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Volumn 477, Issue , 2015, Pages 133-143

Structure and biochemical characterization of bacteriophage phi92 endosialidase

Author keywords

Crystal structure; Endo 2,9 sialidase; Endosialidase; Phi92 bacteriophage; 2,9 linked polysialic acid

Indexed keywords

ALPHA2,9 LINKED SIALIC ACID; CAPSULAR POLYSACCHARIDE; DIMER; ENDOSIALIDASE 92; POLYSACCHARIDE; SIALIC ACID; UNCLASSIFIED DRUG; VIRUS ENZYME; ENDO-N-ACETYLNEURAMINIDASE; N ACETYLNEURAMINIC ACID; PROTEIN BINDING; SIALIDASE;

EID: 84930008984     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.11.002     Document Type: Article
Times cited : (22)

References (56)
  • 2
    • 0042035633 scopus 로고    scopus 로고
    • Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties
    • Anderson E., Teschke C.M. Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties. Virology 2003, 313:184-197.
    • (2003) Virology , vol.313 , pp. 184-197
    • Anderson, E.1    Teschke, C.M.2
  • 3
    • 84858166155 scopus 로고    scopus 로고
    • Short noncontractile tail machines: adsorption and DNA delivery by podoviruses
    • Casjens S.R., Molineux I.J. Short noncontractile tail machines: adsorption and DNA delivery by podoviruses. Adv. Exp. Med. Biol. 2012, 726:143-179.
    • (2012) Adv. Exp. Med. Biol. , vol.726 , pp. 143-179
    • Casjens, S.R.1    Molineux, I.J.2
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N.4 The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sec. D 1994, 50:760-763.
    • (1994) Acta Crystallogr. Sec. D , vol.50 , pp. 760-763
  • 5
    • 0024983502 scopus 로고
    • The biologic significance of bacterial encapsulation
    • Cross A.S. The biologic significance of bacterial encapsulation. Curr. Top. Microbiol. Immunol. 1990, 150:87-95.
    • (1990) Curr. Top. Microbiol. Immunol. , vol.150 , pp. 87-95
    • Cross, A.S.1
  • 7
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System.
    • [0.99rc6] San Carlos, CA, USA, DeLano Scientific. Ref Type: Computer Program
    • DeLano, W. The PyMOL Molecular Graphics System. [0.99rc6]. 2006. San Carlos, CA, USA, DeLano Scientific. Ref Type: Computer Program.
    • (2006)
    • DeLano, W.1
  • 9
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sec. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. Sec. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 10
    • 0020518256 scopus 로고
    • Antigenic similarities between brain components and bacteria causing meningitis. Implications for vaccine development and pathogenesis
    • Finne J., Leinonen M., Mäkelä P.H. Antigenic similarities between brain components and bacteria causing meningitis. Implications for vaccine development and pathogenesis. Lancet 1983, 2:355-362.
    • (1983) Lancet , vol.2 , pp. 355-362
    • Finne, J.1    Leinonen, M.2    Mäkelä, P.H.3
  • 11
    • 0019019959 scopus 로고
    • [1H-NMR-spectroscopic evidence for the release of N-acetyl-alpha-d-neuraminic acid as the first product of neuraminidase action (author[U+05F3]s transl)]
    • Friebolin H., Brossmer R., Keilich G., Ziegler D., Supp M. [1H-NMR-spectroscopic evidence for the release of N-acetyl-alpha-d-neuraminic acid as the first product of neuraminidase action (author[U+05F3]s transl)]. Hoppe Seylers. Z. Physiol. Chem. 1980, 361:697-702.
    • (1980) Hoppe Seylers. Z. Physiol. Chem. , vol.361 , pp. 697-702
    • Friebolin, H.1    Brossmer, R.2    Keilich, G.3    Ziegler, D.4    Supp, M.5
  • 12
    • 0023265359 scopus 로고
    • Serotyping and genotyping of encapsulated Escherichia coli K1 sepsis isolates with a monoclonal IgG anti K1 antibody and K1 gene probes
    • Frosch M., Roberts I., Gorgen I., Metzger S., Boulnois G.J., Bitter-Suermann D. Serotyping and genotyping of encapsulated Escherichia coli K1 sepsis isolates with a monoclonal IgG anti K1 antibody and K1 gene probes. Microb. Pathog. 1987, 2:319-326.
    • (1987) Microb. Pathog. , vol.2 , pp. 319-326
    • Frosch, M.1    Roberts, I.2    Gorgen, I.3    Metzger, S.4    Boulnois, G.J.5    Bitter-Suermann, D.6
