메뉴 건너뛰기




Volumn 193, Issue 2, 2016, Pages 132-140

Structure-based functional studies for the cellular recognition and cytolytic mechanism of pneumolysin from Streptococcus pneumoniae

Author keywords

Cellular recognition; Cholesterol dependent cytolysin; Molecular docking; Pneumolysin; X ray structure

Indexed keywords

CELL SURFACE RECEPTOR; CHOLESTEROL; LEUCINE; MANNOSE; MONOMER; PNEUMOLYSIN; TRYPTOPHAN; BACTERIAL PROTEIN; PLY PROTEIN, STREPTOCOCCUS PNEUMONIAE; STREPTOLYSIN;

EID: 84957441369     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2015.12.002     Document Type: Article
Times cited : (17)

References (40)
  • 2
    • 0029684150 scopus 로고    scopus 로고
    • Site-directed mutagenesis using double-stranded plasmid DNA templates
    • Braman J., Papworth C., Greener A. Site-directed mutagenesis using double-stranded plasmid DNA templates. Methods Mol. Biol. 1996, 57:31-44.
    • (1996) Methods Mol. Biol. , vol.57 , pp. 31-44
    • Braman, J.1    Papworth, C.2    Greener, A.3
  • 4
    • 84864593970 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly
    • Dowd K.J., Tweten R.K. The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly. PLoS Pathog. 2012, 8:e1002787.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002787
    • Dowd, K.J.1    Tweten, R.K.2
  • 6
    • 77749292162 scopus 로고    scopus 로고
    • Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
    • Farrand A.J., LaChapelle S., Hotze E.M., Johnson A.E., Tweten R.K. Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc. Natl. Acad. Sci. USA 2010, 107:4341-4346.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 4341-4346
    • Farrand, A.J.1    LaChapelle, S.2    Hotze, E.M.3    Johnson, A.E.4    Tweten, R.K.5
  • 7
    • 84893639595 scopus 로고    scopus 로고
    • Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration
    • Feil S.C., Ascher D.B., Kuiper M.J., Tweten R.K., Parker M.W. Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration. J. Mol. Biol. 2014, 426:785-792.
    • (2014) J. Mol. Biol. , vol.426 , pp. 785-792
    • Feil, S.C.1    Ascher, D.B.2    Kuiper, M.J.3    Tweten, R.K.4    Parker, M.W.5
  • 8
    • 16544370492 scopus 로고    scopus 로고
    • Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin
    • Giddings K.S., Zhao J., Sims P.J., Tweten R.K. Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin. Nat. Struct. Mol. Biol. 2004, 11:1173-1178.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1173-1178
    • Giddings, K.S.1    Zhao, J.2    Sims, P.J.3    Tweten, R.K.4
  • 9
    • 84906313649 scopus 로고    scopus 로고
    • Structural features of cholesterol dependent cytolysins and comparison to other MACPF-domain containing proteins
    • Gilbert R. Structural features of cholesterol dependent cytolysins and comparison to other MACPF-domain containing proteins. Subcell. Biochem. 2014, 80:47-62.
    • (2014) Subcell. Biochem. , vol.80 , pp. 47-62
    • Gilbert, R.1
  • 10
    • 0020656535 scopus 로고
    • Failure of intensive care unit support to influence mortality from pneumococcal bacteremia
    • Hook E.W., Horton C.A., Schaberg D.R. Failure of intensive care unit support to influence mortality from pneumococcal bacteremia. JAMA 1983, 249:1055-1057.
    • (1983) JAMA , vol.249 , pp. 1055-1057
    • Hook, E.W.1    Horton, C.A.2    Schaberg, D.R.3
  • 11
    • 0020071103 scopus 로고
    • Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein toxin
    • Howard S.P., Buckley J.T. Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein toxin. Biochemistry 1982, 21:1662-1667.
    • (1982) Biochemistry , vol.21 , pp. 1662-1667
    • Howard, S.P.1    Buckley, J.T.2
  • 13
    • 0017253682 scopus 로고
    • Ganglioside and rabbit erythrocyte membrane receptor for staphylococcal alpha-toxin
