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Volumn 50, Issue 12, 2006, Pages 4062-4069

Mutational analysis of class A and class B penicillin-binding proteins in Streptococcus gordonii

Author keywords

[No Author keywords available]

Indexed keywords

CLASS A PENICILLIN BINDING PROTEIN; CLASS B PENICILLIN BINDING PROTEIN; GAMMA GLUTAMYLTRANSFERASE; GLYCAN; GLYCOSYLTRANSFERASE; MONOMER; MURAMYL PEPTIDE; PENICILLIN BINDING PROTEIN; PENICILLIN G; TRITIUM;

EID: 33845254291     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.00677-06     Document Type: Article
Times cited : (19)

References (42)
  • 1
    • 0001994881 scopus 로고    scopus 로고
    • Susceptibility testing of antimicrobials in liquid medium
    • V. Lorian (ed.), Williams and Wilkins, Baltimore, Md.
    • Amsterdam, D. 1996. Susceptibility testing of antimicrobials in liquid medium, p. 52-111. In V. Lorian (ed.), Antibiotics in laboratory medicine. Williams and Wilkins, Baltimore, Md.
    • (1996) Antibiotics in Laboratory Medicine , pp. 52-111
    • Amsterdam, D.1
  • 4
    • 0023887565 scopus 로고
    • Construction and properties of a new insertion vector, pJDC9, that is protected by transcriptional terminators and useful for cloning of DNA from Streptococcus pneumoniae
    • Chen, J.-D., and D. A. Morrison. 1988. Construction and properties of a new insertion vector, pJDC9, that is protected by transcriptional terminators and useful for cloning of DNA from Streptococcus pneumoniae. Gene 64:155-164.
    • (1988) Gene , vol.64 , pp. 155-164
    • Chen, J.-D.1    Morrison, D.A.2
  • 5
    • 0021512404 scopus 로고
    • The stability of the o-phthalaldehyde/2-mercaptoethanol derivatives of amino acids: An investigation using high-pressure liquid chromatography with a precolumn derivatization technique
    • Cooper, J. D., G. Ogden, J. McIntosh, and D. C. Turnell. 1984. The stability of the o-phthalaldehyde/2-mercaptoethanol derivatives of amino acids: an investigation using high-pressure liquid chromatography with a precolumn derivatization technique. Anal. Biochem. 142:98-102.
    • (1984) Anal. Biochem. , vol.142 , pp. 98-102
    • Cooper, J.D.1    Ogden, G.2    McIntosh, J.3    Turnell, D.C.4
  • 6
    • 0024981142 scopus 로고
    • High-performance liquid chromatography of cystathionine, lanthionine and aminoethylcysteine using o-phthaldialdehyde precolumn derivatization
    • Costa, M., I. Pecci, B. Pensa, M. Fontana, and D. Cavallini. 1989. High-performance liquid chromatography of cystathionine, lanthionine and aminoethylcysteine using o-phthaldialdehyde precolumn derivatization. J. Chromatogr. 490:404-410.
    • (1989) J. Chromatogr. , vol.490 , pp. 404-410
    • Costa, M.1    Pecci, I.2    Pensa, B.3    Fontana, M.4    Cavallini, D.5
  • 7
    • 0030009759 scopus 로고    scopus 로고
    • A complex four-gene operon containing essential cell division gene pbpB in Bacillus subtilis. 3
    • Daniel, R., A. Williams, and J. Errington. 1996. A complex four-gene operon containing essential cell division gene pbpB in Bacillus subtilis. 3. Bacteriol. 178:2343-2350.
