메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARBOHYDRATE; MANNOSE; PLY PROTEIN, STREPTOCOCCUS PNEUMONIAE; PROTEIN BINDING; SOLUTION AND SOLUBILITY; STREPTOLYSIN;

EID: 84942755927     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep14352     Document Type: Article
Times cited : (62)

References (63)
  • 1
    • 0034516706 scopus 로고    scopus 로고
    • Epidemiology of invasive and other pneumococcal diseases in children in England and Wales 1996-1998
    • Miller, E., Waight, P., Efstratiou, A., Brisson, M., Johnson, A. Epidemiology of invasive and other pneumococcal diseases in children in England and Wales 1996-1998. Acta Paediatr. Suppl. 89, 11-16 (2000).
    • (2000) Acta Paediatr. Suppl. , vol.89 , pp. 11-16
    • Miller, E.1    Waight, P.2    Efstratiou, A.3    Brisson, M.4    Johnson, A.5
  • 3
    • 3543016107 scopus 로고    scopus 로고
    • Membrane dependent conformational changes initiate cholesterol-dependent cytolysin oligomerisation and intersubunit beta-strand alignment
    • Ramachandran, R., Heuck, A. P., Tweten, R. K., Johnson, A. E. Membrane dependent conformational changes initiate cholesterol-dependent cytolysin oligomerisation and intersubunit beta-strand alignment. Nat. Struct. Biol. 11, 697-705 (2004).
    • (2004) Nat. Struct. Biol. , vol.11 , pp. 697-705
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 4
    • 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. 73, 6199-6209 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 5
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol activated pore-forming toxins: Clostridium perfringens, perfringolysin O: An alpha helical to beta-sheet transition identified by fluorescence spectroscopy
    • Shepard, L. A. et al. Identification of a membrane-spanning domain of the thiol activated pore-forming toxins: Clostridium perfringens, perfringolysin O: an alpha helical to beta-sheet transition identified by fluorescence spectroscopy. Biochemistry 37, 14563-14574 (1998).
    • (1998) Biochemistry , vol.37 , pp. 14563-14574
    • Shepard, L.A.1
  • 6
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for poreforming toxins
    • Shatursky, O. et al. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for poreforming toxins. Cell 99, 293-299 (1999).
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1
  • 7
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • Tilley, S. J., Orlova, E. V., Andrew, P. W., Saibil, H. R. Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121, 247-256 (2005).
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Andrew, P.W.3    Saibil, H.R.4
  • 8
    • 0141706347 scopus 로고    scopus 로고
    • Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins
    • Giddings, K. S., Johnson, A. E., Tweten, R. K. Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins. Proc. Natl. Acad. Sci. USA 100, 11315-11320 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11315-11320
    • Giddings, K.S.1    Johnson, A.E.2    Tweten, R.K.3
  • 9
    • 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 107, 4341-4346 (2010).
    • (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
  • 10
    • 84882891979 scopus 로고    scopus 로고
    • Repertoire and general feature of the family of cholesterol-dependent cytolysins
    • (eds Alouf, J. E., Popoff, M. R.) (Acadamic Press, Oxford, England
    • Alouf, J. E., Billington, S. J., Jost, B. H. Repertoire and general feature of the family of cholesterol-dependent cytolysins in The Comprehensive Sourcebook Of Bacterial Protein Toxins (eds Alouf, J. E., Popoff, M. R.) 643-658 (Acadamic Press, Oxford, England, 2005).
    • (2005) The Comprehensive Sourcebook of Bacterial Protein Toxins , pp. 643-658
    • Alouf, J.E.1    Billington, S.J.2    Jost, B.H.3
  • 11
    • 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. Nature Struct. Biol. 9, 823-827 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 823-827
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 12
    • 2142825136 scopus 로고    scopus 로고
    • The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin
    • Nollmann, M., Gilbert, R., Mitcell, T., Sferrazza, M., Byron, O. The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin. Biophys. J. 86, 3141-3151 (2004).
