메뉴 건너뛰기




Volumn 54, Issue 5, 2010, Pages 1670-1677

Affinity of ceftaroline and other β-lactams for penicillin-binding proteins from Staphylococcus aureus and Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

CEFOTAXIME; CEFTAROLINE; CEFTRIAXONE; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 1; PENICILLIN BINDING PROTEIN 1B; PENICILLIN BINDING PROTEIN 2; PENICILLIN BINDING PROTEIN 2A; PENICILLIN BINDING PROTEIN 2B; PENICILLIN BINDING PROTEIN 2X; PENICILLIN BINDING PROTEIN 3; PENICILLIN BINDING PROTEIN 4; PENICILLIN G; UNCLASSIFIED DRUG;

EID: 77951249813     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00019-10     Document Type: Article
Times cited : (152)

References (65)
  • 1
    • 33645749939 scopus 로고    scopus 로고
    • The emergence of vancomycin-intermediate and vancomycin-resistant Staphylococcus aureus
    • Appelbaum, P. C. 2006. The emergence of vancomycin-intermediate and vancomycin-resistant Staphylococcus aureus. Clin. Microbiol. Infect. 12(Suppl. 1): 16-23.
    • (2006) Clin. Microbiol. Infect. , vol.12 , Issue.SUPPL. 1 , pp. 16-23
    • Appelbaum, P.C.1
  • 2
    • 0032905812 scopus 로고    scopus 로고
    • Diversity of substitutions within or adjacent to conserved amino acid motifs of penicillin-binding protein 2X in cephalosporin-resistant Streptococcus pneumoniae isolates
    • Asahi, Y., Y. Takeuchi, and K. Ubukata. 1999. Diversity of substitutions within or adjacent to conserved amino acid motifs of penicillin-binding protein 2X in cephalosporin-resistant Streptococcus pneumoniae isolates. Antimicrob. Agents Chemother. 43:1252-1255.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1252-1255
    • Asahi, Y.1    Takeuchi, Y.2    Ubukata, K.3
  • 3
    • 0031686778 scopus 로고    scopus 로고
    • Association of a Thr-371 substitution in a conserved amino acid motif of penicillin-binding protein 1A with penicillin resistance of Streptococcus pneumoniae
    • Asahi, Y., and K. Ubukata. 1998. Association of a Thr-371 substitution in a conserved amino acid motif of penicillin-binding protein 1A with penicillin resistance of Streptococcus pneumoniae. Antimicrob. Agents Chemother. 42:2267-2273.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2267-2273
    • Asahi, Y.1    Ubukata, K.2
  • 4
    • 0242437814 scopus 로고    scopus 로고
    • Antibacterial susceptibility of a vancomycin-resistant Staphylococcus aureus strain isolated at the Hershey Medical Center
    • Bozdogan, B., D. Esel, C. Whitener, F. A. Browne, and P. C. Appelbaum. 2003. Antibacterial susceptibility of a vancomycin-resistant Staphylococcus aureus strain isolated at the Hershey Medical Center. J. Antimicrob. Chemother. 52:864-868.
    • (2003) J. Antimicrob. Chemother. , vol.52 , pp. 864-868
    • Bozdogan, B.1    Esel, D.2    Whitener, C.3    Browne, F.A.4    Appelbaum, P.C.5
  • 5
    • 0000214977 scopus 로고    scopus 로고
    • Vancomycin-resistant Staphylococcus aureus - Pennsylvania, 2002
    • Centers for Disease Control and Prevention. 2002. Vancomycin-resistant Staphylococcus aureus - Pennsylvania, 2002. MMWR Morb. Mortal. Wkly. Rep. 51:902. http://www.cdc.gov/mmwr//preview/mmwrhtml/mm5126a1.htm.