    • Kato I., Naiki M. Ganglioside and rabbit erythrocyte membrane receptor for staphylococcal alpha-toxin. Infect. Immun. 1976, 13:289-291.
    • (1976) Infect. Immun. , vol.13 , pp. 289-291
    • Kato, I.1    Naiki, M.2
  • 14
    • 0032007852 scopus 로고    scopus 로고
    • A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers
    • Korchev Y.E., Bashford C.L., Pederzolli C., Pasternak C.A., Morgan P.J., Andrew P.W., Mitchell T.J. A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers. Biochem. J. 1998, 329(Pt 3):571-577.
    • (1998) Biochem. J. , vol.329 , pp. 571-577
    • Korchev, Y.E.1    Bashford, C.L.2    Pederzolli, C.3    Pasternak, C.A.4    Morgan, P.J.5    Andrew, P.W.6    Mitchell, T.J.7
  • 15
    • 0023240763 scopus 로고
    • Pneumococcal bacteremia-no change in mortality in 30 years: analysis of 104 cases and review of the literature
    • Kramer M.R., Rudensky B., Hadas-Halperin I., Isacsohn M., Melzer E. Pneumococcal bacteremia-no change in mortality in 30 years: analysis of 104 cases and review of the literature. Isr. J. Med. Sci. 1987, 23:174-180.
    • (1987) Isr. J. Med. Sci. , vol.23 , pp. 174-180
    • Kramer, M.R.1    Rudensky, B.2    Hadas-Halperin, I.3    Isacsohn, M.4    Melzer, E.5
  • 16
  • 17
    • 84872358998 scopus 로고    scopus 로고
    • Characterization of pneumolysin from Streptococcus pneumoniae, interacting with carbohydrate moiety and cholesterol as a component of cell membrane
    • Lim J.E., Park S.A., Bong S.M., Chi Y.M., Lee K.S. Characterization of pneumolysin from Streptococcus pneumoniae, interacting with carbohydrate moiety and cholesterol as a component of cell membrane. Biochem. Biophys. Res. Commun. 2013, 430:659-663.
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 659-663
    • Lim, J.E.1    Park, S.A.2    Bong, S.M.3    Chi, Y.M.4    Lee, K.S.5
  • 18
    • 0025685253 scopus 로고
    • Attenuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitutions in listeriolysin O
    • Michel E., Reich K.A., Favier R., Berche P., Cossart P. Attenuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitutions in listeriolysin O. Mol. Microbiol. 1990, 4:2167-2178.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2167-2178
    • Michel, E.1    Reich, K.A.2    Favier, R.3    Berche, P.4    Cossart, P.5
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 0024720325 scopus 로고
    • The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity
    • Pinkney M., Beachey E., Kehoe M. The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity. Infect. Immun. 1989, 57:2553-2558.
    • (1989) Infect. Immun. , vol.57 , pp. 2553-2558
    • Pinkney, M.1    Beachey, E.2    Kehoe, M.3
  • 23
    • 14144251524 scopus 로고    scopus 로고
    • Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin
    • Polekhina G., Giddings K.S., Tweten R.K., Parker M.W. Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin. Proc. Natl. Acad. Sci. USA 2005, 102:600-605.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 600-605
    • Polekhina, G.1    Giddings, K.S.2    Tweten, R.K.3    Parker, M.W.4
  • 25
    • 0036830653 scopus 로고    scopus 로고
    • Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
    • Ramachandran R., Heuck A.P., Tweten R.K., Johnson A.E. Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nat. Struct. Biol. 2002, 9:823-827.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 823-827
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 26
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert X., Gouet P. Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res. 2014, 42:W320-324.
    • (2014) Nucleic Acids Res. , vol.42 , pp. W320-324
    • Robert, X.1    Gouet, P.2
  • 27
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn J., Feil S.C., McKinstry W.J., Tweten R.K., Parker M.W. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 1997, 89:685-692.