    • (2004) Biophys. J. , vol.86 , pp. 3141-3151
    • Nollmann, M.1    Gilbert, R.2    Mitcell, T.3    Sferrazza, M.4    Byron, O.5
  • 13
    • 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., Farrand, A. 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. 8, e1002787 (2012).
    • (2012) PLoS Pathog. , vol.8 , pp. e1002787
    • Dowd, K.J.1    Farrand, A.J.2    Tweten, R.K.3
  • 14
    • 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. 11, 1173-1177 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1173-1177
    • Giddings, K.S.1    Zhao, J.2    Sims, P.J.3    Tweten, R.K.4
  • 15
    • 34548666167 scopus 로고    scopus 로고
    • A common fold mediates vertebrate defense and bacterial attack
    • Rosado, C. J. et al. A common fold mediates vertebrate defense and bacterial attack. Science 317, 1548-1551 (2007).
    • (2007) Science , vol.317 , pp. 1548-1551
    • Rosado, C.J.1
  • 16
    • 34548670476 scopus 로고    scopus 로고
    • Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense
    • Hadders, M. A., Beringer, D. X., Gros, P. Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense. Science 317, 1552-1554 (2007).
    • (2007) Science , vol.317 , pp. 1552-1554
    • Hadders, M.A.1    Beringer, D.X.2    Gros, P.3
  • 17
    • 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 102, 600-605 (2005).
    • (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
  • 18
    • 79957978193 scopus 로고    scopus 로고
    • Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8? and C9
    • Wickham, S. E. et al. Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8? and C9. J. Biol. Chem. 286, 20952-20962 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 20952-20962
    • Wickham, S.E.1
  • 19
    • 84878591801 scopus 로고    scopus 로고
    • Structural basis for recognition of the pore-forming toxin intermedilysin by human complement receptor CD59
    • Johnson, S., Brooks, N. J., Smith, R. A., Lea, S. M., Bubeck, D. Structural basis for recognition of the pore-forming toxin intermedilysin by human complement receptor CD59. Cell Rep. 3, 1369-1377 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 1369-1377
    • Johnson, S.1    Brooks, N.J.2    Smith, R.A.3    Lea, S.M.4    Bubeck, D.5
  • 20
    • 84917694808 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysins pneumolysin and streptolysin O require binding to red blood cell glycans for hemolytic activity
    • Shewell, L. K. et al. The cholesterol-dependent cytolysins pneumolysin and streptolysin O require binding to red blood cell glycans for hemolytic activity. Proc. Natl. Acad. Sci. USA 111, E5312-20 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E5312-E5320
    • Shewell, L.K.1
  • 21
    • 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. Communs. 430, 659-663 (2012).
    • (2012) Biochem. Biophys. Res. Communs. , 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
  • 22
    • 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 89, 685-692 (1997).
    • (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
  • 23
    • 67649743349 scopus 로고    scopus 로고
    • Cellular functions and X-ray structure of anthrolysin O, a cholesterol-dependent cytolysin secreted by Bacillus anthracis
    • Bourdeau, R. W. et al. Cellular functions and X-ray structure of anthrolysin O, a cholesterol-dependent cytolysin secreted by Bacillus anthracis. J. Biol. Chem. 284, 14645-14656 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 14645-14656
    • Bourdeau, R.W.1
  • 24
    • 79953148352 scopus 로고    scopus 로고
    • Crystal structure of cytotoxin protein suilysin from Streptococcus suis
    • Xu, L. et al. Crystal structure of cytotoxin protein suilysin from Streptococcus suis. Protein Cell 1, 96-105 (2010).
    • (2010) Protein Cell , vol.1 , pp. 96-105
    • Xu, L.1
  • 25
    • 84893639595 scopus 로고    scopus 로고
    • Structural studies of Streptococcus pyogenes streptolysin O provides 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 provides insights into the early steps of membrane penetration. J. Mol. Biol. 426, 785-792 (2014).
    • (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
  • 26
    • 84899053464 scopus 로고    scopus 로고
    • Crystal structure of listeriolysin O reveals molecular details of oligomerisation and pore formation
    • Köster, S. et al. Crystal structure of listeriolysin O reveals molecular details of oligomerisation and pore formation. Nature Commun. 5, 3690 (2014).