    • (2002) MMWR Morb. Mortal. Wkly. Rep. , vol.51 , pp. 902
  • 6
    • 0033402097 scopus 로고    scopus 로고
    • Penicillin-binding protein-mediated resistance in pneumococci and staphylococci
    • Chambers, H. F. 1999. Penicillin-binding protein-mediated resistance in pneumococci and staphylococci. J. Infect. Dis. 179(Suppl. 2):S353-S359.
    • (1999) J. Infect. Dis. , vol.179 , Issue.SUPPL. 2
    • Chambers, H.F.1
  • 7
    • 0025309479 scopus 로고
    • Binding of β-lactam antibiotics to penicillin-binding proteins in methicillin-resistant Staphylococcus aureus
    • Chambers, H. F., and M. Sachdeva. 1990. Binding of β-lactam antibiotics to penicillin-binding proteins in methicillin-resistant Staphylococcus aureus. J. Infect. Dis. 161:1170-1176.
    • (1990) J. Infect. Dis. , vol.161 , pp. 1170-1176
    • Chambers, H.F.1    Sachdeva, M.2
  • 8
    • 33646693907 scopus 로고    scopus 로고
    • Clinical and Laboratory Standards Institute. Approved standard M07-A8. Eighth edition. Clinical Laboratory Standards Institute, Wayne, PA
    • Clinical and Laboratory Standards Institute. 2009. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically. Approved standard M07-A8. Eighth edition. Clinical Laboratory Standards Institute, Wayne, PA.
    • (2009) Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria That Grow Aerobically
  • 9
    • 33646696219 scopus 로고    scopus 로고
    • Clinical and Laboratory Standards Institute. Approved standard M100-S17. Seventeenth informational supplement. Clinical and Laboratory Standards Institute, Wayne, PA
    • Clinical and Laboratory Standards Institute. 2006. Performance standards for antimicrobial susceptibility testing. Approved standard M100-S17. Seventeenth informational supplement. Clinical and Laboratory Standards Institute, Wayne, PA.
    • (2006) Performance Standards for Antimicrobial Susceptibility Testing
  • 10
    • 33646696219 scopus 로고    scopus 로고
    • Clinical and Laboratory Standards Institute. Approved standard M100-S19. Nineteenth informational supplement. Clinical and Laboratory Standards Institute, Wayne, PA
    • Clinical and Laboratory Standards Institute. 2009. Performance standards for antimicrobial susceptibility testing. Approved standard M100-S19. Nineteenth informational supplement. Clinical and Laboratory Standards Institute, Wayne, PA.
    • (2009) Performance Standards for Antimicrobial Susceptibility Testing
  • 11
    • 34447254695 scopus 로고    scopus 로고
    • Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae
    • Davies, T. A., M. G. Page, W. Shang, T. Andrew, M. Kania, and K. Bush. 2007. Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae. Antimicrob. Agents Chemother. 51:2621-2624.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2621-2624
    • Davies, T.A.1    Page, M.G.2    Shang, W.3    Andrew, T.4    Kania, M.5    Bush, K.6
  • 12
    • 0026639828 scopus 로고
    • Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain. the role of penicillin binding protein 2A
    • de Jonge, B. L., Y. S. 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.L.1    Chang, Y.S.2    Gage, D.3    Tomasz, A.4
  • 15
    • 55849104841 scopus 로고    scopus 로고
    • In vitro activity of ceftaroline against Streptococcus pneumoniae isolates exhibiting resistance to penicillin, amoxicillin, and cefotaxime
    • Fenoll, A., L. Aguilar, O. Robledo, M. J. Gimenez, J. J. Granizo, D. Biek, and D. Tarrago. 2008. In vitro activity of ceftaroline against Streptococcus pneumoniae isolates exhibiting resistance to penicillin, amoxicillin, and cefotaxime. Antimicrob. Agents Chemother. 52:4209-4210.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 4209-4210
    • Fenoll, A.1    Aguilar, L.2    Robledo, O.3    Gimenez, M.J.4    Granizo, J.J.5    Biek, D.6    Tarrago, D.7
  • 16
    • 50949105050 scopus 로고    scopus 로고
    • In vitro profiling of ceftaroline against a collection of recent bacterial clinical isolates from across the United States
    • Ge, Y., D. Biek, G. H. Talbot, and D. F. Sahm. 2008. In vitro profiling of ceftaroline against a collection of recent bacterial clinical isolates from across the United States. Antimicrob. Agents Chemother. 52:3398-3407.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 3398-3407
    • Ge, Y.1    Biek, D.2    Talbot, G.H.3    Sahm, D.F.4
  • 17
    • 0022613456 scopus 로고
    • Possible physiological functions of penicillin-binding proteins in Staphylococcus aureus
    • Georgopapadakou, N. H., B. A. Dix, and Y. R. Mauriz. 1986. Possible physiological functions of penicillin-binding proteins in Staphylococcus aureus. Antimicrob. Agents Chemother. 29:333-336.
