메뉴 건너뛰기




Volumn 394, Issue 1, 2006, Pages 217-225

Homologous versus heterologous interactions in the bicomponent staphylococcal γ-haemolysin pore

Author keywords

Fluorescence resonance energy transfer (FRET); Leucotoxin; Oligomerization; Pore forming toxin; Protein protein interaction; Staphylococcus aureus

Indexed keywords

FLUORESCENCE; INTERFACES (COMPUTER); MONOMERS; OLIGOMERS; PROTEINS; TOPOLOGY;

EID: 32944470382     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051210     Document Type: Article
Times cited : (12)

References (40)
  • 1
    • 0035884894 scopus 로고    scopus 로고
    • Development and spread of bacterial resistance to antimicrobial agents: An overview
    • Tenover, F. C. (2001) Development and spread of bacterial resistance to antimicrobial agents: an overview. Clin. Infect. Dis. 33, S108-S115
    • (2001) Clin. Infect. Dis. , vol.33
    • Tenover, F.C.1
  • 2
    • 0034792586 scopus 로고    scopus 로고
    • Curtailing unnecessary vancomycin usage in a hospital with high rates of methicillin resistant Staphylococcus aureus infections
    • Kumana, C. R., Ching, T. Y., Kong, Y., Ma, E. C. W., Kou, M., Lee, R. A., Cheng, V. C. C., Chiu, S. S. and Seto, W. H. (2001) Curtailing unnecessary vancomycin usage in a hospital with high rates of methicillin resistant Staphylococcus aureus infections. Br. J. Clin. Pharmacol. 52, 427-432
    • (2001) Br. J. Clin. Pharmacol. , vol.52 , pp. 427-432
    • Kumana, C.R.1    Ching, T.Y.2    Kong, Y.3    Ma, E.C.W.4    Kou, M.5    Lee, R.A.6    Cheng, V.C.C.7    Chiu, S.S.8    Seto, W.H.9
  • 3
  • 4
    • 0034869444 scopus 로고    scopus 로고
    • Mode of action of beta-barrel pore-forming toxins of the staphylococcal gamma-hemolysin family
    • Menestrina, G., Dalla Serra, M. and Prévost, G. (2001) Mode of action of beta-barrel pore-forming toxins of the staphylococcal gamma-hemolysin family. Toxicon 39, 1661-1672
    • (2001) Toxicon , vol.39 , pp. 1661-1672
    • Menestrina, G.1    Dalla Serra, M.2    Prévost, G.3
  • 5
    • 32944459815 scopus 로고    scopus 로고
    • Toxins in Staphylococcus aureus pathogenesis
    • (Thomas, P., ed.), Horizon Bioscience, Norfolk, U.K.
    • Prévost, G. (2005) Toxins in Staphylococcus aureus pathogenesis. In Microbial Toxins: Molecular and Cellular Biology (Thomas, P., ed.), pp. 243-283, Horizon Bioscience, Norfolk, U.K.
    • (2005) Microbial Toxins: Molecular and Cellular Biology , pp. 243-283
    • Prévost, G.1
  • 6
    • 0036015641 scopus 로고    scopus 로고
    • Protein engineering modulates the transport properties and ion selectivity of the pores formed by staphylococcal gamma-hemolysins in lipid membranes
    • Comai, M., Dalla Serra, M., Coraiola, M., Werner, S., Colin, D. A., Prévost, G. and Menestrina, G. (2002) Protein engineering modulates the transport properties and ion selectivity of the pores formed by staphylococcal gamma-hemolysins in lipid membranes. Mol. Microbiol. 44, 1251-1268
    • (2002) Mol. Microbiol. , vol.44 , pp. 1251-1268
    • Comai, M.1    Dalla Serra, M.2    Coraiola, M.3    Werner, S.4    Colin, D.A.5    Prévost, G.6    Menestrina, G.7
  • 8
    • 0035942992 scopus 로고    scopus 로고
    • The staphylococcal leukocidin bicomponent toxin forms large ionic channels
    • Miles, G., Cheley, S., Braha, O. and Bayley, H. (2001) The staphylococcal leukocidin bicomponent toxin forms large ionic channels. Biochemistry 40, 8514-8522
    • (2001) Biochemistry , vol.40 , pp. 8514-8522
    • Miles, G.1    Cheley, S.2    Braha, O.3    Bayley, H.4
  • 9
    • 0036128759 scopus 로고    scopus 로고
    • Subunit composition of a bicomponent toxin: Staphylococcal leukocidin forms an octameric transmembrane pore
    • Miles, G., Movileanu, L. and Bayley, H. (2002) Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore. Protein Sci. 11, 894-902