    • (2014) Nature Commun. , vol.5 , pp. 3690
    • Köster, S.1
  • 27
    • 33947163269 scopus 로고    scopus 로고
    • Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins
    • Rossjohn, J. et al. Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins. J. Mol. Biol. 367, 1227-1238 (2007).
    • (2007) J. Mol. Biol. , vol.367 , pp. 1227-1238
    • Rossjohn, J.1
  • 28
    • 84923279935 scopus 로고    scopus 로고
    • An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin
    • Wade, K. R. et al. An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin. Proc. Natl. Acad. Sci. USA 112, 2204-2209 (2015).
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 2204-2209
    • Wade, K.R.1
  • 29
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence, M. C., Colman, P. M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 30
    • 0032509103 scopus 로고    scopus 로고
    • Self-interaction of pneumolysin, the pore forming protein toxin of Streptococcus pneumoniae
    • Gilbert, R. J. et al. Self-interaction of pneumolysin, the pore forming protein toxin of Streptococcus pneumoniae. J. Mol. Biol. 284, 1223-1237 (1998).
    • (1998) J. Mol. Biol. , vol.284 , pp. 1223-1237
    • Gilbert, R.J.1
  • 31
    • 0034702810 scopus 로고    scopus 로고
    • The mechanism of pore assembly for a cholesterol-dependent cytolysin: Formation of a large prepore complex precedes the insertion of the transmembrane-hairpins
    • Shepard, L. A., Shatursky, O., Johnson, A. E., Tweten, R. K. The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane ?-hairpins. Biochemistry 39, 10284-10293 (2000).
    • (2000) Biochemistry , vol.39 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 32
    • 84863799473 scopus 로고    scopus 로고
    • Monomer-monomer interactions propagate structural transitions necessary for pore-formation by the cholesteroldependent cytolysins
    • Hotze, E. et al. Monomer-monomer interactions propagate structural transitions necessary for pore-formation by the cholesteroldependent cytolysins. J. Biol. Chem. 287, 24534-24543 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 24534-24543
    • Hotze, E.1
  • 33
    • 79952682402 scopus 로고    scopus 로고
    • Purification crystallisation, small-angle scattering and preliminary X-ray diffraction analysis of the SH2 domain of Csk-homologous kinase
    • Gunn, N. J., Gorman, M. A., Dobson, R. C. J., Parker, M. W., Mulhern, T. D. Purification, crystallisation, small-angle scattering and preliminary X-ray diffraction analysis of the SH2 domain of Csk-homologous kinase. Acta Crystallogr. F 67, 336-339 (2011).
    • (2011) Acta Crystallogr. F , vol.67 , pp. 336-339
    • Gunn, N.J.1    Gorman, M.A.2    Dobson, R.C.J.3    Parker, M.W.4    Mulhern, T.D.5
  • 34
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • Petoukhov, M. V. et al. New developments in the ATSAS program package for small-angle scattering data analysis. J. Appl. Cryst. 45, 342-350 (2012).
    • (2012) J. Appl. Cryst. , vol.45 , pp. 342-350
    • Petoukhov, M.V.1
  • 35
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering
    • Mylonas, E., Svergum, D. I. Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering. J. Appl. Cryst. 40, s245-s249 (2007).
    • (2007) J. Appl. Cryst. , vol.40 , pp. s245-s249
    • Mylonas, E.1    Svergum, D.I.2
  • 36
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF a program for rapid ab-initio shape determination in small-angle scattering
    • Franke, D., Svergun, D. I. DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J. Appl. Cryst. 42, 342-346 (2009).
    • (2009) J. Appl. Cryst. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 37
    • 0029185933 scopus 로고
    • CRYSOL - A Program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C., Koch, M. H. J. CRYSOL-a Program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Cryst. 28, 768-773 (1995).
