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Volumn 70, Issue 11, 2015, Pages 3032-3041

Activity of OP0595/β-lactam combinations against Gram-negative bacteria with extended-spectrum, AmpC and carbapenem-hydrolysing β-lactamases

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; AZTREONAM; BIAPENEM; CEFEPIME; ERTAPENEM; OP 0595; PIPERACILLIN; UNCLASSIFIED DRUG; AZABICYCLO DERIVATIVE; BETA LACTAM; BETA LACTAMASE; LACTAM; OP0595;

EID: 84949035632     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkv239     Document Type: Article
Times cited : (47)

References (25)
  • 1
    • 78650636489 scopus 로고    scopus 로고
    • Activities of NXL104 combinations with ceftazidime and aztreonam against carbapenemase-producing Enterobacteriaceae
    • Livermore DM, Mushtaq S,Warner M et al. Activities of NXL104 combinations with ceftazidime and aztreonam against carbapenemase-producing Enterobacteriaceae. Antimicrob Agents Chemother 2011; 55: 390-4.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 390-394
    • Livermore, D.M.1    Mushtaq, S.2    Warner, M.3
  • 2
    • 82955187694 scopus 로고    scopus 로고
    • In vitro activity of avibactam (NXL104) in combination with β-lactams against Gram-negative bacteria, including OXA-48 β-lactamase-producing Klebsiella pneumoniae
    • Aktaş Z, Kayacan C, Oncul O. In vitro activity of avibactam (NXL104) in combination with β-lactams against Gram-negative bacteria, including OXA-48 β-lactamase-producing Klebsiella pneumoniae. Int J Antimicrob Agents 2012; 39: 86-9.
    • (2012) Int J Antimicrob Agents , vol.39 , pp. 86-89
    • Aktaş, Z.1    Kayacan, C.2    Oncul, O.3
  • 3
    • 84943800632 scopus 로고    scopus 로고
    • OP0595, a new diazabicyclooctane: mode of action as a serine β-lactamase inhibitor, antibiotic and β-lactam 'enhancer'
    • Morinaka A, Tsutsumi Y, Yamada M et al. OP0595, a new diazabicyclooctane: mode of action as a serine β-lactamase inhibitor, antibiotic and β-lactam 'enhancer'. J Antimicrob Chemother 2015; 70: 2779-86.
    • (2015) J Antimicrob Chemother , vol.70 , pp. 2779-2786
    • Morinaka, A.1    Tsutsumi, Y.2    Yamada, M.3
  • 4
    • 0019192664 scopus 로고
    • Activity of mecillinam alone and in combination with other β-lactam antibiotics
    • Fass RJ. Activity of mecillinam alone and in combination with other β-lactam antibiotics. Antimicrob Agents Chemother 1980; 18: 906-12.
    • (1980) Antimicrob Agents Chemother , vol.18 , pp. 906-912
    • Fass, R.J.1
  • 5
    • 0017192284 scopus 로고
    • Synergy of mecillinam, a ß-amidinopenicillanic acid derivative, combined with β-lactam antibiotics
    • Neu HC. Synergy of mecillinam, a ß-amidinopenicillanic acid derivative, combined with β-lactam antibiotics. Antimicrob Agents Chemother 1976; 10: 535-539.
    • (1976) Antimicrob Agents Chemother , vol.10 , pp. 535-539
    • Neu, H.C.1
  • 6
    • 0019389436 scopus 로고
    • Synergistic effect of cephalexin with mecillinam
    • Otsuki M. Synergistic effect of cephalexin with mecillinam. J Antibiot (Tokyo) 1981; 34: 739-52.
    • (1981) J Antibiot (Tokyo) , vol.34 , pp. 739-752
    • Otsuki, M.1
  • 7
    • 0017683098 scopus 로고
    • The mechanism of mecillinam
    • Spratt BG. The mechanism of mecillinam. J Antimicrob Chemother 1977; 3 Suppl B: 13-9.
