메뉴 건너뛰기




Volumn 52, Issue 32, 2013, Pages 5463-5471

Functional characterization of staphylococcus epidermidis IcaB, a De-N-acetylase important for biofilm formation

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC EFFICIENCIES; EXTRACELLULAR PROTEINS; FUNCTIONAL CHARACTERIZATION; GRAM-POSITIVE BACTERIUM; NOSOCOMIAL PATHOGENS; POLYSACCHARIDE INTERCELLULAR ADHESIN; STAPHYLOCOCCUS EPIDERMIDIS; STEADY-STATE KINETICS;

EID: 84881621050     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400836g     Document Type: Article
Times cited : (33)

References (38)
  • 1
    • 84871580524 scopus 로고    scopus 로고
    • Molecular basis of in vivo biofilm formation by bacterial pathogens
    • Joo, H. S. and Otto, M. (2012) Molecular basis of in vivo biofilm formation by bacterial pathogens Chem. Biol. 19, 1503-1513
    • (2012) Chem. Biol. , vol.19 , pp. 1503-1513
    • Joo, H.S.1    Otto, M.2
  • 2
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: A common cause of persistent infections
    • Costerton, J. W., Stewart, P. S., and Greenberg, E. P. (1999) Bacterial biofilms: a common cause of persistent infections Science 284, 1318-1322
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 3
    • 0036228505 scopus 로고    scopus 로고
    • Biofilms: Survival mechanisms of clinically relevant microorganisms
    • Donlan, R. M. and Costerton, J. W. (2002) Biofilms: survival mechanisms of clinically relevant microorganisms Clin. Microbiol. Rev. 15, 167-193
    • (2002) Clin. Microbiol. Rev. , vol.15 , pp. 167-193
    • Donlan, R.M.1    Costerton, J.W.2
  • 4
    • 0033583045 scopus 로고    scopus 로고
    • Microbiology - Forging a link between biofilms and disease
    • Potera, C. (1999) Microbiology-Forging a link between biofilms and disease Science 283, 1837-1839
    • (1999) Science , vol.283 , pp. 1837-1839
    • Potera, C.1
  • 5
    • 68649115596 scopus 로고    scopus 로고
    • Bacterial extracellular polysaccharides involved in biofilm formation
    • Vu, B., Chen, M., Crawford, R. J., and Ivanova, E. P. (2009) Bacterial extracellular polysaccharides involved in biofilm formation Molecules 14, 2535-2554
    • (2009) Molecules , vol.14 , pp. 2535-2554
    • Vu, B.1    Chen, M.2    Crawford, R.J.3    Ivanova, E.P.4
  • 7
    • 0030065904 scopus 로고    scopus 로고
    • The intercellular adhesin involved in biofilm accumulation of Staphylococcus epidermidis is a linear beta-1,6-linked glucosaminoglycan: Purification and structural analysis
    • Mack, D., Fischer, W., Krokotsch, A., Leopold, K., Hartmann, R., Egge, H., and Laufs, R. (1996) The intercellular adhesin involved in biofilm accumulation of Staphylococcus epidermidis is a linear beta-1,6-linked glucosaminoglycan: Purification and structural analysis J. Bacteriol. 178, 175-183
    • (1996) J. Bacteriol. , vol.178 , pp. 175-183
    • Mack, D.1    Fischer, W.2    Krokotsch, A.3    Leopold, K.4    Hartmann, R.5    Egge, H.6    Laufs, R.7
  • 8
    • 34447249875 scopus 로고    scopus 로고
    • Molecular basis for preferential protective efficacy of antibodies directed to the poorly acetylated form of staphylococcal poly-N-acetyl-beta-(1- 6)-glucosaminev
    • Cerca, N., Jefferson, K. K., Maira-Litran, T., Pier, D. B., Kelly-Quintos, C., Goldmann, D. A., Azeredo, J., and Pier, G. B. (2007) Molecular basis for preferential protective efficacy of antibodies directed to the poorly acetylated form of staphylococcal poly-N-acetyl-beta-(1-6)- glucosaminev Infect. Immun. 75, 3406-3413
    • (2007) Infect. Immun. , vol.75 , pp. 3406-3413
    • Cerca, N.1    Jefferson, K.K.2    Maira-Litran, T.3    Pier, D.B.4    Kelly-Quintos, C.5    Goldmann, D.A.6    Azeredo, J.7    Pier, G.B.8
  • 9
    • 1942443593 scopus 로고    scopus 로고
    • The pgaABCD locus of Escherichia coli promotes the synthesis of a polysaccharide adhesin required for biofilm formation
    • Wang, X., Preston, J. F., and Romeo, T. (2004) The pgaABCD locus of Escherichia coli promotes the synthesis of a polysaccharide adhesin required for biofilm formation J. Bacteriol. 186, 2724-2734