    • (1995) J. Appl. Cryst. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 38
    • 84864371562 scopus 로고    scopus 로고
    • Prediction of carbohydrate binding sites on protein surfaces with 3-dimensional probability density distributions of interacting atoms
    • Tsai, K. C. et al. Prediction of carbohydrate binding sites on protein surfaces with 3-dimensional probability density distributions of interacting atoms. PLoS ONE 7, e40846 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e40846
    • Tsai, K.C.1
  • 39
    • 3042855150 scopus 로고    scopus 로고
    • The solution structure and oligomerization behaviour of two bacterial toxins: Pneumolysin and perfringolysin O
    • Solovyova, A. S., Nöllmann, M., Mitchell, T. J., Byron, O. The solution structure and oligomerization behaviour of two bacterial toxins: pneumolysin and perfringolysin O. Biophys. J. 87, 540-552 (2004).
    • (2004) Biophys. J. , vol.87 , pp. 540-552
    • Solovyova, A.S.1    Nöllmann, M.2    Mitchell, T.J.3    Byron, O.4
  • 40
    • 0033612389 scopus 로고    scopus 로고
    • Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
    • Gilbert, R. J. et al. Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae. Cell 97, 647-655 (1999).
    • (1999) Cell , vol.97 , pp. 647-655
    • Gilbert, R.J.1
  • 41
    • 29644447798 scopus 로고    scopus 로고
    • Construction and immunological characterization of a novel nontoxic protective pneumolysin mutant for use in future pneumococcal vaccines
    • Kirkham, L. A. et al. Construction and immunological characterization of a novel nontoxic protective pneumolysin mutant for use in future pneumococcal vaccines. Infect. Immun. 74, 586-593 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 586-593
    • Kirkham, L.A.1
  • 42
    • 33847317012 scopus 로고    scopus 로고
    • Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural network
    • Malik, A., Ahmad, S. Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural network. BMC Struct. Biol. 7, 1 (2007).
    • (2007) BMC Struct. Biol. , vol.7 , pp. 1
    • Malik, A.1    Ahmad, S.2
  • 43
    • 0023656177 scopus 로고
    • Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens
    • Iwamoto, M., Ohno-Iwashita, Y., Ando, S. Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens. Eur. J. Biochem. 167, 425-430 (1987).
    • (1987) Eur. J. Biochem. , vol.167 , pp. 425-430
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 44
    • 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. 241, 941-947 (1996).
    • (1996) Eur. J. Biochem. , vol.241 , pp. 941-947
    • Sekino-Suzuki, N.1    Nakamura, M.2    Mitsui, K.I.3    Ohno-Iwashita, Y.4
  • 45
    • 0032858797 scopus 로고    scopus 로고
    • The conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding
    • Jacobs, T. et al. The conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding. FEBS Lett. 459, 463-466 (1999).
    • (1999) FEBS Lett. , vol.459 , pp. 463-466
    • Jacobs, T.1
  • 46
    • 84856241048 scopus 로고    scopus 로고
    • Active immunization with pneumolysin versus 23-Valent Polysaccharide Vaccine for Streptococcus pneumoniae keratitis
    • Norcross, E. W. et al. Active immunization with pneumolysin versus 23-Valent Polysaccharide Vaccine for Streptococcus pneumoniae keratitis. Invest. Ophthalmol. Vis. Sci. 52, 9232-9243 (2011).
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , pp. 9232-9243
    • Norcross, E.W.1
  • 47
    • 79953316626 scopus 로고    scopus 로고
    • Structure-guided antigen engineering yields pneumolysin mutants suitable for vaccination against pneumococcal disease
    • Oloo, E. O., Yethon, J. A., Ochs, M. M., Carpick, B., Oomen, R. Structure-guided antigen engineering yields pneumolysin mutants suitable for vaccination against pneumococcal disease. J. Biol. Chem. 286, 12133-12140 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 12133-12140
    • Oloo, E.O.1    Yethon, J.A.2    Ochs, M.M.3    Carpick, B.4    Oomen, R.5
  • 48
    • 85047688160 scopus 로고    scopus 로고
    • Neutralizing antibodies elicited by a novel detoxified pneumolysin derivative, PlyD1, provide protection against both pneumococcal infection and lung injury
    • Salha, D. et al. Neutralizing antibodies elicited by a novel detoxified pneumolysin derivative, PlyD1, provide protection against both pneumococcal infection and lung injury. Infect. Immun. 80, 2212-2220 (2012).