  • 13
    • 0015267422 scopus 로고
    • Two new Escherichia coli O antigens, O150 and O157, and one new K antigen, K92, in strains isolated from veterinary diseases
    • Furowicz A.J., Ørskov F. Two new Escherichia coli O antigens, O150 and O157, and one new K antigen, K92, in strains isolated from veterinary diseases. Acta Pathol. Microbiol. Scand. Sec. B Microbiol. Immunol. 1972, 80:441-444.
    • (1972) Acta Pathol. Microbiol. Scand. Sec. B Microbiol. Immunol. , vol.80 , pp. 441-444
    • Furowicz, A.J.1    Ørskov, F.2
  • 14
    • 0242336022 scopus 로고    scopus 로고
    • C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer
    • Gage M.J., Robinson A.S. C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer. Protein Sci. 2003, 12:2732-2747.
    • (2003) Protein Sci. , vol.12 , pp. 2732-2747
    • Gage, M.J.1    Robinson, A.S.2
  • 16
    • 0017569792 scopus 로고
    • Isolation of bacteriophages specific for the K1 polysaccharide antigen of Escherichia coli
    • Gross R.J., Cheasty T., Rowe B. Isolation of bacteriophages specific for the K1 polysaccharide antigen of Escherichia coli. J. Clin. Microbiol. 1977, 6:548-550.
    • (1977) J. Clin. Microbiol. , vol.6 , pp. 548-550
    • Gross, R.J.1    Cheasty, T.2    Rowe, B.3
  • 17
    • 0023654291 scopus 로고
    • Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units
    • Hallenbeck P.C., Vimr E.R., Yu F., Bassler B., Troy F.A. Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units. J. Biol. Chem. 1987, 262:3553-3561.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3553-3561
    • Hallenbeck, P.C.1    Vimr, E.R.2    Yu, F.3    Bassler, B.4    Troy, F.A.5
  • 18
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 1989, 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 19
    • 84940173994 scopus 로고    scopus 로고
    • Boxshade. [3.31 beta]
    • Ref. Type: Computer Program
    • Hofmann, K. and Baron, M.D. Boxshade. [3.31 beta]. 2010. Ref. Type: Computer Program.
    • (2010)
    • Hofmann, K.1    Baron, M.D.2
  • 20
    • 0036857358 scopus 로고    scopus 로고
    • QuickTree: building huge neighbour-joining trees of protein sequences
    • Howe K., Bateman A., Durbin R. QuickTree: building huge neighbour-joining trees of protein sequences. Bioinformatics 2002, 18:1546-1547.
    • (2002) Bioinformatics , vol.18 , pp. 1546-1547
    • Howe, K.1    Bateman, A.2    Durbin, R.3
  • 21
    • 34547452769 scopus 로고    scopus 로고
    • Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and cleaving activities in Escherichia coli K1 bacteriophages
    • Jakobsson E., Jokilammi A., Aalto J., Ollikka P., Lehtonen J.V., Hirvonen H., Finne J. Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and cleaving activities in Escherichia coli K1 bacteriophages. Biochem. J. 2007, 405:465-472.
    • (2007) Biochem. J. , vol.405 , pp. 465-472
    • Jakobsson, E.1    Jokilammi, A.2    Aalto, J.3    Ollikka, P.4    Lehtonen, J.V.5    Hirvonen, H.6    Finne, J.7
  • 22
    • 84869012232 scopus 로고    scopus 로고
    • Endosialidases - versatile tools for the study of polysialic acid
    • Springer, Heidelberg, R. Gerardy-Schahn, M. von Itzstein, P. Delannoy (Eds.)
    • Jakobsson E., Schwarzer D., Jokilammi A., Finne J. Endosialidases - versatile tools for the study of polysialic acid. SialoGlyco Chemistry and Biology 2012, 1-46. Springer, Heidelberg. R. Gerardy-Schahn, M. von Itzstein, P. Delannoy (Eds.).
    • (2012) SialoGlyco Chemistry and Biology , pp. 1-46
    • Jakobsson, E.1    Schwarzer, D.2    Jokilammi, A.3    Finne, J.4
  • 24
    • 33745636847 scopus 로고    scopus 로고
    • Coliphage derived sialidase preferentially recognizes nonreducing end of polysialic acid
    • Kataoka Y., Miyake K., Iijima S. Coliphage derived sialidase preferentially recognizes nonreducing end of polysialic acid. J. Biosci. Bioeng. 2006, 101:198-201.
    • (2006) J. Biosci. Bioeng. , vol.101 , pp. 198-201
    • Kataoka, Y.1    Miyake, K.2    Iijima, S.3
  • 25