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 28
    • 0031017025 scopus 로고    scopus 로고
    • Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle
    • Saha N., Banerjee K.K. Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle. J. Biol. Chem. 1997, 272:162-167.
    • (1997) J. Biol. Chem. , vol.272 , pp. 162-167
    • Saha, N.1    Banerjee, K.K.2
  • 29
    • 0033397980 scopus 로고    scopus 로고
    • Python: a programming language for software integration and development
    • Sanner M.F. Python: a programming language for software integration and development. J. Mol. Graph. Model 1999, 17:57-61.
    • (1999) J. Mol. Graph. Model , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 30
    • 0024407229 scopus 로고
    • Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity
    • Saunders F.K., Mitchell T.J., Walker J.A., Andrew P.W., Boulnois G.J. Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity. Infect. Immun. 1989, 57:2547-2552.
    • (1989) Infect. Immun. , vol.57 , pp. 2547-2552
    • Saunders, F.K.1    Mitchell, T.J.2    Walker, J.A.3    Andrew, P.W.4    Boulnois, G.J.5
  • 31
    • 79955574923 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System
    • Version 1.3r1.
    • Schrodinger, LLC. 2010. The PyMOL Molecular Graphics System, Version 1.3r1.
    • (2010)
  • 32
    • 0029972377 scopus 로고    scopus 로고
    • Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin
    • Sekino-Suzuki N., Nakamura M., Mitsui K.I., Ohno-Iwashita Y. Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin. Eur. J. Biochem. 1996, 241:941-947.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 941-947
    • Sekino-Suzuki, N.1    Nakamura, M.2    Mitsui, K.I.3    Ohno-Iwashita, Y.4
  • 34
    • 34447536854 scopus 로고    scopus 로고
    • Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin
    • Soltani C.E., Hotze E.M., Johnson A.E., Tweten R.K. Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin. J. Biol. Chem. 2007, 282:15709-15716.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15709-15716
    • Soltani, C.E.1    Hotze, E.M.2    Johnson, A.E.3    Tweten, R.K.4
  • 35
    • 38049125626 scopus 로고    scopus 로고
    • Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions
    • Soltani C.E., Hotze E.M., Johnson A.E., Tweten R.K. Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions. Proc. Natl. Acad. Sci. USA 2007, 104:20226-20231.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20226-20231
    • Soltani, C.E.1    Hotze, E.M.2    Johnson, A.E.3    Tweten, R.K.4
  • 36
    • 84875956336 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cells
    • Taylor S.D., Sanders M.E., Tullos N.A., Stray S.J., Norcross E.W., McDaniel L.S., Marquart M.E. The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cells. PLoS One 2013, 8:e61300.
    • (2013) PLoS One , vol.8 , pp. e61300
    • Taylor, S.D.1    Sanders, M.E.2    Tullos, N.A.3    Stray, S.J.4    Norcross, E.W.5    McDaniel, L.S.6    Marquart, M.E.7
  • 37
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • Tweten R.K. Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect. Immun. 2005, 73:6199-6209.
    • (2005) Infect. Immun. , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 40
    • 79953148352 scopus 로고    scopus 로고
    • Crystal structure of cytotoxin protein suilysin from Streptococcus suis
    • Xu L., Huang B., Du H., Zhang X.C., Xu J., Li X., Rao Z. Crystal structure of cytotoxin protein suilysin from Streptococcus suis. Protein Cell 2010, 1:96-105.
    • (2010) Protein Cell , vol.1 , pp. 96-105
    • Xu, L.1    Huang, B.2    Du, H.3    Zhang, X.C.4    Xu, J.5    Li, X.6    Rao, Z.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.