    • (1986) Antimicrob. Agents Chemother. , vol.29 , pp. 333-336
    • Georgopapadakou, N.H.1    Dix, B.A.2    Mauriz, Y.R.3
  • 18
    • 0030003591 scopus 로고    scopus 로고
    • Penicillin-binding proteins 2b and 2x of Streptococcus pneumoniae are primary resistance determinants for different classes of β-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 β-lactam antibiotics. Antimicrob. Agents Chemother. 40:829-834.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 829-834
    • Grebe, T.1    Hakenbeck, R.2
  • 19
    • 24344466955 scopus 로고    scopus 로고
    • Beta-lactams against methicillin-resistant Staphylococcus aureus
    • Guignard, B., J. M. Entenza, and P. Moreillon. 2005. Beta-lactams against methicillin-resistant Staphylococcus aureus. Curr. Opin. Pharmacol. 5:479-489.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 479-489
    • Guignard, B.1    Entenza, J.M.2    Moreillon, P.3
  • 20
    • 0028895412 scopus 로고
    • Point mutations in Staphylococcus aureus PBP 2 gene affect penicillin-binding kinetics and are associated with resistance
    • Hackbarth, C. J., T. Kocagoz, S. Kocagoz, and H. F. Chambers. 1995. Point mutations in Staphylococcus aureus PBP 2 gene affect penicillin-binding kinetics and are associated with resistance. Antimicrob. Agents Chemother. 39:103-106.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 103-106
    • Hackbarth, C.J.1    Kocagoz, T.2    Kocagoz, S.3    Chambers, H.F.4
  • 21
    • 0033031086 scopus 로고    scopus 로고
    • Beta-lactam-resistant Streptococcus pneumoniae: Epidemiology and evolutionary mechanism
    • Hakenbeck, R. 1999. Beta-lactam-resistant Streptococcus pneumoniae: epidemiology and evolutionary mechanism. Chemotherapy 45:83-94.
    • (1999) Chemotherapy , vol.45 , pp. 83-94
    • Hakenbeck, R.1
  • 22
    • 0031940944 scopus 로고    scopus 로고
    • Mosaic genes and their role in penicillin-resistant Streptococcus pneumoniae
    • Hakenbeck, R. 1998. Mosaic genes and their role in penicillin-resistant Streptococcus pneumoniae. Electrophoresis 19:597-601.
    • (1998) Electrophoresis , vol.19 , pp. 597-601
    • Hakenbeck, R.1
  • 23
    • 0031594816 scopus 로고    scopus 로고
    • Acquisition of five high-Mr penicillin-binding protein variants during transfer of high-level beta-lactam resistance from Streptococcus mitis to Streptococcus pneumoniae
    • Hakenbeck, R., A. Konig, I. Kern, M. van der Linden, W. Keck, D. Billot- Klein, R. Legrand, B. Schoot, and L. Gutmann. 1998. Acquisition of five high-Mr penicillin-binding protein variants during transfer of high-level beta-lactam resistance from Streptococcus mitis to Streptococcus pneumoniae. J. Bacteriol. 180:1831-1840.
