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Volumn 380, Issue 3, 2009, Pages 467-471

Crystal structures of respiratory pathogen neuraminidases

Author keywords

Crystal structure; Neuraminidase; Pneumonia; Pseudomonas aeruginosa; Streptococcus pneumoniae

Indexed keywords

BACTERIAL ENZYME; NANA ENZYME; NANP ENZYME; SIALIDASE; UNCLASSIFIED DRUG;

EID: 60549101305     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.01.108     Document Type: Article
Times cited : (30)

References (33)
  • 1
    • 0030444832 scopus 로고    scopus 로고
    • Sialidases: structures, biological significance and therapeutic potential
    • Taylor G. Sialidases: structures, biological significance and therapeutic potential. Curr. Opin. Struct. Biol. 6 (1996) 830-837
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 830-837
    • Taylor, G.1
  • 2
    • 40549135865 scopus 로고    scopus 로고
    • Pneumococcal conjugate vaccine for childhood immunization - WHO position paper, Weekly Epidemiological Record
    • World Health Organisation WHO
    • World Health Organisation (WHO), Pneumococcal conjugate vaccine for childhood immunization - WHO position paper, Weekly Epidemiological Record, WHO, Geneva, 2007, pp. 93-104.
    • (2007) WHO, Geneva , pp. 93-104
  • 3
    • 37349058158 scopus 로고    scopus 로고
    • Vaccine escape recombinants emerge after pneumococcal vaccination in the United States
    • Brueggemann A.B., Pai R., Crook D.W., and Beall B. Vaccine escape recombinants emerge after pneumococcal vaccination in the United States. PLoS Pathog. 3 (2007) e168
    • (2007) PLoS Pathog. , vol.3
    • Brueggemann, A.B.1    Pai, R.2    Crook, D.W.3    Beall, B.4
  • 4
    • 34247498668 scopus 로고    scopus 로고
    • Invasive pneumococcal disease caused by nonvaccine serotypes among Alaska native children with high levels of 7-valent pneumococcal conjugate vaccine coverage
    • Singleton R.J., Hennessy T.W., Bulkow L.R., Hammitt L.L., Zulz T., Hurlburt D.A., Butler J.C., Rudolph K., and Parkinson A. Invasive pneumococcal disease caused by nonvaccine serotypes among Alaska native children with high levels of 7-valent pneumococcal conjugate vaccine coverage. JAMA 297 (2007) 1784-1792
    • (2007) JAMA , vol.297 , pp. 1784-1792
    • Singleton, R.J.1    Hennessy, T.W.2    Bulkow, L.R.3    Hammitt, L.L.4    Zulz, T.5    Hurlburt, D.A.6    Butler, J.C.7    Rudolph, K.8    Parkinson, A.9
  • 5
    • 33646950675 scopus 로고    scopus 로고
    • Variation in the presence of neuraminidase genes among Streptococcus pneumoniae isolates with identical sequence types
    • Pettigrew M.M., Fennie K.P., York M.P., Daniels J., and Ghaffar F. Variation in the presence of neuraminidase genes among Streptococcus pneumoniae isolates with identical sequence types. Infect. Immun. 74 (2006) 3360-3365
    • (2006) Infect. Immun. , vol.74 , pp. 3360-3365
    • Pettigrew, M.M.1    Fennie, K.P.2    York, M.P.3    Daniels, J.4    Ghaffar, F.5
  • 6
    • 33745585810 scopus 로고    scopus 로고
    • Pneumococcal neuraminidases A and B both have essential roles during infection of the respiratory tract and sepsis
    • Manco S., Hernon F., Yesilkaya H., Paton J.C., Andrew P.W., and Kadioglu A. Pneumococcal neuraminidases A and B both have essential roles during infection of the respiratory tract and sepsis. Infect. Immun. 74 (2006) 4014-4020
    • (2006) Infect. Immun. , vol.74 , pp. 4014-4020
    • Manco, S.1    Hernon, F.2    Yesilkaya, H.3    Paton, J.C.4    Andrew, P.W.5    Kadioglu, A.6
  • 7
    • 0014104556 scopus 로고
    • Neuraminidase activities of clinical isolates of Diplococcus pneumoniae
    • Kelly R.T., Farmer S., and Greiff D. Neuraminidase activities of clinical isolates of Diplococcus pneumoniae. J. Bacteriol. 94 (1967) 272-273
