메뉴 건너뛰기




Volumn 405, Issue 3, 2007, Pages 465-472

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

Author keywords

Bacteriophage; Catalytic activity; Endosialidase (endo N acetylneuraminidase); Host range mutant; Polysialic acid

Indexed keywords

ENDOSIALIDASE; HOST RANGE MUTANT; POLYSIALIC ACID;

EID: 34547452769     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070177     Document Type: Article
Times cited : (29)

References (42)
  • 1
    • 0021459417 scopus 로고
    • Structure, conformation and immunology of sialic acid-containing polysaccharides of human pathogenic bacteria
    • Jennings, H. J., Katzenellenbogen, E., Lugowski, C., Michon, F., Roy, R. and Kasper, D. L. (1984) Structure, conformation and immunology of sialic acid-containing polysaccharides of human pathogenic bacteria. Pure Appl. Chem. 56, 893-905
    • (1984) Pure Appl. Chem , vol.56 , pp. 893-905
    • Jennings, H.J.1    Katzenellenbogen, E.2    Lugowski, C.3    Michon, F.4    Roy, R.5    Kasper, D.L.6
  • 2
    • 0025967376 scopus 로고
    • Identity between polysaccharide antigens of Moraxella nonliquefaciens, group B Neisseria meningitidis, and Escherichia coli K1 (non-O acetylated)
    • Devi, S. J. N., Schneerson, R., Egan, W., Vann, W. F., Robbins, J. B. and Shiloach, J. (1991) Identity between polysaccharide antigens of Moraxella nonliquefaciens, group B Neisseria meningitidis, and Escherichia coli K1 (non-O acetylated). Infect. Immun. 59, 732-736
    • (1991) Infect. Immun , vol.59 , pp. 732-736
    • Devi, S.J.N.1    Schneerson, R.2    Egan, W.3    Vann, W.F.4    Robbins, J.B.5    Shiloach, J.6
  • 4
    • 2142758676 scopus 로고    scopus 로고
    • Prevention and cure of systemic Escherichia coli K1 infection by modification of the bacterial phenotype
    • Mushtaq, N., Redpath, M. B., Luzio, J. P. and Taylor, P. W. (2004) Prevention and cure of systemic Escherichia coli K1 infection by modification of the bacterial phenotype. Antimicrob. Agents Chemother. 48, 1503-1508
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 1503-1508
    • Mushtaq, N.1    Redpath, M.B.2    Luzio, J.P.3    Taylor, P.W.4
  • 5
    • 24044532239 scopus 로고    scopus 로고
    • Treatment of experimental Escherichia coli infection with recombinant bacteriophage-derived capsule depolymerase
    • Mushtaq, N., Redpath, M. B., Luzio, J. P. and Taylor, P. W. (2005) Treatment of experimental Escherichia coli infection with recombinant bacteriophage-derived capsule depolymerase. J. Antimicrob. Chemother. 56, 160-165
    • (2005) J. Antimicrob. Chemother , vol.56 , pp. 160-165
    • Mushtaq, N.1    Redpath, M.B.2    Luzio, J.P.3    Taylor, P.W.4
  • 6
    • 0031904239 scopus 로고    scopus 로고
    • Polysialic acid at the cell surface: Biophysics in service of cell interactions and tissue plasticity
    • Rutishauser, U. (1998) Polysialic acid at the cell surface: biophysics in service of cell interactions and tissue plasticity. J. Cell. Biochem. 70, 304-312
    • (1998) J. Cell. Biochem , vol.70 , pp. 304-312
    • Rutishauser, U.1
  • 7
    • 0020405904 scopus 로고
    • Occurrence of unique polysialosyl carbohydrate units in glycoproteins of developing brain
    • Finne, J. (1982) Occurrence of unique polysialosyl carbohydrate units in glycoproteins of developing brain. J. Biol. Chem. 257, 11966-11970
    • (1982) J. Biol. Chem , vol.257 , pp. 11966-11970
    • Finne, J.1
  • 10
    • 0042131904 scopus 로고    scopus 로고
    • Polysialic acid directs tumor cell growth by controlling heterophilic neural cell adhesion molecule interactions