    • (1998) J. Bacteriol. , vol.180 , pp. 1831-1840
    • Hakenbeck, R.1    Konig, A.2    Kern, I.3    Van Der Linden, M.4    Keck, W.5    Billot- Klein, D.6    Legrand, R.7    Schoot, B.8    Gutmann, L.9
  • 24
    • 0023093968 scopus 로고
    • Interaction of nonlytic β-lactams with penicillin-binding proteins in Streptococcus pneumoniae
    • Hakenbeck, R., S. Tornette, and N. F. Adkinson. 1987. Interaction of nonlytic β-lactams with penicillin-binding proteins in Streptococcus pneumoniae. J. Gen. Microbiol. 133:755-760.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 755-760
    • Hakenbeck, R.1    Tornette, S.2    Adkinson, N.F.3
  • 25
    • 0035115180 scopus 로고    scopus 로고
    • In vitro and in vivo properties of Ro 63-9141, a novel broadspectrum cephalosporin with activity against methicillin-resistant staphylococci
    • Hebeisen, P., I. Heinze-Krauss, P. Angehrn, P. Hohl, M. G. Page, and R. L. Then. 2001. In vitro and in vivo properties of Ro 63-9141, a novel broadspectrum cephalosporin with activity against methicillin-resistant staphylococci. Antimicrob. Agents Chemother. 45:825-836.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 825-836
    • Hebeisen, P.1    Heinze-Krauss, I.2    Angehrn, P.3    Hohl, P.4    Page, M.G.5    Then, R.L.6
  • 26
    • 0032906330 scopus 로고    scopus 로고
    • Role of inhibition of penicillin binding proteins and cell wall crosslinking by β-lactam antibiotics in low- And high-level methicillin resistance of Staphylococcus aureus
    • Higashi, Y., A. Wakabayashi, Y. Matsumoto, Y. Watanabe, and A. Ohno. 1999. Role of inhibition of penicillin binding proteins and cell wall crosslinking by β-lactam antibiotics in low- and high-level methicillin resistance of Staphylococcus aureus. Chemotherapy 45:37-47.
    • (1999) Chemotherapy , vol.45 , pp. 37-47
    • Higashi, Y.1    Wakabayashi, A.2    Matsumoto, Y.3    Watanabe, Y.4    Ohno, A.5
  • 28
    • 35548957431 scopus 로고    scopus 로고
    • LEADER surveillance program results for 2006: An activity and spectrum analysis of linezolid using clinical isolates from the United States (50 medical centers)
    • Jones, R. N., T. R. Fritsche, H. S. Sader, and J. E. Ross. 2007. LEADER surveillance program results for 2006: an activity and spectrum analysis of linezolid using clinical isolates from the United States (50 medical centers). Diagn. Microbiol. Infect. Dis. 59:309-317.
    • (2007) Diagn. Microbiol. Infect. Dis. , vol.59 , pp. 309-317
    • Jones, R.N.1    Fritsche, T.R.2    Sader, H.S.3    Ross, J.E.4
  • 30
    • 0942279626 scopus 로고    scopus 로고
    • PBP 2a mutations producing very-high-level resistance to β-lactams
    • Katayama, Y., H. Z. Zhang, and H. F. Chambers. 2004. PBP 2a mutations producing very-high-level resistance to β-lactams. Antimicrob. Agents Chemother. 48:453-459.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 453-459
    • Katayama, Y.1    Zhang, H.Z.2    Chambers, H.F.3
  • 31
    • 4644341061 scopus 로고    scopus 로고
    • Alterations of penicillin-binding proteins 1A, 2X, and 2B in Streptococcus pneumoniae isolates for which amoxicillin MICs are higher than penicillin MICs
    • Kosowska, K., M. R. Jacobs, S. Bajaksouzian, L. Koeth, and P. C. Appelbaum. 2004. Alterations of penicillin-binding proteins 1A, 2X, and 2B in Streptococcus pneumoniae isolates for which amoxicillin MICs are higher than penicillin MICs. Antimicrob. Agents Chemother. 48:4020-4022.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4020-4022
    • Kosowska, K.1    Jacobs, M.R.2    Bajaksouzian, S.3    Koeth, L.4    Appelbaum, P.C.5
  • 33
    • 57049173575 scopus 로고    scopus 로고
    • Incidence and characteristics of vancomycin nonsusceptible strains of methicillin-resistant Staphylococcus aureus at Hershey Medical Center