    • (1996) Bacteriol. , vol.178 , pp. 2343-2350
    • Daniel, R.1    Williams, A.2    Errington, J.3
  • 8
    • 0026639828 scopus 로고
    • Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain. the role of penicillin binding protein 2A
    • de Jonge, B., Y. Chang, D. Gage, and A. Tomasz. 1992. Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain. The role of penicillin binding protein 2A. J. Biol. Chem. 267:11248-11254.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11248-11254
    • De Jonge, B.1    Chang, Y.2    Gage, D.3    Tomasz, A.4
  • 9
    • 0032985224 scopus 로고    scopus 로고
    • Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: Viability, characteristics, and implications for peptidoglycan synthesis
    • Denome, S. A., P. K. Elf, T. A. Henderson, D. E. Nelson, and K. D. Young. 1999. Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis. J. Bacteriol. 181:3981-3993.
    • (1999) J. Bacteriol. , vol.181 , pp. 3981-3993
    • Denome, S.A.1    Elf, P.K.2    Henderson, T.A.3    Nelson, D.E.4    Young, K.D.5
  • 10
    • 0037371611 scopus 로고    scopus 로고
    • Functional characterization of penicillin-binding protein 1b from Streptococcus pneumoniae
    • Di Guilmi, A. M., A. Dessen, O. Dideberg, and T. Vernet. 2003. Functional characterization of penicillin-binding protein 1b from Streptococcus pneumoniae. J. Bacteriol. 185:1650-1658.
    • (2003) J. Bacteriol. , vol.185 , pp. 1650-1658
    • Di Guilmi, A.M.1    Dessen, A.2    Dideberg, O.3    Vernet, T.4
  • 11
    • 0031771077 scopus 로고    scopus 로고
    • Identification, purification, and characterization of transpeptidase and glycosyltransferase domains of Streptococcus pneumoniae penicillin-binding protein 1a
    • Di Guilmi, A. M., N. Mouz, J.-P. Andrieu, J. Hoskins, S. R. Jaskunas, J. Gagnon, O. Dideberg, and T. Vernet. 1998. Identification, purification, and characterization of transpeptidase and glycosyltransferase domains of Streptococcus pneumoniae penicillin-binding protein 1a. J. Bacteriol. 180:5652-5659.
    • (1998) J. Bacteriol. , vol.180 , pp. 5652-5659
    • Di Guilmi, A.M.1    Mouz, N.2    Andrieu, J.-P.3    Hoskins, J.4    Jaskunas, S.R.5    Gagnon, J.6    Dideberg, O.7    Vernet, T.8
  • 12
    • 0032955590 scopus 로고    scopus 로고
    • Glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae is membrane associated
    • Di Guilmi, A. M., N. Mouz, L. Martin, J. Hoskins, S. R. Jaskunas, O. Dideberg, and T. Vernet. 1999. Glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae is membrane associated. J. Bacteriol. 181:2773-2781.
    • (1999) J. Bacteriol. , vol.181 , pp. 2773-2781
    • Di Guilmi, A.M.1    Mouz, N.2    Martin, L.3    Hoskins, J.4    Jaskunas, S.R.5    Dideberg, O.6    Vernet, T.7
  • 13
    • 0027198174 scopus 로고
    • Identity of viridans streptococci isolated from cases of infective endocarditis
    • Douglas, C. W., J. Heath, K. K. Hampton, and F. E. Preston. 1993. Identity of viridans streptococci isolated from cases of infective endocarditis. J. Med. Microbiol. 39:179-182.
    • (1993) J. Med. Microbiol. , vol.39 , pp. 179-182
    • Douglas, C.W.1    Heath, J.2    Hampton, K.K.3    Preston, F.E.4
  • 14
    • 0026178870 scopus 로고
    • Ecology of viridans streptococci in the oral cavity and pharynx
    • Frandsen, E. V., V. Pedrazzoli, and M. Kilian. 1991. Ecology of viridans streptococci in the oral cavity and pharynx. Oral Microbiol. Immunol. 6:129-133.
    • (1991) Oral Microbiol. Immunol. , vol.6 , pp. 129-133
    • Frandsen, E.V.1    Pedrazzoli, V.2    Kilian, M.3
  • 15
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon, C., and G. Deleage. 1995. SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput. Appl. Biosci. 11:681-684.