    • (2002) Protein Sci. , vol.11 , pp. 894-902
    • Miles, G.1    Movileanu, L.2    Bayley, H.3
  • 11
    • 4644355909 scopus 로고    scopus 로고
    • Crystal structure of leucotoxin S component: New insight into the staphylococcal beta-barrel pore-forming toxins
    • Guillet, V., Roblin, P., Werner, S., Coraiola, M., Menestrina, G., Monteil, H., Prévost, G. and Mourey, L. (2004) Crystal structure of leucotoxin S component: new insight into the staphylococcal beta-barrel pore-forming toxins. J. Biol. Chem. 279, 41028-41037
    • (2004) J. Biol. Chem. , vol.279 , pp. 41028-41037
    • Guillet, V.1    Roblin, P.2    Werner, S.3    Coraiola, M.4    Menestrina, G.5    Monteil, H.6    Prévost, G.7    Mourey, L.8
  • 13
    • 0032508971 scopus 로고    scopus 로고
    • The interaction of Staphylococcus aureus bi-component gamma hemolysins and leucocidins with cells and model membranes
    • Ferreras, M., Hoeper, F., Dalla Serra, M., Colin, D. A., Prévost, G. and Menestrina, G. (1998) The interaction of Staphylococcus aureus bi-component gamma hemolysins and leucocidins with cells and model membranes. Biochim. Biophys. Acta 1414, 108-126
    • (1998) Biochim. Biophys. Acta , vol.1414 , pp. 108-126
    • Ferreras, M.1    Hoeper, F.2    Dalla Serra, M.3    Colin, D.A.4    Prévost, G.5    Menestrina, G.6
  • 14
    • 0030987870 scopus 로고    scopus 로고
    • A predicted β-sheet from class S components of staphylococcal gamma-hemolysins is essential for the secondary interaction of the class F component
    • Meunier, O., Ferreras, M., Supersac, G., Hoeper, F., Baba-Moussa, L., Monteil, H., Colin, D. A., Menestrina, G. and Prévost, G. (1997) A predicted β-sheet from class S components of staphylococcal gamma-hemolysins is essential for the secondary interaction of the class F component. Biochim. Biophys. Acta 1326, 275-286
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 275-286
    • Meunier, O.1    Ferreras, M.2    Supersac, G.3    Hoeper, F.4    Baba-Moussa, L.5    Monteil, H.6    Colin, D.A.7    Menestrina, G.8    Prévost, G.9
  • 15
    • 0030740555 scopus 로고    scopus 로고
    • Assembly of Staphylococcus aureus gamma-hemolysin into a pore-forming ring-shaped complex on the surface of human erythrocytes
    • Sugawara, N., Tomita, T. and Kamio, Y. (1997) Assembly of Staphylococcus aureus gamma-hemolysin into a pore-forming ring-shaped complex on the surface of human erythrocytes. FEBS Lett. 410, 333-337
    • (1997) FEBS Lett. , vol.410 , pp. 333-337
    • Sugawara, N.1    Tomita, T.2    Kamio, Y.3
  • 16
    • 0036716731 scopus 로고    scopus 로고
    • Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3
    • Sugawara-Tomita, N., Tomita, T. and Kamio, Y. (2002) Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3. J. Bacteriol. 184, 4747-4756
    • (2002) J. Bacteriol. , vol.184 , pp. 4747-4756
    • Sugawara-Tomita, N.1    Tomita, T.2    Kamio, Y.3
  • 17
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of transmembrane channel
    • Olson, R., Nariya, H., Yokota, K., Kamio, Y. and Gouaux, J. E. (1999) Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of transmembrane channel. Nat. Struct. Biol. 6, 134-140
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, J.E.5
  • 18
    • 0033103175 scopus 로고    scopus 로고
    • The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
    • Pédelacq, J. D., Maveyraud, L., Prévost, G., Baba-Moussa, L., Gonzalez, A., Courcelle, E., Shepard, W., Monteil, H., Samama, J. P. and Mourey, L. (1999) The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins. Structure 7, 277-287
    • (1999) Structure , vol.7 , pp. 277-287
