메뉴 건너뛰기




Volumn 50, Issue 2, 2011, Pages 172-180

Conformational changes in IpaD from shigella flexneri upon binding bile salts provide insight into the second step of type III secretion

Author keywords

[No Author keywords available]

Indexed keywords

BILE SALTS; CONFORMATIONAL CHANGE; DEOXYCHOLATE; DIRECT INTERACTIONS; ENVIRONMENTAL FACTORS; EUKARYOTIC CELLS; GLOBULAR DOMAINS; HOST CELLS; MUTATION ANALYSIS; NMR CHEMICAL SHIFTS; NMR SPECTROSCOPY; RESONANCE ENERGY TRANSFER; SHIGELLA FLEXNERI; SPECIFIC SITES; TRANSLOCATORS; TYPE III SECRETIONS;

EID: 78651374014     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101365f     Document Type: Article
Times cited : (54)

References (31)
  • 1
    • 19344366789 scopus 로고    scopus 로고
    • Shigellosis
    • Niyogi, S. K. (2005) Shigellosis J. Microbiol. 43, 133-143
    • (2005) J. Microbiol. , vol.43 , pp. 133-143
    • Niyogi, S.K.1
  • 4
    • 38549126641 scopus 로고    scopus 로고
    • Molecular pathogenesis of Shigella spp.: Controlling host cell signaling, invasion, and death by type III secretion
    • Schroeder, G. N. and Hilbi, H. (2008) Molecular pathogenesis of Shigella spp.: controlling host cell signaling, invasion, and death by type III secretion Clin. Microbiol. Rev. 21, 134-156
    • (2008) Clin. Microbiol. Rev. , vol.21 , pp. 134-156
    • Schroeder, G.N.1    Hilbi, H.2
  • 5
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • Zychlinsky, A., Prevost, M. C., and Sansonetti, P. J. (1992) Shigella flexneri induces apoptosis in infected macrophages Nature 358, 167-169
    • (1992) Nature , vol.358 , pp. 167-169
    • Zychlinsky, A.1    Prevost, M.C.2    Sansonetti, P.J.3
  • 6
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan, J. E. and Wolf-Watz, H. (2006) Protein delivery into eukaryotic cells by type III secretion machines Nature 444, 567-573
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 9
    • 33947712323 scopus 로고    scopus 로고
    • Bile salts stimulate recruitment of IpaB to the Shigella flexneri surface, where it colocalizes with IpaD at the tip of the type III secretion needle
    • Olive, A. J., Kenjale, R., Espina, M., Moore, D. S., Picking, W. L., and Picking, W. D. (2007) Bile salts stimulate recruitment of IpaB to the Shigella flexneri surface, where it colocalizes with IpaD at the tip of the type III secretion needle Infect. Immun. 75, 2626-2629
    • (2007) Infect. Immun. , vol.75 , pp. 2626-2629
    • Olive, A.J.1    Kenjale, R.2    Espina, M.3    Moore, D.S.4    Picking, W.L.5    Picking, W.D.6
  • 10
    • 67650090752 scopus 로고    scopus 로고
    • Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction
    • Epler, C. R., Dickenson, N. E., Olive, A. J., Picking, W. L., and Picking, W. D. (2009) Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction Infect. Immun. 77, 2754-2761
    • (2009) Infect. Immun. , vol.77 , pp. 2754-2761
    • Epler, C.R.1    Dickenson, N.E.2    Olive, A.J.3    Picking, W.L.4    Picking, W.D.5
  • 13
    • 33746614695 scopus 로고    scopus 로고
    • Spectroscopic and calorimetric analyses of invasion plasmid antigen D (IpaD) from Shigella flexneri reveal the presence of two structural domains
    • Espina, M., Ausar, S. F., Middaugh, C. R., Picking, W. D., and Picking, W. L. (2006) Spectroscopic and calorimetric analyses of invasion plasmid antigen D (IpaD) from Shigella flexneri reveal the presence of two structural domains Biochemistry 45, 9219-9227