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 0037082166 scopus 로고    scopus 로고
    • PCR-mediated generation of a gene disruption construct without the use of DNA ligase and plasmid vectors
    • Kuwayama H., Obara S., Morio T., Katoh M., Urushihara H., Tanaka Y. PCR-mediated generation of a gene disruption construct without the use of DNA ligase and plasmid vectors. Nucleic Acids Res. 2002, 30:E2.
    • (2002) Nucleic Acids Res. , vol.30 , pp. E2
    • Kuwayama, H.1    Obara, S.2    Morio, T.3    Katoh, M.4    Urushihara, H.5    Tanaka, Y.6
  • 27
    • 0020701818 scopus 로고
    • Substrate specificity of two bacteriophage-associated endo-N-acetylneuraminidases
    • Kwiatkowski B., Boschek B., Thiele H., Stirm S. Substrate specificity of two bacteriophage-associated endo-N-acetylneuraminidases. J. Virol. 1983, 45:367-374.
    • (1983) J. Virol. , vol.45 , pp. 367-374
    • Kwiatkowski, B.1    Boschek, B.2    Thiele, H.3    Stirm, S.4
  • 28
    • 34447620875 scopus 로고    scopus 로고
    • The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities
    • Leiman P.G., Battisti A.J., Bowman V.D., Stummeyer K., Mühlenhoff M., Gerardy-Schahn R., Scholl D., Molineux I.J. The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. J. Mol. Biol. 2007, 371:836-849.
    • (2007) J. Mol. Biol. , vol.371 , pp. 836-849
    • Leiman, P.G.1    Battisti, A.J.2    Bowman, V.D.3    Stummeyer, K.4    Mühlenhoff, M.5    Gerardy-Schahn, R.6    Scholl, D.7    Molineux, I.J.8
  • 29
    • 84858189224 scopus 로고    scopus 로고
    • Contractile tail machines of bacteriophages
    • Leiman P.G., Shneider M.M. Contractile tail machines of bacteriophages. Adv. Exp. Med. Biol. 2012, 726:93-114.
    • (2012) Adv. Exp. Med. Biol. , vol.726 , pp. 93-114
    • Leiman, P.G.1    Shneider, M.M.2
  • 30
    • 0000651639 scopus 로고
    • Bacterial surface carbohydrates and bacteriophage adsorption
    • Academic Press Inc. (London) Ltd., London; United Kingdom, I.W. Sutherland (Ed.)
    • Lindberg A.A. Bacterial surface carbohydrates and bacteriophage adsorption. Surface Carbohydrates of the Prokaryotic Cell 1977, 289-356. Academic Press Inc. (London) Ltd., London; United Kingdom. I.W. Sutherland (Ed.).
    • (1977) Surface Carbohydrates of the Prokaryotic Cell , pp. 289-356
    • Lindberg, A.A.1
  • 32
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • [20] Processing of X-ray diffraction data collected in oscillation mode
    • Academic Press, New York, W.C. Charles (Ed.)
    • Otwinowski Z., Minor W. [20] Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology - Macromolecular Crystallography Part A 1997, 307-326. Academic Press, New York. W.C. Charles (Ed.).
    • (1997) Methods in Enzymology - Macromolecular Crystallography Part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 23744448545 scopus 로고    scopus 로고
    • Escherichia coli K1[U+05F3]s capsule is a barrier to bacteriophage T7
    • Scholl D., Adhya S., Merril C. Escherichia coli K1[U+05F3]s capsule is a barrier to bacteriophage T7. Appl. Environ. Microbiol. 2005, 71:4872-4874.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4872-4874
    • Scholl, D.1    Adhya, S.2    Merril, C.3
  • 38
    • 28844498371 scopus 로고    scopus 로고
    • The genome of bacteriophage K1F, a T7-like phage that has acquired the ability to replicate on K1 strains of Escherichia coli
    • Scholl D., Merril C. The genome of bacteriophage K1F, a T7-like phage that has acquired the ability to replicate on K1 strains of Escherichia coli. J. Bacteriol. 2005, 187:8499-8503.
    • (2005) J. Bacteriol. , vol.187 , pp. 8499-8503
    • Scholl, D.1    Merril, C.2
  • 39
    • 0035120334 scopus 로고    scopus 로고
    • Bacteriophage K1-5 encodes two different tail fiber proteins, allowing it to infect and replicate on both K1 and K5 strains of Escherichia coli
    • Scholl D., Rogers S., Adhya S., Merril C.R. Bacteriophage K1-5 encodes two different tail fiber proteins, allowing it to infect and replicate on both K1 and K5 strains of Escherichia coli. J. Virol. 2001, 75:2509-2515.