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 16
    • 0026049801 scopus 로고
    • Serine beta-lactamases and penicillin-binding proteins
    • Ghuysen, J. M. 1991. Serine beta-lactamases and penicillin-binding proteins. Annu. Rev. Microbiol. 45:37-67.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 37-67
    • Ghuysen, J.M.1
  • 17
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: An enigmatic family of orthologs and paralogs
    • Goffin, C., and J.-M. Ghuysen. 1998. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62:1079-1093.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1079-1093
    • Goffin, C.1    Ghuysen, J.-M.2
  • 18
    • 0034595512 scopus 로고    scopus 로고
    • The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: Implication in drug resistance
    • Gordon, E., N. Mouz, E. Duee, and O. Dideberg. 2000. The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance. J. Mol. Biol. 299:477-485.
    • (2000) J. Mol. Biol. , vol.299 , pp. 477-485
    • Gordon, E.1    Mouz, N.2    Duee, E.3    Dideberg, O.4
  • 19
    • 0030003591 scopus 로고    scopus 로고
    • Penicillin-binding proteins 2b and 2x of Streptococcus pneumoniae are primary resistance determinants for different classes of beta-lactam antibiotics
    • Grebe, T., and R. Hakenbeck. 1996. Penicillin-binding proteins 2b and 2x of Streptococcus pneumoniae are primary resistance determinants for different classes of beta-lactam antibiotics. Antimicrob. Agents Chemother. 40:829-834.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 829-834
    • Grebe, T.1    Hakenbeck, R.2
  • 20
    • 33845273792 scopus 로고    scopus 로고
    • Mutations in penicillin-binding protein (PBP) genes and in non-PBP genes during selection of penicillin-resistant Streptococcus gordonii
    • Haenni, M., and P. Moreillon. 2006. Mutations in penicillin-binding protein (PBP) genes and in non-PBP genes during selection of penicillin-resistant Streptococcus gordonii. Antimicrob. Agents Chemother. 50:4053-4061.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 4053-4061
    • Haenni, M.1    Moreillon, P.2
  • 21
    • 0022538204 scopus 로고
    • Penicillin-binding proteins of penicillin-susceptible and -resistant pneumococci: Immunological relatedness of altered proteins and changes in peptides carrying the beta-lactam binding site
    • Hakenbeck, R., H. Ellerbrok, T. Briese, S. Handwerger, and A. Tomasz. 1986. Penicillin-binding proteins of penicillin-susceptible and -resistant pneumococci: immunological relatedness of altered proteins and changes in peptides carrying the beta-lactam binding site. Antimicrob. Agents Chemother. 30:553-558.
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 553-558
    • Hakenbeck, R.1    Ellerbrok, H.2    Briese, T.3    Handwerger, S.4    Tomasz, A.5
  • 23
    • 0018111832 scopus 로고
    • Streptococci and the human oral flora
    • F. A. Skinner and L. B. Quesnel (ed.). Academic Press, Inc., New York, N. Y.
    • Hardy, J. M., and P. D. Marsh. 1978. Streptococci and the human oral flora, p. 157-206. In F. A. Skinner and L. B. Quesnel (ed.). Streptococci. Academic Press, Inc., New York, N. Y.
    • (1978) Streptococci , pp. 157-206
    • Hardy, J.M.1    Marsh, P.D.2
  • 24
    • 0008955958 scopus 로고
    • A fixation and imbedding procedure for thin-sectioning bacteria
    • A. I. Laskin and H. Lechevalier (ed.), CRC Press, Cleveland, Ohio
    • Higgins, M. L. 1973. A fixation and imbedding procedure for thin-sectioning bacteria, p. 686-689. In A. I. Laskin and H. Lechevalier (ed.), CRC handbook of microbiology, vol. 1. CRC Press, Cleveland, Ohio.
