메뉴 건너뛰기




Volumn 290, Issue 36, 2015, Pages 22111-22126

A crystallin fold in the interleukin-4-inducing principle of schistosoma mansoni eggs (IPSE/α-1) mediates IgE binding for antigen-independent basophil activation

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84941353131     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.675066     Document Type: Article
Times cited : (29)

References (48)
  • 1
    • 77958088338 scopus 로고    scopus 로고
    • Th2 immune response against Schistosoma mansoni infection
    • Schramm, G., and Haas, H. (2010) Th2 immune response against Schistosoma mansoni infection. Microbes Infect. 12, 881-888.
    • (2010) Microbes Infect. , vol.12 , pp. 881-888
    • Schramm, G.1    Haas, H.2
  • 3
    • 0031570939 scopus 로고    scopus 로고
    • IL-4 protects against TNF-α 32 -mediated cachexia and death during acute schistosomiasis
    • Brunet, L. R., Finkelman, F. D., Cheever, A. W., Kopf, M. A., and Pearce, E. J. (1997) IL-4 protects against TNF-α 32 -mediated cachexia and death during acute schistosomiasis. J. Immunol. 159, 777-785.
    • (1997) J. Immunol. , vol.159 , pp. 777-785
    • Brunet, L.R.1    Finkelman, F.D.2    Cheever, A.W.3    Kopf, M.A.4    Pearce, E.J.5
  • 4
    • 44449098751 scopus 로고    scopus 로고
    • IL-4Rα expression by bone marrow-derived cells is necessary and sufficient for host protection against acute schistosomiasis
    • Herbert, D. R., Orekov, T., Perkins, C., Rothenberg, M. E., and Finkelman, F. D. (2008) IL-4Rα expression by bone marrow-derived cells is necessary and sufficient for host protection against acute schistosomiasis. J. Immunol. 180, 4948-4955.
    • (2008) J. Immunol. , vol.180 , pp. 4948-4955
    • Herbert, D.R.1    Orekov, T.2    Perkins, C.3    Rothenberg, M.E.4    Finkelman, F.D.5
  • 6
    • 79952741741 scopus 로고    scopus 로고
    • Basophils are the major producers of IL-4 during primary helminth infection
    • van Panhuys, N., Prout, M., Forbes, E., Min, B., Paul, W. E., and Le Gros, G. (2011) Basophils are the major producers of IL-4 during primary helminth infection. J. Immunol. 186, 2719-2728.
    • (2011) J. Immunol. , vol.186 , pp. 2719-2728
    • Van Panhuys, N.1    Prout, M.2    Forbes, E.3    Min, B.4    Paul, W.E.5    Le Gros, G.6
  • 8
    • 34248143481 scopus 로고    scopus 로고
    • Cutting edge: IPSE/-α1, a glycoprotein from Schistosoma mansoni eggs, induces IgE-dependent, antigen-independent IL-4 production by murine basophils in vivo
    • Schramm, G., Mohrs, K., Wodrich, M., Doenhoff, M. J., Pearce, E. J., Haas, H., and Mohrs, M. (2007) Cutting edge: IPSE/-α1, a glycoprotein from Schistosoma mansoni eggs, induces IgE-dependent, antigen-independent IL-4 production by murine basophils in vivo. J. Immunol. 178, 6023-6027.
    • (2007) J. Immunol. , vol.178 , pp. 6023-6027
    • Schramm, G.1    Mohrs, K.2    Wodrich, M.3    Doenhoff, M.J.4    Pearce, E.J.5    Haas, H.6    Mohrs, M.7
  • 10
    • 0025744455 scopus 로고
    • The purification, characterization, serological activity and hepatotoxic properties of two cationic glycoproteins (α1 and ω1) from Schistosoma mansoni eggs
    • Dunne, D. W., Jones, F. M., and Doenhoff, M. J. (1991) The purification, characterization, serological activity and hepatotoxic properties of two cationic glycoproteins (α1 and ω1) from Schistosoma mansoni eggs. Parasitology 103, 225-236.
    • (1991) Parasitology , vol.103 , pp. 225-236
    • Dunne, D.W.1    Jones, F.M.2    Doenhoff, M.J.3
  • 13
    • 0032989460 scopus 로고    scopus 로고
    • Lipid A directly inhibits IL-4 production by murine Th2 cells but does not inhibit IFN production by Th1 cells
    • Watanabe, T., Inoue, T., Ochi, H., Terashima, M., Asano, Y., and Nakatani, T. (1999) Lipid A directly inhibits IL-4 production by murine Th2 cells but does not inhibit IFN production by Th1 cells. Eur. J. Immunol. 29, 413-418.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 413-418
    • Watanabe, T.1    Inoue, T.2    Ochi, H.3    Terashima, M.4    Asano, Y.5    Nakatani, T.6
  • 15
    • 79953328088 scopus 로고    scopus 로고
    • Interleukin-4-inducing principle from Schistosoma mansoni eggs contains a functional C-terminal nuclear localization signal necessary for nuclear translocation in mammalian cells but not for its uptake