    • (2012) Infect. Immun. , vol.80 , pp. 2212-2220
    • Salha, D.1
  • 49
    • 84875304782 scopus 로고    scopus 로고
    • Characterization of protective immune responses induced by pneumococcal surface protein A in fusion with pneumolysin derivatives
    • Goulart, C. et al. Characterization of protective immune responses induced by pneumococcal surface protein A in fusion with pneumolysin derivatives. PLoS One 8, e59605 (2013).
    • (2013) PLoS One , vol.8 , pp. e59605
    • Goulart, C.1
  • 50
    • 84876909001 scopus 로고    scopus 로고
    • Nasopharyngeal carriage with Streptococcus pneumoniae augments the immunizing effect of pneumolysin toxoid B
    • Neill, D. R., Smeaton, S., Bangert, M., Kadioglu, A. Nasopharyngeal carriage with Streptococcus pneumoniae augments the immunizing effect of pneumolysin toxoid B. J. Allergy Clin. Immunol. 131, 1433-1435 (2013).
    • (2013) J. Allergy Clin. Immunol. , vol.131 , pp. 1433-1435
    • Neill, D.R.1    Smeaton, S.2    Bangert, M.3    Kadioglu, A.4
  • 51
    • 84898964001 scopus 로고    scopus 로고
    • Broadly protective protein-based pneumococcal vaccine composed of pneumolysin toxoid-CbpA peptide recombinant fusion protein
    • Mann, B. et al. Broadly protective protein-based pneumococcal vaccine composed of pneumolysin toxoid-CbpA peptide recombinant fusion protein. J. Infect. Dis. 209, 1116-1125 (2014).
    • (2014) J. Infect. Dis. , vol.209 , pp. 1116-1125
    • Mann, B.1
  • 52
    • 84887980683 scopus 로고    scopus 로고
    • A low-background-intensity focusing small-angle X-ray scattering undulator beamline
    • Kirby, N. M. et al. A low-background-intensity focusing small-angle X-ray scattering undulator beamline. J. Appl. Cryst. 46, 1670-1680 (2013).
    • (2013) J. Appl. Cryst. , vol.46 , pp. 1670-1680
    • Kirby, N.M.1
  • 53
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V., Svergun, D. I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864 (2003).
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 54
    • 0036849859 scopus 로고    scopus 로고
    • Blu-Ice and the Distributed Control System: Software for data acquisition and instrument control at macromolecular crystallography beamlines
    • McPhillips, T. M. et al. Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines. J. Synchrotron Radiat. 9, 401-406 (2002).
    • (2002) J. Synchrotron Radiat. , vol.9 , pp. 401-406
    • McPhillips, T.M.1
  • 55
    • 76449106188 scopus 로고    scopus 로고
    • Integration scaling, space-group assignment and post-refinement
    • Kabsch, W. Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D. Biol. Crystallogr. 66, 133-144 (2010).
    • (2010) Acta Crystallogr. D. Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 56
    • 0014432781 scopus 로고
    • Solvent contents of protein crystal
    • Matthews, B. W. Solvent contents of protein crystal. J. Mol. Biol. 33, 491-497 (1968).
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 57
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 59
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building a software for automated crystallographic structure determination
    • Adams, P. D. et al. PHENIX: building a software for automated crystallographic structure determination. Acta Crystallogr. D Biol. Crystallogr. 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 60
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the sterochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M. PROCHECK: a program to check the sterochemical quality of protein structures. J. Appl. Cryst. 26, 283-291 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 61
    • 34247343346 scopus 로고    scopus 로고
    • Surflex-Dock 2.1: Robust performance from ligand energetic modelling, ring flexibility, and knowledge-based search
    • Jain, A. N. Surflex-Dock 2.1: robust performance from ligand energetic modelling, ring flexibility, and knowledge-based search. J. Comput. Aided Mol. Des. 21, 281-306 (2007).
    • (2007) J. Comput. Aided Mol. Des. , vol.21 , pp. 281-306
    • Jain, A.N.1
  • 62
  • 63
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503 (1992).
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.