    • (1973) CRC Handbook of Microbiology , vol.1 , pp. 686-689
    • Higgins, M.L.1
  • 26
    • 0027446117 scopus 로고
    • Deletion analysis of the essentiality of penicillin-binding proteins 1A, 2B and 2X of Streptococcus pneumoniae
    • Kell, C. M., U. K. Sharma, C. G. Dowson, C. Town, T. S. Balganesh, and B. G. Spratt. 1993. Deletion analysis of the essentiality of penicillin-binding proteins 1A, 2B and 2X of Streptococcus pneumoniae. FEMS Microbiol. Lett. 106:171-175.
    • (1993) FEMS Microbiol. Lett. , vol.106 , pp. 171-175
    • Kell, C.M.1    Sharma, U.K.2    Dowson, C.G.3    Town, C.4    Balganesh, T.S.5    Spratt, B.G.6
  • 27
    • 0036164801 scopus 로고    scopus 로고
    • PCR ligation mutagenesis in transformable streptococci: Application and efficiency
    • Lau, P. C. Y., C. K. Sung, J. H. Lee, D. A. Morrison, and D. G. Cvitkovitch. 2002. PCR ligation mutagenesis in transformable streptococci: application and efficiency. J. Microbiol. Methods 49:193-205.
    • (2002) J. Microbiol. Methods , vol.49 , pp. 193-205
    • Lau, P.C.Y.1    Sung, C.K.2    Lee, J.H.3    Morrison, D.A.4    Cvitkovitch, D.G.5
  • 28
    • 10044253923 scopus 로고
    • Utilization of lipid-linked precursors and the formation of peptidoglycan in the process of cell growth and division: Membrane enzymes involved in the final steps of peptidoglycan synthesis and the mechanism of their regulation
    • J.-M. Ghuysen and R. Hakenbeck (ed.), Elsevier, Amsterdam, The Netherlands
    • Matsuhashi, M. 1994. Utilization of lipid-linked precursors and the formation of peptidoglycan in the process of cell growth and division: membrane enzymes involved in the final steps of peptidoglycan synthesis and the mechanism of their regulation, p. 55-71. In J.-M. Ghuysen and R. Hakenbeck (ed.), Bacterial cell wall. Elsevier, Amsterdam, The Netherlands.
    • (1994) Bacterial Cell Wall , pp. 55-71
    • Matsuhashi, M.1
  • 29
    • 0242437870 scopus 로고    scopus 로고
    • Growth and division of Streptococcus pneumoniae: Localization of the high molecular weight penicillin-binding proteins during the cell cycle
    • Morlot, C., A. Zapun, O. Dideberg, and T. Vernet. 2003. Growth and division of Streptococcus pneumoniae: localization of the high molecular weight penicillin-binding proteins during the cell cycle. Mol. Microbiol. 50:845-855.
    • (2003) Mol. Microbiol. , vol.50 , pp. 845-855
    • Morlot, C.1    Zapun, A.2    Dideberg, O.3    Vernet, T.4
  • 30
    • 2142770267 scopus 로고    scopus 로고
    • Biochemical characterization of Streptococcus pneumoniae penicillin-binding protein-2b and its implication in beta-lactam resistance
    • Pagliero, E., L. Chesnel, J. Hopkins, J. Croize, O. Dideberg, T. Vernet, and A. M. Di Guilmi. 2004. Biochemical characterization of Streptococcus pneumoniae penicillin-binding protein-2b and its implication in beta-lactam resistance. Antimicrob. Agents Chemother. 48:1848-1855.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1848-1855
    • Pagliero, E.1    Chesnel, L.2    Hopkins, J.3    Croize, J.4    Dideberg, O.5    Vernet, T.6    Di Guilmi, A.M.7
  • 31
    • 0033014014 scopus 로고    scopus 로고
    • Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins
    • Paik, J., I. Kern, R. Lurz, and R. Hakenbeck. 1999. Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins. J. Bacteriol. 181:3852-3856.