    • Kosowska-Shick, K., L. M. Ednie, P. McGhee, K. Smith, C. D. Todd, A. Wehler, and P. C. Appelbaum. 2008. Incidence and characteristics of vancomycin nonsusceptible strains of methicillin-resistant Staphylococcus aureus at Hershey Medical Center. Antimicrob. Agents Chemother. 52: 4510-4513.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 4510-4513
    • Kosowska-Shick, K.1    Ednie, L.M.2    McGhee, P.3    Smith, K.4    Todd, C.D.5    Wehler, A.6    Appelbaum, P.C.7
  • 34
    • 66149132214 scopus 로고    scopus 로고
    • Binding of faropenem and other β-lactam agents to penicillin-binding proteins of pneumococci with various β-lactam susceptibilities
    • Kosowska-Shick, K., P. McGhee, and P. C. Appelbaum. 2009. Binding of faropenem and other β-lactam agents to penicillin-binding proteins of pneumococci with various β-lactam susceptibilities. Antimicrob. Agents Chemother. 53:2176-2180.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2176-2180
    • Kosowska-Shick, K.1    McGhee, P.2    Appelbaum, P.C.3
  • 35
    • 0025816587 scopus 로고
    • Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillinresistant clinical isolates of Streptococcus pneumoniae
    • Laible, G., B. G. Spratt, and R. Hakenbeck. 1991. Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillinresistant clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 5:1993-2002.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1993-2002
    • Laible, G.1    Spratt, B.G.2    Hakenbeck, R.3
  • 36
    • 14244254169 scopus 로고    scopus 로고
    • Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: Evidence for the cooperative functioning of PBP2, PBP4, and PBP2A
    • Leski, T. A., and A. Tomasz. 2005. Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: evidence for the cooperative functioning of PBP2, PBP4, and PBP2A. J. Bacteriol. 187:1815-1824.
    • (2005) J. Bacteriol. , vol.187 , pp. 1815-1824
    • Leski, T.A.1    Tomasz, A.2
  • 37
    • 0036829003 scopus 로고    scopus 로고
    • Structural basis for the β-lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus
    • Lim, D., and N. C. Strynadka. 2002. Structural basis for the β-lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus. Nat. Struct. Biol. 9:870-876.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 870-876
    • Lim, D.1    Strynadka, N.C.2
  • 38
    • 0028999211 scopus 로고
    • Decreased teicoplanin susceptibility of methicillin-resistant strains of Staphylococcus aureus
    • Mainardi, J. L., D. M. Shlaes, R. V. Goering, J. H. Shlaes, J. F. Acar, and F. W. Goldstein. 1995. Decreased teicoplanin susceptibility of methicillin-resistant strains of Staphylococcus aureus. J. Infect. Dis. 171:1646-1650.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1646-1650
    • Mainardi, J.L.1    Shlaes, D.M.2    Goering, R.V.3    Shlaes, J.H.4    Acar, J.F.5    Goldstein, F.W.6
  • 41
    • 55849101500 scopus 로고    scopus 로고
    • Staphylococcus aureus PBP4 is essential for β-lactam resistance in community-acquired methicillin-resistant strains
    • Memmi, G., S. R. Filipe, M. G. Pinho, Z. Fu, and A. Cheung. 2008. Staphylococcus aureus PBP4 is essential for β-lactam resistance in community-acquired methicillin-resistant strains. Antimicrob. Agents Chemother. 52: 3955-3966.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 3955-3966
    • Memmi, G.1    Filipe, S.R.2    Pinho, M.G.3    Fu, Z.4    Cheung, A.5
  • 42
    • 77952578858 scopus 로고    scopus 로고
    • Binding of ceftaroline to penicillin-binding proteins of Staphylococcus aureus and Streptococcus pneumoniae
    • 22 January posting date. [Epub ahead of print.] doi:10.1093/jac/dkp503
    • Moisan, H., M. Pruneau, and F. Malouin. 22 January 2010, posting date. Binding of ceftaroline to penicillin-binding proteins of Staphylococcus aureus and Streptococcus pneumoniae. J. Antimicrob. Chemother. [Epub ahead of print.] doi:10.1093/jac/dkp503.