    • Seidenfaden, R., Krauter, A., Schertzinger, F., Gerardy-Schahn, R. and Hildebrandt, H. (2003) Polysialic acid directs tumor cell growth by controlling heterophilic neural cell adhesion molecule interactions. Mol. Cell. Biol. 23, 5908-5918
    • (2003) Mol. Cell. Biol , vol.23 , pp. 5908-5918
    • Seidenfaden, R.1    Krauter, A.2    Schertzinger, F.3    Gerardy-Schahn, R.4    Hildebrandt, H.5
  • 11
    • 0017569792 scopus 로고
    • Isolation of bacteriophages specific for the K1 polysaccharide antigen of Escherichia coli
    • Gross, R. J., Cheasty, T. and Rowe, B. (1977) Isolation of bacteriophages specific for the K1 polysaccharide antigen of Escherichia coli. J. Clin. Microbiol. 6, 548-550
    • (1977) J. Clin. Microbiol , vol.6 , pp. 548-550
    • Gross, R.J.1    Cheasty, T.2    Rowe, B.3
  • 13
    • 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. and Merril, C. R. (2001) 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. 75, 2509-2515
    • (2001) J. Virol , vol.75 , pp. 2509-2515
    • Scholl, D.1    Rogers, S.2    Adhya, S.3    Merril, C.R.4
  • 14
    • 0028997818 scopus 로고
    • Complete nucleotide sequence of the gene encoding bacteriophage E endosialidase: Implication for K1E endosialidase structure and function
    • Long, G. S., Bryant, J. M., Taylor, P. W. and Luzio, J. P. (1995) Complete nucleotide sequence of the gene encoding bacteriophage E endosialidase: implication for K1E endosialidase structure and function. Biochem. J. 309, 543-550
    • (1995) Biochem. J , vol.309 , pp. 543-550
    • Long, G.S.1    Bryant, J.M.2    Taylor, P.W.3    Luzio, J.P.4
  • 16
    • 0026446254 scopus 로고
    • Differential activities of bacteriophage depolymerase on bacterial polysaccharide: Binding is essential but degradation is inhibitory in phage infection of K1-defective Escherichia coli
    • Pelkonen, S., Aalto, J. and Finne, J. (1992) Differential activities of bacteriophage depolymerase on bacterial polysaccharide: binding is essential but degradation is inhibitory in phage infection of K1-defective Escherichia coli. J. Bacteriol. 174, 7757-7761
    • (1992) J. Bacteriol , vol.174 , pp. 7757-7761
    • Pelkonen, S.1    Aalto, J.2    Finne, J.3
  • 17
    • 0025088466 scopus 로고
    • Capsular sialyl chains of Escherichia coli K1 mutants resistant to K1 phage
    • Pelkonen, S. (1990) Capsular sialyl chains of Escherichia coli K1 mutants resistant to K1 phage. Curr. Microbiol. 21, 23-28
    • (1990) Curr. Microbiol , vol.21 , pp. 23-28
    • Pelkonen, S.1
  • 18
    • 0035497422 scopus 로고    scopus 로고
    • Mutant bacteriophage with non-catalytic endosialidase binds to both bacterial and eukaryotic polysialic acid and can be used as probe for its detection
    • Aalto, J., Pelkonen, S., Kalimo, H. and Finne, J. (2001) Mutant bacteriophage with non-catalytic endosialidase binds to both bacterial and eukaryotic polysialic acid and can be used as probe for its detection. Glycoconj. J. 18, 751-758
    • (2001) Glycoconj. J , vol.18 , pp. 751-758
    • Aalto, J.1    Pelkonen, S.2    Kalimo, H.3    Finne, J.4
  • 19
    • 0023196238 scopus 로고
    • A rapid turbidimetric assay for the study of serum sensitivity of Escherichia coli
    • Pelkonen, S. and Finne, J. (1987) A rapid turbidimetric assay for the study of serum sensitivity of Escherichia coli. FEMS Microbiol. Lett. 42, 53-57
    • (1987) FEMS Microbiol. Lett , vol.42 , pp. 53-57
    • Pelkonen, S.1    Finne, J.2
  • 20
    • 0004136246 scopus 로고
