). Properties of tree and grass pollen allergens: reinvestigation of the linkage between solubility and allergenicity. Int. Arch. Allergy Immunol. 102, 160-169.
    • (1993) Int. Arch. Allergy Immunol. , vol.102 , pp. 160-169
    • Vrtala, S.1    Valenta, R.2
  • 46
    • 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., et al., & Scheiner, O. (1995). 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. 95, 962-969.
    • (1995) J. Allergy Clin. Immunol. , vol.95 , pp. 962-969
    • Ebner, C.1    Scheiner, O.2
  • 47
    • 0029664756 scopus 로고    scopus 로고
    • Type I allergic reactions to plant-derived food: A consequence of primary sensitization to pollen allergens
    • Valenta, R. & Kraft, D. (1996). Type I allergic reactions to plant-derived food: a consequence of primary sensitization to pollen allergens. J. Allergy Clin. Immunol. 97, 893-895.
    • (1996) J. Allergy Clin. Immunol. , vol.97 , pp. 893-895
    • Valenta, R.1    Kraft, D.2
  • 48
    • 0027939421 scopus 로고
    • Isolation of an immunodominant IgE hapten from an epitope expression cDNA library. Dissection of the allergic effector reaction
    • Ball, T., et al., & Valenta, R. (1994). Isolation of an immunodominant IgE hapten from an epitope expression cDNA library. Dissection of the allergic effector reaction. J. Biol. Chem. 269, 28323-28328.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28323-28328
    • Ball, T.1    Valenta, R.2
  • 49
    • 0028316191 scopus 로고
    • Purification, characterization and crystallization of Acanthamoeba profilin expressed in E. coli
    • Almo, S.C., Pollard, T.D., Way, M. & Lattman, E.E. (1994). Purification, characterization and crystallization of Acanthamoeba profilin expressed in E. coli. J. Mol. Biol. 236, 950-952.
    • (1994) J. Mol. Biol. , vol.236 , pp. 950-952
    • Almo, S.C.1    Pollard, T.D.2    Way, M.3    Lattman, E.E.4
  • 50
    • 85046526624 scopus 로고
    • Evaluation of single crystal X-ray diffraction data from a position sensitive detector
    • Kabsch, W. (1988). Evaluation of single crystal X-ray diffraction data from a position sensitive detector. J. Appl. Cryst. 21, 916-924.
    • (1988) J. Appl. Cryst. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 52
    • 0002701928 scopus 로고
    • PHASES-a program package for processing and analysis of diffraction data for macromolecules
    • Furey, W. & Swaminathan, S. (1990). PHASES-a program package for processing and analysis of diffraction data for macromolecules. Acta. Cryst. 18, 73.
    • (1990) Acta. Cryst. , vol.18 , pp. 73
    • Furey, W.1    Swaminathan, S.2
  • 53
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones, T.A. (1985). Interactive computer graphics: FRODO. Methods Enzymol. 115, 157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 55
    • 0026244229 scopus 로고
    • MOLSCRIPT a program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 56
    • 84986522918 scopus 로고
    • ICM: A new method for structure modeling and design
    • Abagyan, R.A., Totrov, M.M. & Kuznetsov, D.A. (1994). ICM: a new method for structure modeling and design. J. Comput Chem. 15, 488-506.
    • (1994) J. Comput Chem. , vol.15 , pp. 488-506
    • Abagyan, R.A.1    Totrov, M.M.2    Kuznetsov, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.