    • (1977) J Antimicrob Chemother , vol.3 , pp. 13-19
    • Spratt, B.G.1
  • 8
    • 62549121211 scopus 로고    scopus 로고
    • Molecular mechanisms disrupting porin expression in ertapenem-resistant Klebsiella and Enterobacter spp. clinical isolates fromthe UK
    • Doumith M, Ellington MJ, Livermore DM et al. Molecular mechanisms disrupting porin expression in ertapenem-resistant Klebsiella and Enterobacter spp. clinical isolates fromthe UK. J Antimicrob Chemother 2009; 63: 659-67.
    • (2009) J Antimicrob Chemother , vol.63 , pp. 659-667
    • Doumith, M.1    Ellington, M.J.2    Livermore, D.M.3
  • 10
    • 0028263074 scopus 로고
    • Comparative in-vitro activity of biapenem against enterobacteria with β-lactamase-mediated antibiotic resistance
    • Chen HY, Livermore DM. Comparative in-vitro activity of biapenem against enterobacteria with β-lactamase-mediated antibiotic resistance. J Antimicrob Chemother 1994; 33: 453-64.
    • (1994) J Antimicrob Chemother , vol.33 , pp. 453-464
    • Chen, H.Y.1    Livermore, D.M.2
  • 11
    • 84926465439 scopus 로고    scopus 로고
    • Heterogeneous hydrolytic features for OXA-48-like β-lactamases
    • Oueslati S, Nordmann P, Poirel L. Heterogeneous hydrolytic features for OXA-48-like β-lactamases. J Antimicrob Chemother 2015; 70: 1059-63.
    • (2015) J Antimicrob Chemother , vol.70 , pp. 1059-1063
    • Oueslati, S.1    Nordmann, P.2    Poirel, L.3
  • 12
    • 0028214069 scopus 로고
    • In-vitro activity of biapenem, compared with imipenem and meropenem, against Pseudomonas aeruginosa strains and mutants with known resistance mechanisms
    • Chen HY, Livermore DM. In-vitro activity of biapenem, compared with imipenem and meropenem, against Pseudomonas aeruginosa strains and mutants with known resistance mechanisms. J Antimicrob Chemother 1994; 33: 949-58.
    • (1994) J Antimicrob Chemother , vol.33 , pp. 949-958
    • Chen, H.Y.1    Livermore, D.M.2
  • 13
    • 84888787952 scopus 로고    scopus 로고
    • Activity of MK-7655 combined with imipenem against Enterobacteriaceae and Pseudomonas aeruginosa
    • Livermore DM, Warner M, Mushtaq S. Activity of MK-7655 combined with imipenem against Enterobacteriaceae and Pseudomonas aeruginosa. J Antimicrob Chemother 2013; 68: 2286-90.
    • (2013) J Antimicrob Chemother , vol.68 , pp. 2286-2290
    • Livermore, D.M.1    Warner, M.2    Mushtaq, S.3
  • 14
    • 0027196080 scopus 로고
    • Role of cephalosporinase in carbapenem resistance of clinical isolates of Pseudomonas aeruginosa
    • Zhou XY, Kitzis MD, Gutmann L. Role of cephalosporinase in carbapenem resistance of clinical isolates of Pseudomonas aeruginosa. Antimicrob Agents Chemother 1993; 37: 1387-9.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 1387-1389
    • Zhou, X.Y.1    Kitzis, M.D.2    Gutmann, L.3
  • 15
    • 0030762264 scopus 로고    scopus 로고
    • Potentiation of β-lactams against Pseudomonas aeruginosa by Ro 48-1256, a bridged monobactam inhibitor of AmpC β-lactamases
    • Livermore DM, Chen HY. Potentiation of β-lactams against Pseudomonas aeruginosa by Ro 48-1256, a bridged monobactam inhibitor of AmpC β-lactamases. J Antimicrob Chemother 1997; 40: 335-43.