    • (2010) J. Antimicrob. Chemother.
    • Moisan, H.1    Pruneau, M.2    Malouin, F.3
  • 43
    • 64549135399 scopus 로고    scopus 로고
    • Activity of the new cephalosporin ceftaroline against bacteraemia isolates from patients with community-acquired pneumonia
    • Morrissey, I., Y. Ge, and R. Janes. 2009. Activity of the new cephalosporin ceftaroline against bacteraemia isolates from patients with community-acquired pneumonia. Int. J. Antimicrob. Agents 33:515-519.
    • (2009) Int. J. Antimicrob. Agents , vol.33 , pp. 515-519
    • Morrissey, I.1    Ge, Y.2    Janes, R.3
  • 44
    • 0026787870 scopus 로고
    • Genetics of resistance to third-generation cephalosporins in clinical isolates of Streptococcus pneumoniae
    • Munoz, R., C. G. Dowson, M. Daniels, T. J. Coffey, C. Martin, R. Hakenbeck, and B. G. Spratt. 1992. Genetics of resistance to third-generation cephalosporins in clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 6:2461-2465.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2461-2465
    • Munoz, R.1    Dowson, C.G.2    Daniels, M.3    Coffey, T.J.4    Martin, C.5    Hakenbeck, R.6    Spratt, B.G.7
  • 45
    • 34547841550 scopus 로고    scopus 로고
    • In vitro activity of ceftaroline (PPI-0903M, T-91825) against bacteria with defined resistance mechanisms and phenotypes
    • Mushtaq, S., M. Warner, Y. Ge, K. Kaniga, and D. M. Livermore. 2007. In vitro activity of ceftaroline (PPI-0903M, T-91825) against bacteria with defined resistance mechanisms and phenotypes. J. Antimicrob. Chemother. 60:300-311.
    • (2007) J. Antimicrob. Chemother. , vol.60 , pp. 300-311
    • Mushtaq, S.1    Warner, M.2    Ge, Y.3    Kaniga, K.4    Livermore, D.M.5
  • 46
    • 0036236855 scopus 로고    scopus 로고
    • Effects of amino acid alterations in penicillin-binding proteins (PBPs) 1a, 2b, and 2x on PBP affinities of penicillin, ampicillin, amoxicillin, cefditoren, cefuroxime, cefprozil, and cefaclor in 18 clinical isolates of penicillin-susceptible, -intermediate, and -resistant pneumococci
    • Nagai, K., T. A. Davies, M. R. Jacobs, and P. C. Appelbaum. 2002. Effects of amino acid alterations in penicillin-binding proteins (PBPs) 1a, 2b, and 2x on PBP affinities of penicillin, ampicillin, amoxicillin, cefditoren, cefuroxime, cefprozil, and cefaclor in 18 clinical isolates of penicillin-susceptible, -intermediate, and -resistant pneumococci. Antimicrob. Agents Chemother. 46: 1273-1280.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1273-1280
    • Nagai, K.1    Davies, T.A.2    Jacobs, M.R.3    Appelbaum, P.C.4
  • 47
    • 0007363844 scopus 로고
    • The possible physiological roles of penicillin-binding proteins of methicillin-susceptible and methicillin-resistant Staphylococcus aureus
    • Okonogi, K., Y. Noji, M. Nakao, and A. Imada. 1995. The possible physiological roles of penicillin-binding proteins of methicillin-susceptible and methicillin-resistant Staphylococcus aureus. J. Infect. Chemother. 1:50-58.