    • (2001) J. Virol. , vol.75 , pp. 2509-2515
    • Scholl, D.1    Rogers, S.2    Adhya, S.3    Merril, C.R.4
  • 41
    • 79953088876 scopus 로고    scopus 로고
    • Knitting and snipping: chaperones in beta-helix folding
    • Schulz E.C., Ficner R. Knitting and snipping: chaperones in beta-helix folding. Curr. Opin. Struct. Biol. 2011, 21:232-239.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 232-239
    • Schulz, E.C.1    Ficner, R.2
  • 45
    • 34047268904 scopus 로고    scopus 로고
    • Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins
    • Schwarzer D., Stummeyer K., Gerardy-Schahn R., Mühlenhoff M. Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins. J. Biol. Chem. 2007, 282:2821-2831.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2821-2831
    • Schwarzer, D.1    Stummeyer, K.2    Gerardy-Schahn, R.3    Mühlenhoff, M.4
  • 47
    • 0017177631 scopus 로고
    • Stable thiobarbituric acid chromophore with dimethyl sulphoxide. Application to sialic acid assay in analytical de-O-acetylation
    • Skoza L., Mohos S. Stable thiobarbituric acid chromophore with dimethyl sulphoxide. Application to sialic acid assay in analytical de-O-acetylation. Biochem. J. 1976, 159:457-462.
    • (1976) Biochem. J. , vol.159 , pp. 457-462
    • Skoza, L.1    Mohos, S.2
  • 48
  • 50
    • 0000173501 scopus 로고
    • Enzymes acting on bacterial surface carbohydrates
    • Academic Press Inc. Ltd., London; United Kingdom, I.W. Sutherland (Ed.)
    • Sutherland I.W. Enzymes acting on bacterial surface carbohydrates. Surface Carbohydrates of the Prokaryotic Cell 1977, 209-245. Academic Press Inc. Ltd., London; United Kingdom. I.W. Sutherland (Ed.).
    • (1977) Surface Carbohydrates of the Prokaryotic Cell , pp. 209-245
    • Sutherland, I.W.1
  • 51
    • 16544370625 scopus 로고    scopus 로고
    • Capsular polysaccharides and their role in virulence
    • Taylor C.M., Roberts I.S. Capsular polysaccharides and their role in virulence. Contrib. Microbiol. 2005, 12:55-66.
    • (2005) Contrib. Microbiol. , vol.12 , pp. 55-66
    • Taylor, C.M.1    Roberts, I.S.2
  • 52
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 53
    • 0342368769 scopus 로고    scopus 로고
    • Trans-sialidase from Trypanosoma cruzi catalyzes sialoside hydrolysis with retention of configuration
    • Todeschini A.R., Mendonca-Previato L., Previato J.O., Varki A., van Halbeek H. Trans-sialidase from Trypanosoma cruzi catalyzes sialoside hydrolysis with retention of configuration. Glycobiology 2000, 10:213-221.
    • (2000) Glycobiology , vol.10 , pp. 213-221
    • Todeschini, A.R.1    Mendonca-Previato, L.2    Previato, J.O.3    Varki, A.4    van Halbeek, H.5
  • 54
    • 8344231575 scopus 로고    scopus 로고
    • Purification of the Escherichia coli K5 capsular polysaccharide and use of high-performance capillary electrophoresis to qualitative and quantitative monitor the process
    • Volpi N. Purification of the Escherichia coli K5 capsular polysaccharide and use of high-performance capillary electrophoresis to qualitative and quantitative monitor the process. Electrophoresis 2004, 25:3307-3312.
    • (2004) Electrophoresis , vol.25 , pp. 3307-3312
    • Volpi, N.1
  • 55
    • 0038154169 scopus 로고    scopus 로고
    • Homotrimeric, beta-stranded viral adhesins and tail proteins
    • Weigele P.R., Scanlon E., King J. Homotrimeric, beta-stranded viral adhesins and tail proteins. J. Bacteriol. 2003, 185:4022-4030.
    • (2003) J. Bacteriol. , vol.185 , pp. 4022-4030
    • Weigele, P.R.1    Scanlon, E.2    King, J.3
  • 56
    • 33746356503 scopus 로고    scopus 로고
    • Biosynthesis and assembly of capsular polysaccharides in Escherichia coli
    • Whitfield C. Biosynthesis and assembly of capsular polysaccharides in Escherichia coli. Annu. Rev. Biochem. 2006, 75:39-68.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 39-68
    • Whitfield, C.1


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