    • Pédelacq, J.D.1    Maveyraud, L.2    Prévost, G.3    Baba-Moussa, L.4    Gonzalez, A.5    Courcelle, E.6    Shepard, W.7    Monteil, H.8    Samama, J.P.9    Mourey, L.10
  • 19
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H. and Gouaux, J. E. (1996) Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 20
    • 0141530906 scopus 로고    scopus 로고
    • Single-molecule imaging of cooperative assembly of gamma-hemolysin on erythrocyte membranes
    • Nguyen, V. T., Kamio, Y. and Higuchi, H. (2003) Single-molecule imaging of cooperative assembly of gamma-hemolysin on erythrocyte membranes. EMBO J. 22, 4968-4979
    • (2003) EMBO J. , vol.22 , pp. 4968-4979
    • Nguyen, V.T.1    Kamio, Y.2    Higuchi, H.3
  • 22
    • 0032476021 scopus 로고    scopus 로고
    • Characterization of a novel structural member, LukE-LukD, of the bi-component staphylococcal leucotoxins family
    • Gravet, A., Colin, D. A., Keller, D., Girardot, R., Monteil, H. and Prévost, G. (1998) Characterization of a novel structural member, LukE-LukD, of the bi-component staphylococcal leucotoxins family. FEBS Lett. 436, 202-208
    • (1998) FEBS Lett. , vol.436 , pp. 202-208
    • Gravet, A.1    Colin, D.A.2    Keller, D.3    Girardot, R.4    Monteil, H.5    Prévost, G.6
  • 24
    • 0035004910 scopus 로고    scopus 로고
    • Effects of lipid composition on membrane permeabilization by Sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus
    • Alvarez, C., Dalla Serra, M., Potrich, C., Bernhart, I., Tejuca, M., Martinez, D., Pazos, I. F., Lanio, M. E. and Menestrina, G. (2001) Effects of lipid composition on membrane permeabilization by Sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus. Biophys. J. 80, 2761-2774
    • (2001) Biophys. J. , vol.80 , pp. 2761-2774
    • Alvarez, C.1    Dalla Serra, M.2    Potrich, C.3    Bernhart, I.4    Tejuca, M.5    Martinez, D.6    Pazos, I.F.7    Lanio, M.E.8    Menestrina, G.9
  • 25
    • 0035942337 scopus 로고    scopus 로고
    • Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: An alternative model based on fluorescence resonance energy transfer experiments
    • Tricerri, M. A., Behling Agree, A. K., Sanchez, S. A., Bronski, J. and Jonas, A. (2001) Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments. Biochemistry 40, 5065-5074
    • (2001) Biochemistry , vol.40 , pp. 5065-5074
    • Tricerri, M.A.1    Behling Agree, A.K.2    Sanchez, S.A.3    Bronski, J.4    Jonas, A.5
  • 26
    • 0001252358 scopus 로고    scopus 로고
    • Energy transfer
    • Kluwer Academic/Plenum Publishers, New York
    • Lakowicz, J. R. (1999) Energy transfer. In Principles of Fluorescence Spectroscopy, pp. 368-391, Kluwer Academic/Plenum Publishers, New York
    • (1999) Principles of Fluorescence Spectroscopy , pp. 368-391
    • Lakowicz, J.R.1
  • 27
    • 0028884014 scopus 로고
    • Fluorescence resonance energy transfer spectroscopy is a reliable 'ruler' for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor
    • dos Remedios, C. G. and Moens, P. D. (1995) Fluorescence resonance energy transfer spectroscopy is a reliable 'ruler' for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor. J. Struct. Biol. 115, 175-185
    • (1995) J. Struct. Biol. , vol.115 , pp. 175-185
    • Dos Remedios, C.G.1    Moens, P.D.2
  • 28
    • 0037418210 scopus 로고    scopus 로고
    • A fluorescence resonance energy transfer sensor for the beta-domain of metallothionein
    • Hong, S. H. and Maret, W. (2003) A fluorescence resonance energy transfer sensor for the beta-domain of metallothionein. Proc. Natl. Acad. Sci. U.S.A. 100, 2255-2260
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 2255-2260
    • Hong, S.H.1    Maret, W.2
  • 29
    • 0030770425 scopus 로고    scopus 로고
    • Protein S alters the active site location of activated protein C above the membrane surface. A fluorescence resonance energy transfer study of topography