    • (1995) J. Infect. Chemother. , vol.1 , pp. 50-58
    • Okonogi, K.1    Noji, Y.2    Nakao, M.3    Imada, A.4
  • 48
    • 0024331845 scopus 로고
    • Emergence of methicillin-resistant clones from cephamycin-resistant Staphylococcus aureus
    • Okonogi, K., Y. Noji, M. Kondo, A. Imada, and T. Yokota. 1989. Emergence of methicillin-resistant clones from cephamycin-resistant Staphylococcus aureus. J. Antimicrob. Chemother. 24:637-645.
    • (1989) J. Antimicrob. Chemother. , vol.24 , pp. 637-645
    • Okonogi, K.1    Noji, Y.2    Kondo, M.3    Imada, A.4    Yokota, T.5
  • 49
    • 56749154034 scopus 로고    scopus 로고
    • No relationship exists between PBP 2a amounts expressed in different MRSA strains obtained clinically and their β-lactam MIC values
    • Parvez, M. A., H. Shibata, T. Nakano, S. Niimi, N. Fujii, N. Arakaki, and T. Higuti. 2008. No relationship exists between PBP 2a amounts expressed in different MRSA strains obtained clinically and their β-lactam MIC values. J. Med. Invest. 55:246-253.
    • (2008) J. Med. Invest. , vol.55 , pp. 246-253
    • Parvez, M.A.1    Shibata, H.2    Nakano, T.3    Niimi, S.4    Fujii, N.5    Arakaki, N.6    Higuti, T.7
  • 51
    • 0035845487 scopus 로고    scopus 로고
    • An acquired and a native penicillin-binding protein cooperate in building the cell wall of drugresistant staphylococci
    • Pinho, M. G., H. de Lencastre, and A. Tomasz. 2001. An acquired and a native penicillin-binding protein cooperate in building the cell wall of drugresistant staphylococci. Proc. Natl. Acad. Sci. U. S. A. 98:10886-10891.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10886-10891
    • Pinho, M.G.1    De Lencastre, H.2    Tomasz, A.3
  • 52
    • 44049098886 scopus 로고    scopus 로고
    • A method to assay penicillin-binding proteins
    • Pucci, M. J., and T. J. Dougherty. 2008. A method to assay penicillin-binding proteins. Methods Mol. Med. 142:131-141.
    • (2008) Methods Mol. Med. , vol.142 , pp. 131-141
    • Pucci, M.J.1    Dougherty, T.J.2
  • 53
    • 34548583324 scopus 로고    scopus 로고
    • SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model
    • Regev-Yochay, G., K. Trzcinski, C. M. Thompson, M. Lipsitch, and R. Malley. 2007. SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model. J. Bacteriol. 189:6532-6539.