    • (1967) J. Bacteriol. , vol.94 , pp. 272-273
    • Kelly, R.T.1    Farmer, S.2    Greiff, D.3
  • 8
    • 22544485354 scopus 로고    scopus 로고
    • NanA, a neuraminidase from Streptococcus Pneumoniae, shows high levels of sequence diversity at least in part through recombination with Streptococcus oralis
    • King S.J., Whatmore A.M., and Dowson C.G. NanA, a neuraminidase from Streptococcus Pneumoniae, shows high levels of sequence diversity at least in part through recombination with Streptococcus oralis. J. Bacteriol. 187 (2005) 5376-5386
    • (2005) J. Bacteriol. , vol.187 , pp. 5376-5386
    • King, S.J.1    Whatmore, A.M.2    Dowson, C.G.3
  • 10
    • 33645087140 scopus 로고    scopus 로고
    • Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae
    • King S.J., Hippe K.R., and Weiser J.N. Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae. Mol. Microbiol. 59 (2006) 961-974
    • (2006) Mol. Microbiol. , vol.59 , pp. 961-974
    • King, S.J.1    Hippe, K.R.2    Weiser, J.N.3
  • 11
    • 6944224035 scopus 로고    scopus 로고
    • Tissue-specific contributions of pneumococcal virulence factors to pathogenesis
    • Orihuela C.J., Gao G., Francis K.P., Yu J., and Tuomanen E.I. Tissue-specific contributions of pneumococcal virulence factors to pathogenesis. J. Infect. Dis. 190 (2004) 1661-1669
    • (2004) J. Infect. Dis. , vol.190 , pp. 1661-1669
    • Orihuela, C.J.1    Gao, G.2    Francis, K.P.3    Yu, J.4    Tuomanen, E.I.5
  • 12
    • 0033977389 scopus 로고    scopus 로고
    • Evaluation of the virulence of a Streptococcus pneumoniae neuraminidase-deficient mutant in nasopharyngeal colonization and development of otitis media in the chinchilla model
    • Tong H.H., Blue L.E., James M.A., and DeMaria T.F. Evaluation of the virulence of a Streptococcus pneumoniae neuraminidase-deficient mutant in nasopharyngeal colonization and development of otitis media in the chinchilla model. Infect. Immun. 68 (2000) 921-924
    • (2000) Infect. Immun. , vol.68 , pp. 921-924
    • Tong, H.H.1    Blue, L.E.2    James, M.A.3    DeMaria, T.F.4
  • 14
    • 1542530299 scopus 로고    scopus 로고
    • Genetic features of Pseudomonas aeruginosa isolates from cystic fibrosis patients compared with those of isolates from other origins
    • Lanotte P., Watt S., Mereghetti L., Dartiguelongue N., Rastegar-Lari A., Goudeau A., and Quentin R. Genetic features of Pseudomonas aeruginosa isolates from cystic fibrosis patients compared with those of isolates from other origins. J. Med. Microbiol. 53 (2004) 73-81
    • (2004) J. Med. Microbiol. , vol.53 , pp. 73-81
    • Lanotte, P.1    Watt, S.2    Mereghetti, L.3    Dartiguelongue, N.4    Rastegar-Lari, A.5    Goudeau, A.6    Quentin, R.7
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 19944409045 scopus 로고    scopus 로고
    • The design implementation of SnB v2.0
    • Weeks C.M., and Miller R. The design implementation of SnB v2.0. J. Appl. Crystallogr. 32 (1999) 120-124
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 18
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: automated structure solution and density modification
    • Terwilliger T.C. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374 (2003) 22-37
    • (2003) Methods Enzymol. , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 Pt. 2 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 21
    • 0029937503 scopus 로고    scopus 로고
    • The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution
    • Crennell S.J., Garman E.F., Philippon C., Vasella A., Laver W.G., Vimr E.R., and Taylor G.L. The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution. J. Mol. Biol. 259 (1996) 264-280
    • (1996) J. Mol. Biol. , vol.259 , pp. 264-280