    • (2006) Biochemistry , vol.45 , pp. 9219-9227
    • Espina, M.1    Ausar, S.F.2    Middaugh, C.R.3    Picking, W.D.4    Picking, W.L.5
  • 14
    • 36148933351 scopus 로고    scopus 로고
    • Identification of the MxiH needle protein residues responsible for anchoring invasion plasmid antigen D to the type III secretion needle tip
    • Zhang, L., Wang, Y., Olive, A. J., Smith, N. D., Picking, W. D., De Guzman, R. N., and Picking, W. L. (2007) Identification of the MxiH needle protein residues responsible for anchoring invasion plasmid antigen D to the type III secretion needle tip J. Biol. Chem. 282, 32144-32151
    • (2007) J. Biol. Chem. , vol.282 , pp. 32144-32151
    • Zhang, L.1    Wang, Y.2    Olive, A.J.3    Smith, N.D.4    Picking, W.D.5    De Guzman, R.N.6    Picking, W.L.7
  • 15
    • 17644366419 scopus 로고    scopus 로고
    • Cholesterol binding by the bacterial type III translocon is essential for virulence effector delivery into mammalian cells
    • Hayward, R. D., Cain, R. J., McGhie, E. J., Phillips, N., Garner, M. J., and Koronakis, V. (2005) Cholesterol binding by the bacterial type III translocon is essential for virulence effector delivery into mammalian cells Mol. Microbiol. 56, 590-603
    • (2005) Mol. Microbiol. , vol.56 , pp. 590-603
    • Hayward, R.D.1    Cain, R.J.2    McGhie, E.J.3    Phillips, N.4    Garner, M.J.5    Koronakis, V.6
  • 16
    • 0037009369 scopus 로고    scopus 로고
    • Initial steps of Shigella infection depend on the cholesterol/ sphingolipid raft-mediated CD44-IpaB interaction
    • Lafont, F., Tran Van Nhieu, G., Hanada, K., Sansonetti, P., and van der Goot, F. G. (2002) Initial steps of Shigella infection depend on the cholesterol/sphingolipid raft-mediated CD44-IpaB interaction EMBO J. 21, 4449-4457
    • (2002) EMBO J. , vol.21 , pp. 4449-4457
    • Lafont, F.1    Tran Van Nhieu, G.2    Hanada, K.3    Sansonetti, P.4    Van Der Goot, F.G.5
  • 19
    • 30044445766 scopus 로고    scopus 로고
    • The needle component of the type III secreton of Shigella regulates the activity of the secretion apparatus
    • Kenjale, R., Wilson, J., Zenk, S. F., Saurya, S., Picking, W. L., Picking, W. D., and Blocker, A. (2005) The needle component of the type III secreton of Shigella regulates the activity of the secretion apparatus J. Biol. Chem. 280, 42929-42937
    • (2005) J. Biol. Chem. , vol.280 , pp. 42929-42937
    • Kenjale, R.1    Wilson, J.2    Zenk, S.F.3    Saurya, S.4    Picking, W.L.5    Picking, W.D.6    Blocker, A.7
  • 20
    • 0035181397 scopus 로고    scopus 로고
    • Identification of functional regions within invasion plasmid antigen C (IpaC) of Shigella flexneri
    • Picking, W. L., Coye, L., Osiecki, J. C., Barnoski Serfis, A., Schaper, E., and Picking, W. D. (2001) Identification of functional regions within invasion plasmid antigen C (IpaC) of Shigella flexneri Mol. Microbiol. 39, 100-111
    • (2001) Mol. Microbiol. , vol.39 , pp. 100-111
    • Picking, W.L.1    Coye, L.2    Osiecki, J.C.3    Barnoski Serfis, A.4    Schaper, E.5    Picking, W.D.6
  • 21
    • 15544376398 scopus 로고    scopus 로고
    • IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes
    • Picking, W. L., Nishioka, H., Hearn, P. D., Baxter, M. A., Harrington, A. T., Blocker, A., and Picking, W. D. (2005) IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes Infect. Immun. 73, 1432-1440
    • (2005) Infect. Immun. , vol.73 , pp. 1432-1440