    • Maniatis, T, Fritsch, E. F. and Sambrook, J, eds, Cold Spring Harbor Laboratory Press, Plainview, NY
    • Maniatis, T., Fritsch, E. F. and Sambrook, J. (eds) (1982) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Plainview, NY
    • (1982) Molecular Cloning: A Laboratory Manual
  • 21
    • 4244057723 scopus 로고
    • The use of bacteriophagesin the study of bacterial cell surface structures
    • Korhonen, T. K, Dawes, E. A. and Mäkelä, P. H, eds, pp, Elsevier Science Publishers, Amsterdam
    • Mäkelä, P. H. (1985) The use of bacteriophagesin the study of bacterial cell surface structures. In Enterobacterial Surface Antigenes: Methods tor Molecular Characterization (Korhonen, T. K., Dawes, E. A. and Mäkelä, P. H., eds.), pp. 155-178, Elsevier Science Publishers, Amsterdam
    • (1985) Enterobacterial Surface Antigenes: Methods tor Molecular Characterization , pp. 155-178
    • Mäkelä, P.H.1
  • 25
    • 0019796391 scopus 로고
    • A modified spectrophotometric method for determination nanogram quantities of sialic acid
    • Horgan, I. E. (1981) A modified spectrophotometric method for determination nanogram quantities of sialic acid. Clin. Chim. Acta 116, 409-415
    • (1981) Clin. Chim. Acta , vol.116 , pp. 409-415
    • Horgan, I.E.1
  • 27
    • 0027361123 scopus 로고    scopus 로고
    • Johnson, M. S. and Overington, J. P. (1993) A structural basis for sequence comparisons. An evaluation of scoring methodologies. J. Mol. Biol. 233, 716-738
    • Johnson, M. S. and Overington, J. P. (1993) A structural basis for sequence comparisons. An evaluation of scoring methodologies. J. Mol. Biol. 233, 716-738
  • 29
    • 0037969598 scopus 로고    scopus 로고
    • Proteolytic processing and oligomerization of bacteriophage-derived endosialidases
    • Mühlenhoff, M., Stummeyer, K., Grove, M., Sauerborn, M. and Gerardy-Schahn, R. (2003) Proteolytic processing and oligomerization of bacteriophage-derived endosialidases. J. Biol. Chem. 278, 12634-12644
    • (2003) J. Biol. Chem , vol.278 , pp. 12634-12644
    • Mühlenhoff, M.1    Stummeyer, K.2    Grove, M.3    Sauerborn, M.4    Gerardy-Schahn, R.5
  • 30
    • 0030249583 scopus 로고    scopus 로고
    • Site-directed mutations of the catalytic and conserved amino acids of the neuraminidase gene, nanH, of Clostridium perfingens ATCC 10543
    • Chien, C. H., Shann, Y. J. and Sheu, S. Y. (1996) Site-directed mutations of the catalytic and conserved amino acids of the neuraminidase gene, nanH, of Clostridium perfingens ATCC 10543. Enzyme Microb. Technol. 19, 267-276
    • (1996) Enzyme Microb. Technol , vol.19 , pp. 267-276
    • Chien, C.H.1    Shann, Y.J.2    Sheu, S.Y.3
  • 31
    • 0036093757 scopus 로고    scopus 로고
    • Expression, mutagenesis and kinetic analysis of recombinant K1E endosialidase to define the site of proteolytic processing and requirements for catalysis
    • Leggate, D. R., Bryant, J. M., Redpath, M. B., Head, D., Taylor, P. W. and Luzio, J. P. (2002) Expression, mutagenesis and kinetic analysis of recombinant K1E endosialidase to define the site of proteolytic processing and requirements for catalysis. Mol. Microbiol. 44, 749-760
    • (2002) Mol. Microbiol , vol.44 , pp. 749-760
    • Leggate, D.R.1    Bryant, J.M.2    Redpath, M.B.3    Head, D.4    Taylor, P.W.5    Luzio, J.P.6
  • 32
    • 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. (1994) Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure 2, 535-544
    • (1994) Structure , vol.2 , pp. 535-544