    • (2004) J. Bacteriol. , vol.186 , pp. 2724-2734
    • Wang, X.1    Preston, J.F.2    Romeo, T.3
  • 10
    • 70349125920 scopus 로고    scopus 로고
    • The pgaABCD locus of Acinetobacter baumannii encodes the production of poly-beta-1,6-N-acetylglucosamine, which is critical for biofilm formation
    • Choi, A. H., Slamti, L., Avci, F. Y., Pier, G. B., and Maira-Litran, T. (2009) The pgaABCD locus of Acinetobacter baumannii encodes the production of poly-beta-1,6-N-acetylglucosamine, which is critical for biofilm formation J. Bacteriol. 191, 5953-5963
    • (2009) J. Bacteriol. , vol.191 , pp. 5953-5963
    • Choi, A.H.1    Slamti, L.2    Avci, F.Y.3    Pier, G.B.4    Maira-Litran, T.5
  • 11
    • 36549050407 scopus 로고    scopus 로고
    • The Bordetella Bps polysaccharide is critical for biofilm development in the mouse respiratory tract
    • Sloan, G. P., Love, C. F., Sukurnar, N., Mishra, M., and Deora, R. (2007) The Bordetella Bps polysaccharide is critical for biofilm development in the mouse respiratory tract J. Bacteriol. 189, 8270-8276
    • (2007) J. Bacteriol. , vol.189 , pp. 8270-8276
    • Sloan, G.P.1    Love, C.F.2    Sukurnar, N.3    Mishra, M.4    Deora, R.5
  • 12
    • 77956620995 scopus 로고    scopus 로고
    • The Bps polysaccharide of Bordetella pertussis promotes colonization and biofilm formation in the nose by functioning as an adhesin
    • Conover, M. S., Sloan, G. P., Love, C. F., Sukumar, N., and Deora, R. (2010) The Bps polysaccharide of Bordetella pertussis promotes colonization and biofilm formation in the nose by functioning as an adhesin Mol. Microbiol. 77, 1439-1455
    • (2010) Mol. Microbiol. , vol.77 , pp. 1439-1455
    • Conover, M.S.1    Sloan, G.P.2    Love, C.F.3    Sukumar, N.4    Deora, R.5
  • 15
    • 11144330206 scopus 로고    scopus 로고
    • Depolymerization of beta-1,6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms
    • Itoh, Y., Wang, X., Hinnebusch, B. J., Preston, J. F., and Romeo, T. (2005) Depolymerization of beta-1,6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms J. Bacteriol. 187, 382-387
    • (2005) J. Bacteriol. , vol.187 , pp. 382-387
    • Itoh, Y.1    Wang, X.2    Hinnebusch, B.J.3    Preston, J.F.4    Romeo, T.5
  • 17
    • 0029888438 scopus 로고    scopus 로고
    • Molecular basis of intercellular adhesion in the biofilm-forming Staphylococcus epidermidis
    • Heilmann, C., Schweitzer, O., Gerke, C., Vanittanakom, N., Mack, D., and Gotz, F. (1996) Molecular basis of intercellular adhesion in the biofilm-forming Staphylococcus epidermidis Mol. Microbiol. 20, 1083-1091
    • (1996) Mol. Microbiol. , vol.20 , pp. 1083-1091
    • Heilmann, C.1    Schweitzer, O.2    Gerke, C.3    Vanittanakom, N.4    Mack, D.5    Gotz, F.6
  • 18
    • 0031936896 scopus 로고    scopus 로고
    • Further characterization of Staphylococcus epidermidis transposon mutants deficient in primary attachment or intercellular adhesion
    • Heilmann, C. and Gotz, F. (1998) Further characterization of Staphylococcus epidermidis transposon mutants deficient in primary attachment or intercellular adhesion Zentralbl. Bakteriol. 287, 69-83
    • (1998) Zentralbl. Bakteriol. , vol.287 , pp. 69-83
    • Heilmann, C.1    Gotz, F.2
  • 19
    • 0030058648 scopus 로고    scopus 로고
    • Characterization of Tn917 insertion mutants of Staphylococcus epidermidis affected in biofilm formation
    • Heilmann, C., Gerke, C., Perdreau-Remington, F., and Gotz, F. (1996) Characterization of Tn917 insertion mutants of Staphylococcus epidermidis affected in biofilm formation Infect. Immun. 64, 277-282
    • (1996) Infect. Immun. , vol.64 , pp. 277-282
    • Heilmann, C.1    Gerke, C.2    Perdreau-Remington, F.3    Gotz, F.4
  • 20
    • 0032540949 scopus 로고    scopus 로고
    • Characterization of the N-acetylglucosaminyltransferase activity involved in the biosynthesis of the Staphylococcus epidermidis polysaccharide intercellular adhesin