    • Kaur, I., Schramm, G., Everts, B., Scholzen, T., Kindle, K. B., Beetz, C., Montiel-Duarte, C., Blindow, S., Jones, A. T., Haas, H., Stolnik, S., Heery, D. M., and Falcone, F. H. (2011) Interleukin-4-inducing principle from Schistosoma mansoni eggs contains a functional C-terminal nuclear localization signal necessary for nuclear translocation in mammalian cells but not for its uptake. Infect. Immun. 79, 1779-1788.
    • (2011) Infect. Immun. , vol.79 , pp. 1779-1788
    • Kaur, I.1    Schramm, G.2    Everts, B.3    Scholzen, T.4    Kindle, K.B.5    Beetz, C.6    Montiel-Duarte, C.7    Blindow, S.8    Jones, A.T.9    Haas, H.10    Stolnik, S.11    Heery, D.M.12    Falcone, F.H.13
  • 16
    • 33646265778 scopus 로고    scopus 로고
    • IPSE/α-1, a major secretory glycoprotein antigen from schistosome eggs, expresses the Lewis X motif on core-difucosylatedN-glycans
    • Wuhrer, M., Balog, C. I., Catalina, M. I., Jones, F. M., Schramm, G., Haas, H., Doenhoff, M. J., Dunne, D. W., Deelder, A. M., and Hokke, C. H. (2006) IPSE/α-1, a major secretory glycoprotein antigen from schistosome eggs, expresses the Lewis X motif on core-difucosylatedN-glycans. FEBS J. 273, 2276-2292.
    • (2006) FEBS J. , vol.273 , pp. 2276-2292
    • Wuhrer, M.1    Balog, C.I.2    Catalina, M.I.3    Jones, F.M.4    Schramm, G.5    Haas, H.6    Doenhoff, M.J.7    Dunne, D.W.8    Deelder, A.M.9    Hokke, C.H.10
  • 17
    • 67649105327 scopus 로고    scopus 로고
    • Cloning, expression, purification, crystallization and preliminary x-ray crystallographic analysis of interleukin-4-inducing principle from Schistosoma mansoni eggs (IPSE/α-1). Acta Crystallogr
    • Mayerhofer, H., Schramm, G., Hatzopoulos, G. N., Mueller-Dieckmann, C., Haas, H., and Mueller-Dieckmann, J. (2009) Cloning, expression, purification, crystallization and preliminary x-ray crystallographic analysis of interleukin-4-inducing principle from Schistosoma mansoni eggs (IPSE/α-1). Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65, 594 -596.
    • (2009) Sect. F Struct. Biol. Cryst. Commun. , vol.65 , pp. 594-596
    • Mayerhofer, H.1    Schramm, G.2    Hatzopoulos, G.N.3    Mueller-Dieckmann, C.4    Haas, H.5    Mueller-Dieckmann, J.6
  • 18
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 19
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler, M., Schleucher, J., and Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. Nuclear Magn. Reson. Spectrosc. 34, 93-158.
    • (1999) Prog. Nuclear Magn. Reson. Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 20
    • 84855392765 scopus 로고    scopus 로고
    • (1)H, (13)C and (15)N chemical shift assignments of IPSEΔNLS
    • Meyer, N. H., Schramm, G., and Sattler, M. (2011) (1)H, (13)C and (15)N chemical shift assignments of IPSEΔNLS. Biomol. NMR Assign. 5, 225-227.
    • (2011) Biomol. NMR Assign. , vol.5 , pp. 225-227
    • Meyer, N.H.1    Schramm, G.2    Sattler, M.3
  • 22
    • 58849162221 scopus 로고    scopus 로고
    • Automated structure determination from NMR spectra
    • Güntert, P. (2009) Automated structure determination from NMR spectra. Eur. Biophys. J. 38, 129-143.
    • (2009) Eur. Biophys. J , vol.38 , pp. 129-143
    • Güntert, P.1
  • 23
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR. 44, 213-223.
    • (2009) J. Biomol. NMR. , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 26
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8, 477-486.
    • (1996) J. Biomol. NMR. , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 28
    • 0033609011 scopus 로고    scopus 로고
    • Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules
    • Riek, R., Wider, G., Pervushin, K., and Wüthrich, K. (1999) Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules. Proc. Natl. Acad. Sci. U.S.A. 96, 4918-4923.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4918-4923
    • Riek, R.1    Wider, G.2    Pervushin, K.3    Wüthrich, K.4
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 3242877815 scopus 로고    scopus 로고
    • Clus-Pro: A fully automated algorithm for protein-protein docking
    • Comeau, S. R., Gatchell, D. W., Vajda, S., and Camacho, C. J. (2004) Clus-Pro: A fully automated algorithm for protein-protein docking. Nucleic Acids Res. 32, W96-W99.
    • (2004) Nucleic Acids Res. , vol.32 , pp. W96-W99