    • Yegneswaran, S., Wood, G. M., Esmon, C. T. and Johnson, A. E. (1997) Protein S alters the active site location of activated protein C above the membrane surface. A fluorescence resonance energy transfer study of topography. J. Biol. Chem. 272, 25013-25021
    • (1997) J. Biol. Chem. , vol.272 , pp. 25013-25021
    • Yegneswaran, S.1    Wood, G.M.2    Esmon, C.T.3    Johnson, A.E.4
  • 30
    • 0026640565 scopus 로고
    • Orientation factor in steady-state and time-resolved resonance energy transfer measurements
    • Wu, P. and Brand, L. (1992) Orientation factor in steady-state and time-resolved resonance energy transfer measurements. Biochemistry 31, 7939-7947
    • (1992) Biochemistry , vol.31 , pp. 7939-7947
    • Wu, P.1    Brand, L.2
  • 31
    • 0033125070 scopus 로고    scopus 로고
    • Assembly of Staphylococcus aureus leukocidin into a pore-forming ring-shaped oligomer on human polymorphonuclear leukocytes and rabbit erythrocytes
    • Sugawara, N., Tomita, T., Sato, T. and Kamio, Y. (1999) Assembly of Staphylococcus aureus leukocidin into a pore-forming ring-shaped oligomer on human polymorphonuclear leukocytes and rabbit erythrocytes. Biosci. Biotechnol. Biochem. 63, 884-891
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 884-891
    • Sugawara, N.1    Tomita, T.2    Sato, T.3    Kamio, Y.4
  • 32
    • 0033105888 scopus 로고    scopus 로고
    • Heptameric structures of two alpha-hemolysin mutants imaged with in situ atomic force microscopy
    • Malghani, M. S., Fang, Y., Cheley, S., Bayley, H. and Yang, J. (1999) Heptameric structures of two alpha-hemolysin mutants imaged with in situ atomic force microscopy. Microsc. Res. Tech. 44, 353-356
    • (1999) Microsc. Res. Tech. , vol.44 , pp. 353-356
    • Malghani, M.S.1    Fang, Y.2    Cheley, S.3    Bayley, H.4    Yang, J.5
  • 33
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers
    • Czajkowsky, D. M., Sheng, S. T. and Shao, Z. F. (1998) Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers. J. Mol. Biol. 276, 325-330
    • (1998) J. Mol. Biol. , vol.276 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.T.2    Shao, Z.F.3
  • 34
    • 0000056380 scopus 로고
    • Resonance energy transfer
    • (Lakowicz, J. R., ed.), Plenum Press, New York
    • Cheung, H. C. (1991) Resonance Energy Transfer. In Topics in Fluorescence Spectroscopy. Principles (Lakowicz, J. R., ed.), pp. 127-176, Plenum Press, New York
    • (1991) Topics in Fluorescence Spectroscopy. Principles , pp. 127-176
    • Cheung, H.C.1
  • 35
    • 0025042733 scopus 로고
    • Mechanism of leakage of phospholipid vesicle contents induced by the peptide GALA
    • Parente, R. A., Nir, S. and Szoka, Jr, F. C. (1990) Mechanism of leakage of phospholipid vesicle contents induced by the peptide GALA. Biochemistry 29, 8720-8728
    • (1990) Biochemistry , vol.29 , pp. 8720-8728
    • Parente, R.A.1    Nir, S.2    Szoka Jr., F.C.3
  • 36
    • 0030025781 scopus 로고    scopus 로고
    • Reversible surface aggregation in pore formation by pardaxin
    • Rapaport, D., Peled, R., Nir, S. and Shai, Y. (1996) Reversible surface aggregation in pore formation by pardaxin. Biophys. J. 70, 2502-2512
    • (1996) Biophys. J. , vol.70 , pp. 2502-2512
    • Rapaport, D.1    Peled, R.2    Nir, S.3    Shai, Y.4
  • 40
    • 0028072693 scopus 로고
    • Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer
    • Gohlke, C., Murchie, A. I., Lilley, D. M. and Clegg, R. M. (1994) Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. U.S.A. 91, 11660-11664
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11660-11664
    • Gohlke, C.1    Murchie, A.I.2    Lilley, D.M.3    Clegg, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.