    • (2007) J. Bacteriol. , vol.189 , pp. 6532-6539
    • Regev-Yochay, G.1    Trzcinski, K.2    Thompson, C.M.3    Lipsitch, M.4    Malley, R.5
  • 55
    • 0033516654 scopus 로고    scopus 로고
    • Inactivated pbp4 in highly glycopeptide-resistant laboratory mutants of Staphylococcus aureus
    • Sieradzki, K., M. G. Pinho, and A. Tomasz. 1999. Inactivated pbp4 in highly glycopeptide-resistant laboratory mutants of Staphylococcus aureus. J. Biol. Chem. 274:18942-18946.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18942-18946
    • Sieradzki, K.1    Pinho, M.G.2    Tomasz, A.3
  • 56
    • 0030060360 scopus 로고    scopus 로고
    • In vitro selection of onestep mutants of Streptococcus pneumoniae resistant to different oral β-lactam antibiotics is associated with alterations of PBP2x
    • Sifaoui, F., M. D. Kitzis, and L. Gutmann. 1996. In vitro selection of onestep mutants of Streptococcus pneumoniae resistant to different oral β-lactam antibiotics is associated with alterations of PBP2x. Antimicrob. Agents Chemother. 40:152-156.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 152-156
    • Sifaoui, F.1    Kitzis, M.D.2    Gutmann, L.3
  • 57
    • 0028927085 scopus 로고
    • Alterations in penicillin-binding protein 2B from penicillin-resistant wild-type strains of Streptococcus pneumoniae
    • Smith, A. M., and K. P. Klugman. 1995. Alterations in penicillin-binding protein 2B from penicillin-resistant wild-type strains of Streptococcus pneumoniae. Antimicrob. Agents Chemother. 39:859-867.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 859-867
    • Smith, A.M.1    Klugman, K.P.2
  • 58
    • 0023184524 scopus 로고
    • Evolution of an inducible penicillin-target protein in methicillin-resistant Staphylococcus aureus by gene fusion
    • Song, M. D., M. Wachi, M. Doi, F. Ishino, and M. Matsuhashi. 1987. Evolution of an inducible penicillin-target protein in methicillin-resistant Staphylococcus aureus by gene fusion. FEBS Lett. 221:167-171.
    • (1987) FEBS Lett. , vol.221 , pp. 167-171
    • Song, M.D.1    Wachi, M.2    Doi, M.3    Ishino, F.4    Matsuhashi, M.5
  • 59
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • Spratt, B. G. 1994. Resistance to antibiotics mediated by target alterations. Science 264:388-393.
    • (1994) Science , vol.264 , pp. 388-393
    • Spratt, B.G.1
  • 60
    • 0021810288 scopus 로고
    • Role of an altered penicillin-binding protein in methicillin- And cephem-resistant Staphylococcus aureus
    • Utsui, Y., and T. Yokota. 1985. Role of an altered penicillin-binding protein in methicillin- and cephem-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 28:397-403.
    • (1985) Antimicrob. Agents Chemother. , vol.28 , pp. 397-403
    • Utsui, Y.1    Yokota, T.2
  • 61
    • 47749154496 scopus 로고    scopus 로고
    • Co-opting the cell wall in fighting methicillin-resistant Staphylococcus aureus: Potent inhibition of PBP 2a by two anti-MRSA β-lactam antibiotics
    • Villegas-Estrada, A., M. Lee, D. Hesek, S. B. Vakulenko, and S. Mobashery. 2008. Co-opting the cell wall in fighting methicillin-resistant Staphylococcus aureus: potent inhibition of PBP 2a by two anti-MRSA β-lactam antibiotics. J. Am. Chem. Soc. 130:9212-9213.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9212-9213
    • Villegas-Estrada, A.1    Lee, M.2    Hesek, D.3    Vakulenko, S.B.4    Mobashery, S.5
  • 62
    • 0019218755 scopus 로고
    • In vivo interaction of β-lactam antibiotics with the penicillin-binding proteins of Streptococcus pneumoniae
    • Williamson, R., R. Hakenbeck, and A. Tomasz. 1980. In vivo interaction of β-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    Hakenbeck, R.2    Tomasz, A.3
  • 63
    • 62949215691 scopus 로고    scopus 로고
    • An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: Mutational analysis of Thr338
    • Zerfass, I., R. Hakenbeck, and D. Denapaite. 2009. An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: mutational analysis of Thr338. Antimicrob. Agents Chemother. 53:1107-1115.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1107-1115
    • Zerfass, I.1    Hakenbeck, R.2    Denapaite, D.3
  • 65
    • 0032908481 scopus 로고    scopus 로고
    • BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins
    • Zhao, G., T. I. Meier, S. D. Kahl, K. R. Gee, and L. C. Blaszczak. 1999. BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins. Antimicrob. Agents Chemother. 43: 1124-1128.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1124-1128
    • Zhao, G.1    Meier, T.I.2    Kahl, S.D.3    Gee, K.R.4    Blaszczak, L.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.