    • (1999) J. Bacteriol. , vol.181 , pp. 3852-3856
    • Paik, J.1    Kern, I.2    Lurz, R.3    Hakenbeck, R.4
  • 32
    • 0029988098 scopus 로고    scopus 로고
    • X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme
    • Pares, S., N. Mouz, Y. Petillot, R. Hakenbeck, and O. Dideberg. 1996. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 3:284-289.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 284-289
    • Pares, S.1    Mouz, N.2    Petillot, Y.3    Hakenbeck, R.4    Dideberg, O.5
  • 33
    • 0030600488 scopus 로고    scopus 로고
    • Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS)
    • Podbielski, A., B. Spellerberg, M. Woischnik, B. Pohl, and R. Lutticken. 1996. Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS). Gene 177:137-147.
    • (1996) Gene , vol.177 , pp. 137-147
    • Podbielski, A.1    Spellerberg, B.2    Woischnik, M.3    Pohl, B.4    Lutticken, R.5
  • 35
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electron-opaque stain in electron microscopy
    • Reynolds, E. S. 1963. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J. Cell Biol. 17:208-212.
    • (1963) J. Cell Biol. , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 36
    • 70449232353 scopus 로고
    • Etude au microscope électronique de plasmas contenant de l'acide désoxyribonucléique. I. Les nucléoïdes des bactéries en croissance active
    • Ryter, A., E. Kellenberger, A. Birchandersen, and O. Maaloe. 1958. Etude au microscope électronique de plasmas contenant de l'acide désoxyribonucléique. I. Les nucléoïdes des bactéries en croissance active. Z. Naturforsch B 13b:597-605.
    • (1958) Z. Naturforsch B , vol.13 B , pp. 597-605
    • Ryter, A.1    Kellenberger, E.2    Birchandersen, A.3    Maaloe, O.4
  • 38
    • 0022395367 scopus 로고
    • Cell wall and DNA cosegregation in Bacillus subtilis studied by electron microscope autoradiography
    • Schlaeppi, J. M., O. Schaefer, and D. Karamata. 1985. Cell wall and DNA cosegregation in Bacillus subtilis studied by electron microscope autoradiography. J. Bacteriol. 164:130-135.
    • (1985) J. Bacteriol. , vol.164 , pp. 130-135
    • Schlaeppi, J.M.1    Schaefer, O.2    Karamata, D.3
  • 39
    • 0013096299 scopus 로고
    • Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12
    • Spratt, B. G. 1975. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. USA. 72:2999-3003.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2999-3003
    • Spratt, B.G.1
  • 40
    • 0029803020 scopus 로고    scopus 로고
    • Disruption of the gene encoding penicillin-binding protein 2b (pbp2b) causes altered cell morphology and cease in exopolysaccharide production in Streptococcus thermophilus Sfi6
    • Stingele, F., and B. Mollet. 1996. Disruption of the gene encoding penicillin-binding protein 2b (pbp2b) causes altered cell morphology and cease in exopolysaccharide production in Streptococcus thermophilus Sfi6. Mol. Microbiol. 22:357-366.
    • (1996) Mol. Microbiol. , vol.22 , pp. 357-366
    • Stingele, F.1    Mollet, B.2
  • 41
    • 0020329162 scopus 로고
    • Total amino acid analysis using pre-column fluorescence derivatization
    • Umagat, H., P. Kucera, and L. F. Wen. 1982. Total amino acid analysis using pre-column fluorescence derivatization. J. Chromatogr. 239:463-474.
    • (1982) J. Chromatogr. , vol.239 , pp. 463-474
    • Umagat, H.1    Kucera, P.2    Wen, L.F.3
  • 42
    • 0019218755 scopus 로고
    • In vivo interaction of beta-lactam antibiotics with the penicillin-binding-proteins of Streptococcus pneumoniae
    • Williamson, R., R. Hakenback, and A. Tomasz. 1980. In vivo interaction of beta-lactam antibiotics with the penicillin-binding-proteins of Streptococcus pneumoniae. Antimicrob. Agents Chemother. 18:629-637.
    • (1980) Antimicrob. Agents Chemother. , vol.18 , pp. 629-637
    • Williamson, R.1    Hakenback, R.2    Tomasz, A.3


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