    • Gerke, C., Kraft, A., Sussmuth, R., Schweitzer, O., and Gotz, F. (1998) Characterization of the N-acetylglucosaminyltransferase activity involved in the biosynthesis of the Staphylococcus epidermidis polysaccharide intercellular adhesin J. Biol. Chem. 273, 18586-18593
    • (1998) J. Biol. Chem. , vol.273 , pp. 18586-18593
    • Gerke, C.1    Kraft, A.2    Sussmuth, R.3    Schweitzer, O.4    Gotz, F.5
  • 21
    • 11144237620 scopus 로고    scopus 로고
    • A crucial role for exopolysaccharide modification in bacterial biofilm formation, immune evasion, and virulence
    • Vuong, C., Kocianova, S., Voyich, J. M., Yao, Y. F., Fischer, E. R., DeLeo, F. R., and Otto, M. (2004) A crucial role for exopolysaccharide modification in bacterial biofilm formation, immune evasion, and virulence J. Biol. Chem. 279, 54881-54886
    • (2004) J. Biol. Chem. , vol.279 , pp. 54881-54886
    • Vuong, C.1    Kocianova, S.2    Voyich, J.M.3    Yao, Y.F.4    Fischer, E.R.5    Deleo, F.R.6    Otto, M.7
  • 23
    • 84865222416 scopus 로고    scopus 로고
    • The structure- and metal-dependent activity of Escherichia coli PgaB provides insight into the partial de-N-acetylation of poly-beta-1,6-N-acetyl-D- glucosamine
    • Little, D. J., Poloczek, J., Whitney, J. C., Robinson, H., Nitz, M., and Howell, P. L. (2012) The structure- and metal-dependent activity of Escherichia coli PgaB provides insight into the partial de-N-acetylation of poly-beta-1,6-N-acetyl-D-glucosamine J. Biol. Chem. 287, 31126-31137
    • (2012) J. Biol. Chem. , vol.287 , pp. 31126-31137
    • Little, D.J.1    Poloczek, J.2    Whitney, J.C.3    Robinson, H.4    Nitz, M.5    Howell, P.L.6
  • 24
    • 84871876187 scopus 로고    scopus 로고
    • The structure of the deacetylase domain of Escherichia coli PgaB, an enzyme required for biofilm formation: A circularly permuted member of the carbohydrate esterase 4 family
    • Nishiyama, T., Noguchi, H., Yoshida, H., Park, S. Y., and Tame, J. R. (2013) The structure of the deacetylase domain of Escherichia coli PgaB, an enzyme required for biofilm formation: a circularly permuted member of the carbohydrate esterase 4 family Acta Crystallogr., Sect. D: Biol. Crystallogr. 69, 44-51
    • (2013) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.69 , pp. 44-51
    • Nishiyama, T.1    Noguchi, H.2    Yoshida, H.3    Park, S.Y.4    Tame, J.R.5
  • 25
    • 62549103295 scopus 로고    scopus 로고
    • Efficient synthesis and protein conjugation of beta-(1→6)-D-N- acetylglucosamine oligosaccharides from the polysaccharide intercellular adhesin
    • Leung, C., Chibba, A., Gomez-Biagi, R. F., and Nitz, M. (2009) Efficient synthesis and protein conjugation of beta-(1→6)-D-N-acetylglucosamine oligosaccharides from the polysaccharide intercellular adhesin Carbohydr. Res. 344, 570-575
    • (2009) Carbohydr. Res. , vol.344 , pp. 570-575
    • Leung, C.1    Chibba, A.2    Gomez-Biagi, R.F.3    Nitz, M.4
  • 26
    • 27344441825 scopus 로고    scopus 로고
    • Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor
    • Blair, D. E., Schuttelkopf, A. W., MacRae, J. I., and van Aalten, D. M. F. (2005) Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor Proc. Natl. Acad. Sci. U. S. A. 102, 15429-15434
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15429-15434
    • Blair, D.E.1    Schuttelkopf, A.W.2    Macrae, J.I.3    Van Aalten, D.M.F.4
  • 27
    • 84865272057 scopus 로고    scopus 로고
    • Synthesis and evaluation of inhibitors of E coli PgaB, a polysaccharide de-N-acetylase involved in biofilm formation
    • Chibba, A., Poloczek, J., Little, D. J., Howell, P. L., and Nitz, M. (2012) Synthesis and evaluation of inhibitors of E. coli PgaB, a polysaccharide de-N-acetylase involved in biofilm formation Org. Biomol. Chem. 10, 7103-7107
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 7103-7107
    • Chibba, A.1    Poloczek, J.2    Little, D.J.3    Howell, P.L.4    Nitz, M.5
  • 28
    • 84881640224 scopus 로고    scopus 로고
    • GraFit Version 7, Erithacus Software Limited, London, UK.