    • Crennell, S.1    Garman, E.2    Laver, G.3    Vimr, E.4    Taylor, G.5
  • 33
    • 0029645872 scopus 로고
    • The tree domains of a bacterial sialidase: A beta-propeller an immunoglobulin module and a galactose-binding jelly-roll
    • Gaskell, A., Crennell, S. J. and Tailor, G. L. (1995) The tree domains of a bacterial sialidase: a beta-propeller an immunoglobulin module and a galactose-binding jelly-roll. Structure 3, 1197-1205
    • (1995) Structure , vol.3 , pp. 1197-1205
    • Gaskell, A.1    Crennell, S.J.2    Tailor, G.L.3
  • 34
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. and Gay, N. J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 35
    • 0025048136 scopus 로고
    • The P-loop - a common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P. R. and Wittinghofer, A. (1990) The P-loop - a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15, 430-434
    • (1990) Trends Biochem. Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 36
    • 0347914560 scopus 로고    scopus 로고
    • Genomic analysis of bacteriophages SP6 and K1-5, an estranged subgroup of the T7 supergroup
    • Scholl, D., Kieleczawa, J., Kemp, P., Rush, J., C., R. C., Merril, C., Adhya, S. and Molineux, I. J. (2004) Genomic analysis of bacteriophages SP6 and K1-5, an estranged subgroup of the T7 supergroup. J. Mol. Biol. 335, 1151-1171
    • (2004) J. Mol. Biol , vol.335 , pp. 1151-1171
    • Scholl, D.1    Kieleczawa, J.2    Kemp, P.3    Rush, J.C.R.C.4    Merril, C.5    Adhya, S.6    Molineux, I.J.7
  • 37
    • 0026589426 scopus 로고
    • DNA sequences of the tail fiber genes of bacteriophage P2: Evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages
    • Haggård-Ljungquist, E., Halling, C. and Calendar, R. (1992) DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages. J. Bacteriol. 174, 1462-1477
    • (1992) J. Bacteriol , vol.174 , pp. 1462-1477
    • Haggård-Ljungquist, E.1    Halling, C.2    Calendar, R.3
  • 38
    • 10044253266 scopus 로고    scopus 로고
    • Comparative genomics of the T4-like Escherichia coli phage JS98: Implications for the evolution of T4 phages
    • Chibani-Chennoufi, S., Canchaya, C., Bruttin, A. and Brüssow, H. (2004) Comparative genomics of the T4-like Escherichia coli phage JS98: implications for the evolution of T4 phages. J. Bacteriol. 186, 8276-8286
    • (2004) J. Bacteriol , vol.186 , pp. 8276-8286
    • Chibani-Chennoufi, S.1    Canchaya, C.2    Bruttin, A.3    Brüssow, H.4
  • 39
    • 0027214249 scopus 로고
    • Affinity of monoclonal antibodies to large multivalent antigens: Influence of steric hindrance on antibody affinity constants calculated from Scatchard plots
    • Pellequer, J. L. and Van Regenmortel, M. H. (1993) Affinity of monoclonal antibodies to large multivalent antigens: influence of steric hindrance on antibody affinity constants calculated from Scatchard plots. Mol. Immunol. 30, 955-958
    • (1993) Mol. Immunol , vol.30 , pp. 955-958
    • Pellequer, J.L.1    Van Regenmortel, M.H.2
  • 40
    • 34547488649 scopus 로고    scopus 로고
    • Genomewide screens for Escherichia coli genes affecting growth of T7 bacteriophage
    • Qimron, U., Marintcheva, B., Tabor, S. and Richardson, C. C. (2006) Genomewide screens for Escherichia coli genes affecting growth of T7 bacteriophage. Proc. Natl. Acad. Sci. U.S.A. 103, 19039-19044
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 19039-19044
    • Qimron, U.1    Marintcheva, B.2    Tabor, S.3    Richardson, C.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.