    • Crennell, S.J.1    Garman, E.F.2    Philippon, C.3    Vasella, A.4    Laver, W.G.5    Vimr, E.R.6    Taylor, G.L.7
  • 22
    • 0028773635 scopus 로고
    • Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain
    • Crennell S., Garman E., Laver G., Vimr E., and Taylor G. Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure 2 (1994) 535-544
    • (1994) Structure , vol.2 , pp. 535-544
    • Crennell, S.1    Garman, E.2    Laver, G.3    Vimr, E.4    Taylor, G.5
  • 24
    • 0029645872 scopus 로고
    • The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll
    • Gaskell A., Crennell S., and Taylor G. The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Structure 3 (1995) 1197-1205
    • (1995) Structure , vol.3 , pp. 1197-1205
    • Gaskell, A.1    Crennell, S.2    Taylor, G.3
  • 25
    • 51149114195 scopus 로고    scopus 로고
    • Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA
    • Xu G., Li X., Andrew P.W., and Taylor G.L. Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA. Acta Crystallogr. F64 (2008) 772-775
    • (2008) Acta Crystallogr. , vol.F64 , pp. 772-775
    • Xu, G.1    Li, X.2    Andrew, P.W.3    Taylor, G.L.4
  • 26
    • 53049107996 scopus 로고    scopus 로고
    • Structural and functional studies of Streptococcus pneumoniae neuraminidase B: an intramolecular trans-sialidase
    • Gut H., King S.J., and Walsh M.A. Structural and functional studies of Streptococcus pneumoniae neuraminidase B: an intramolecular trans-sialidase. FEBS Lett. (2008)
    • (2008) FEBS Lett.
    • Gut, H.1    King, S.J.2    Walsh, M.A.3
  • 27
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D60 (2004) 2256-2268
    • (2004) Acta Crystallogr. , vol.D60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 28
    • 0030573054 scopus 로고    scopus 로고
    • Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans
    • Fong S., Hamill S.J., Proctoer M., Freund S.M.V., Benian G.M., Chothia C., Bycroft M., and Clarke J. Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J. Mol. Biol. 264 (1996) 624-639
    • (1996) J. Mol. Biol. , vol.264 , pp. 624-639
    • Fong, S.1    Hamill, S.J.2    Proctoer, M.3    Freund, S.M.V.4    Benian, G.M.5    Chothia, C.6    Bycroft, M.7    Clarke, J.8
  • 29
    • 0036224388 scopus 로고    scopus 로고
    • Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo
    • Carr J., Ives J., Kelly L., Lambkin R., Oxford J., Mendel D., Tai L., and Roberts N. Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo. Antiviral Res. 54 (2002) 79-88
    • (2002) Antiviral Res. , vol.54 , pp. 79-88
    • Carr, J.1    Ives, J.2    Kelly, L.3    Lambkin, R.4    Oxford, J.5    Mendel, D.6    Tai, L.7    Roberts, N.8
  • 30
    • 0037462977 scopus 로고    scopus 로고
    • The high resolution structures of free and inhibitor-bound Trypanosoma rangeli sialidase and its comparison with T. cruzi trans-sialidase
    • Amaya M.F., Buschiazzo A., Nguyen T., and Alzari P.M. The high resolution structures of free and inhibitor-bound Trypanosoma rangeli sialidase and its comparison with T. cruzi trans-sialidase. J. Mol. Biol. 325 (2003) 773-784
    • (2003) J. Mol. Biol. , vol.325 , pp. 773-784
    • Amaya, M.F.1    Buschiazzo, A.2    Nguyen, T.3    Alzari, P.M.4
  • 31
    • 0027185635 scopus 로고
    • The sialidase superfamily and its spread by horizontal gene transfer
    • Roggentin P., Schauer R., Hoyer L.L., and Vimr E.R. The sialidase superfamily and its spread by horizontal gene transfer. Mol. Microbiol. 9 (1993) 915-921
    • (1993) Mol. Microbiol. , vol.9 , pp. 915-921
    • Roggentin, P.1    Schauer, R.2    Hoyer, L.L.3    Vimr, E.R.4
  • 33
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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