    • Leatherbarrow, R. J. (2011) GraFit Version 7, Erithacus Software Limited, London, UK.
    • (2011)
    • Leatherbarrow, R.J.1
  • 29
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range
    • Udenfriend, S., Stein, S., Bohlen, P., Dairman, W., Leimgruber, W., and Weigele, M. (1972) Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range Science 178, 871-872
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4    Leimgruber, W.5    Weigele, M.6
  • 30
    • 79958097953 scopus 로고    scopus 로고
    • The moderately efficient enzyme: Evolutionary and physicochemical trends shaping enzyme parameters
    • Bar-Even, A., Noor, E., Savir, Y., Liebermeister, W., Davidi, D., Tawfik, D. S., and Milo, R. (2011) The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters Biochemistry 50, 4402-4410
    • (2011) Biochemistry , vol.50 , pp. 4402-4410
    • Bar-Even, A.1    Noor, E.2    Savir, Y.3    Liebermeister, W.4    Davidi, D.5    Tawfik, D.S.6    Milo, R.7
  • 31
    • 30744475705 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa C5-mannuronan epimerase: Steady-state kinetics and characterization of the product
    • Jerga, A., Raychaudhuri, A., and Tipton, P. A. (2006) Pseudomonas aeruginosa C5-mannuronan epimerase: steady-state kinetics and characterization of the product Biochemistry 45, 552-560
    • (2006) Biochemistry , vol.45 , pp. 552-560
    • Jerga, A.1    Raychaudhuri, A.2    Tipton, P.A.3
  • 32
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L. A. and Sternberg, M. J. (2009) Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4, 363-371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 34
    • 0001547462 scopus 로고
    • Comparable rates for cleavage of amide and ester bonds through nucleophilic-attack by carboxylate anion and general acid catalysis by metal-bound water in a carboxypeptidase-a model
    • Suh, J. H., Park, T. H., and Hwang, B. K. (1992) Comparable rates for cleavage of amide and ester bonds through nucleophilic-attack by carboxylate anion and general acid catalysis by metal-bound water in a carboxypeptidase-a model J. Am. Chem. Soc. 114, 5141-5146
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5141-5146
    • Suh, J.H.1    Park, T.H.2    Hwang, B.K.3
  • 35
    • 79957616635 scopus 로고    scopus 로고
    • Development of screening assays and discovery of initial inhibitors of pneumococcal peptidoglycan deacetylase PgdA
    • Bui, N. K., Turk, S., Buckenmaier, S., Stevenson-Jones, F., Zeuch, B., Gobec, S., and Vollmer, W. (2011) Development of screening assays and discovery of initial inhibitors of pneumococcal peptidoglycan deacetylase PgdA Biochem. Pharmacol. 82, 43-52
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 43-52
    • Bui, N.K.1    Turk, S.2    Buckenmaier, S.3    Stevenson-Jones, F.4    Zeuch, B.5    Gobec, S.6    Vollmer, W.7
  • 36
    • 58149488638 scopus 로고    scopus 로고
    • Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin
    • Deng, D. M., Urch, J. E., ten Cate, J. M., Rao, V. A., van Aalten, D. M., and Crielaard, W. (2009) Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin J. Bacteriol. 191, 394-402
    • (2009) J. Bacteriol. , vol.191 , pp. 394-402
    • Deng, D.M.1    Urch, J.E.2    Ten Cate, J.M.3    Rao, V.A.4    Van Aalten, D.M.5    Crielaard, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.