    • Picking, W.L.1    Nishioka, H.2    Hearn, P.D.3    Baxter, M.A.4    Harrington, A.T.5    Blocker, A.6    Picking, W.D.7
  • 22
    • 12344296442 scopus 로고    scopus 로고
    • Dynamic motion of helix A in the amino-terminal domain of calmodulin is stabilized upon calcium activation
    • Chen, B., Mayer, M. U., Markillie, L. M., Stenoien, D. L., and Squier, T. C. (2005) Dynamic motion of helix A in the amino-terminal domain of calmodulin is stabilized upon calcium activation Biochemistry 44, 905-914
    • (2005) Biochemistry , vol.44 , pp. 905-914
    • Chen, B.1    Mayer, M.U.2    Markillie, L.M.3    Stenoien, D.L.4    Squier, T.C.5
  • 23
    • 34250376066 scopus 로고    scopus 로고
    • Structure and conformational changes in the C-terminal domain of the beta2-adrenoceptor: Insights from fluorescence resonance energy transfer studies
    • Granier, S., Kim, S., Shafer, A. M., Ratnala, V. R., Fung, J. J., Zare, R. N., and Kobilka, B. (2007) Structure and conformational changes in the C-terminal domain of the beta2-adrenoceptor: insights from fluorescence resonance energy transfer studies J. Biol. Chem. 282, 13895-13905
    • (2007) J. Biol. Chem. , vol.282 , pp. 13895-13905
    • Granier, S.1    Kim, S.2    Shafer, A.M.3    Ratnala, V.R.4    Fung, J.J.5    Zare, R.N.6    Kobilka, B.7
  • 24
    • 4644225722 scopus 로고    scopus 로고
    • Heterologous RNA encapsidated in Pariacoto virus-like particles forms a dodecahedral cage similar to genomic RNA in wild-type virions
    • Johnson, K. N., Tang, L., Johnson, J. E., and Ball, L. A. (2004) Heterologous RNA encapsidated in Pariacoto virus-like particles forms a dodecahedral cage similar to genomic RNA in wild-type virions J. Virol. 78, 11371-11378
    • (2004) J. Virol. , vol.78 , pp. 11371-11378
    • Johnson, K.N.1    Tang, L.2    Johnson, J.E.3    Ball, L.A.4
  • 26
    • 0032162021 scopus 로고    scopus 로고
    • Sensitivity enhancement in the TROSY experiment
    • Czisch, M. and Boelens, R. (1998) Sensitivity enhancement in the TROSY experiment J. Magn. Reson. 134, 158-160
    • (1998) J. Magn. Reson. , vol.134 , pp. 158-160
    • Czisch, M.1    Boelens, R.2
  • 27
    • 0033518575 scopus 로고    scopus 로고
    • TROSY-type triple resonance experiments for sequential NMR assignments of large proteins
    • Salzmann, M., Wider, G., Pervushin, K., Senn, H., and Wuthrich, K. (1999) TROSY-type triple resonance experiments for sequential NMR assignments of large proteins J. Am. Chem. Soc. 121, 844-848
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 844-848
    • Salzmann, M.1    Wider, G.2    Pervushin, K.3    Senn, H.4    Wuthrich, K.5
  • 28
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
    • Salzmann, M., Pervushin, K., Wider, G., Senn, H., and Wuthrich, K. (1998) TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins Proc. Natl. Acad. Sci. U.S.A. 95, 13585-13590
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wuthrich, K.5
  • 30
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., Riek, R., Wider, G., and Wuthrich, K. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 31
    • 0028072943 scopus 로고
    • The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD
    • Menard, R., Sansonetti, P., and Parsot, C. (1994) The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD EMBO J. 13, 5293-5302
    • (1994) EMBO J. , vol.13 , pp. 5293-5302
    • Menard, R.1    Sansonetti, P.2    Parsot, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.