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 35
    • 33947626069 scopus 로고    scopus 로고
    • Synthesis of a fluorescent ganglioside GM1 derivative and screening of a synthetic peptide library for GM1 binding sequence motifs
    • Röckendorf, N., Bade, S., Hirst, T. R., Gorris, H. H., and Frey, A. (2007) Synthesis of a fluorescent ganglioside GM1 derivative and screening of a synthetic peptide library for GM1 binding sequence motifs. Bioconjug. Chem. 18, 573-578.
    • (2007) Bioconjug. Chem. , vol.18 , pp. 573-578
    • Röckendorf, N.1    Bade, S.2    Hirst, T.R.3    Gorris, H.H.4    Frey, A.5
  • 37
    • 77950023643 scopus 로고    scopus 로고
    • A comparative proteomic study of the undeveloped and developed Schistosoma mansoni egg and its contents: The miracidium, hatch fluid and secretions
    • Mathieson, W., and Wilson, R. A. (2010) A comparative proteomic study of the undeveloped and developed Schistosoma mansoni egg and its contents: The miracidium, hatch fluid and secretions. Int. J. Parasitol. 40, 617-628.
    • (2010) Int. J. Parasitol. , vol.40 , pp. 617-628
    • Mathieson, W.1    Wilson, R.A.2
  • 38
    • 0035167113 scopus 로고    scopus 로고
    • Lens crystallins and their microbial homologs: Structure, stability, and function
    • Jaenicke, R., and Slingsby, C. (2001) Lens crystallins and their microbial homologs: structure, stability, and function. Crit. Rev. Biochem. Mol. Biol. 36, 435-499.
    • (2001) Crit. Rev. Biochem. Mol. Biol. , vol.36 , pp. 435-499
    • Jaenicke, R.1    Slingsby, C.2
  • 39
  • 41
    • 34248157158 scopus 로고    scopus 로고
    • Insights into immunoglobulin E receptor signaling from structurally defined ligands
    • Holowka, D., Sil, D., Torigoe, C., and Baird, B. (2007) Insights into immunoglobulin E receptor signaling from structurally defined ligands. Immunol. Rev. 217, 269-279.
    • (2007) Immunol. Rev. , vol.217 , pp. 269-279
    • Holowka, D.1    Sil, D.2    Torigoe, C.3    Baird, B.4
  • 42
    • 4644275745 scopus 로고    scopus 로고
    • Early divergence of Fcε receptor I signals for receptor up-regulation and internalization from degranulation, cytokine production, and survival
    • Kitaura, J., Xiao, W., Maeda-Yamamoto, M., Kawakami, Y., Lowell, C. A., and Kawakami, T. (2004) Early divergence of Fcε receptor I signals for receptor up-regulation and internalization from degranulation, cytokine production, and survival. J. Immunol. 173, 4317-4323.
    • (2004) J. Immunol. , vol.173 , pp. 4317-4323
    • Kitaura, J.1    Xiao, W.2    Maeda-Yamamoto, M.3    Kawakami, Y.4    Lowell, C.A.5    Kawakami, T.6
  • 44
    • 18344378070 scopus 로고    scopus 로고
    • Death of a dogma or enforcing the artificial: Monomeric IgE binding may initiate mast cell response by inducing its receptor aggregation
    • Schweitzer-Stenner, R., and Pecht, I. (2005) Death of a dogma or enforcing the artificial: Monomeric IgE binding may initiate mast cell response by inducing its receptor aggregation. J. Immunol. 174, 4461-4464.
    • (2005) J. Immunol. , vol.174 , pp. 4461-4464
    • Schweitzer-Stenner, R.1    Pecht, I.2
  • 45
    • 77957125242 scopus 로고    scopus 로고
    • Oligomeric organization of the B-cell antigen receptor on resting cells
    • Yang, J., and Reth, M. (2010) Oligomeric organization of the B-cell antigen receptor on resting cells. Nature 467, 465-469.
    • (2010) Nature , vol.467 , pp. 465-469
    • Yang, J.1    Reth, M.2
  • 46
    • 74049157769 scopus 로고    scopus 로고
    • TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation
    • Lillemeier, B. F., Mörtelmaier, M. A., Forstner, M. B., Huppa, J. B., Groves, J. T., and Davis, M. M. (2010) TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation. Nat. Immunol. 11, 90-96.
    • (2010) Nat. Immunol. , vol.11 , pp. 90-96
    • Lillemeier, B.F.1    Mörtelmaier, M.A.2    Forstner, M.B.3    Huppa, J.B.4    Groves, J.T.5    Davis, M.M.6
  • 47
    • 78649863361 scopus 로고    scopus 로고
    • The dissociation activation model of B cell antigen receptor triggering
    • Yang, J., and Reth, M. (2010) The dissociation activation model of B cell antigen receptor triggering. FEBS Lett. 584, 4872-4877.
    • (2010) FEBS Lett. , vol.584 , pp. 4872-4877
    • Yang, J.1    Reth, M.2
  • 48


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.