    • (1997) J Antimicrob Chemother , vol.40 , pp. 335-343
    • Livermore, D.M.1    Chen, H.Y.2
  • 16
    • 0017081909 scopus 로고
    • Mecillinam, a novel penicillanic acid derivative with unusual activity against Gram-negative bacteria
    • Neu HC. Mecillinam, a novel penicillanic acid derivative with unusual activity against Gram-negative bacteria. Antimicrob Agents Chemother 1976; 9: 793-9.
    • (1976) Antimicrob Agents Chemother , vol.9 , pp. 793-799
    • Neu, H.C.1
  • 17
    • 34248184558 scopus 로고    scopus 로고
    • Function of penicillin-binding protein 2 in viability and morphology of Pseudomonas aeruginosa
    • Legaree BA, Daniels K, Weadge JT et al. Function of penicillin-binding protein 2 in viability and morphology of Pseudomonas aeruginosa. J Antimicrob Chemother. 2007; 59: 411-24.
    • (2007) J Antimicrob Chemother. , vol.59 , pp. 411-424
    • Legaree, B.A.1    Daniels, K.2    Weadge, J.T.3
  • 18
    • 0028923077 scopus 로고
    • Biochemical comparison of imipenem, meropenem and biapenem: permeability, binding to penicillin-binding proteins, and stability to hydrolysis by β-lactamases
    • Yang Y, Bhachech N, Bush K. Biochemical comparison of imipenem, meropenem and biapenem: permeability, binding to penicillin-binding proteins, and stability to hydrolysis by β-lactamases. J Antimicrob Chemother 1995; 35: 75-84.
    • (1995) J Antimicrob Chemother , vol.35 , pp. 75-84
    • Yang, Y.1    Bhachech, N.2    Bush, K.3
  • 19
    • 84884764949 scopus 로고    scopus 로고
    • Kinetics of avibactam inhibition against Class A, C, and D β-lactamases
    • Ehmann DE, Jahic H, Ross PL et al. Kinetics of avibactam inhibition against Class A, C, and D β-lactamases. J Biol Chem 2013; 288: 27960-71.
    • (2013) J Biol Chem , vol.288 , pp. 27960-27971
    • Ehmann, D.E.1    Jahic, H.2    Ross, P.L.3
  • 20
    • 66149136478 scopus 로고    scopus 로고
    • In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2
    • Varma A, Young KD. In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2. J Bacteriol 2009; 191: 3526-33.
    • (2009) J Bacteriol , vol.191 , pp. 3526-3533
    • Varma, A.1    Young, K.D.2
  • 21
    • 0034528869 scopus 로고    scopus 로고
    • Selected amplification of the cell division genes ftsQ-ftsA-ftsZ in Escherichia coli
    • Vinella D, Cashel M, D'Ari R. Selected amplification of the cell division genes ftsQ-ftsA-ftsZ in Escherichia coli. Genetics 2000; 156: 1483-92.
    • (2000) Genetics , vol.156 , pp. 1483-1492
    • Vinella, D.1    Cashel, M.2    D'Ari, R.3
  • 22
    • 39749101237 scopus 로고    scopus 로고
    • Why spherical Escherichia coli dies: the inside story
    • Young KD. Why spherical Escherichia coli dies: the inside story. J Bacteriol 2008; 190: 1497-8.
    • (2008) J Bacteriol , vol.190 , pp. 1497-1498
    • Young, K.D.1
  • 23
    • 84923250957 scopus 로고    scopus 로고
    • Amdinocillin (mecillinam) resistance mutations in clinical isolates and laboratory-selected mutants of Escherichia coli
    • Thulin E, Sundqvist M, Andersson DI. Amdinocillin (mecillinam) resistance mutations in clinical isolates and laboratory-selected mutants of Escherichia coli. Antimicrob Agents Chemother 2015; 59: 1718-27.
    • (2015) Antimicrob Agents Chemother , vol.59 , pp. 1718-1727
    • Thulin, E.1    Sundqvist, M.2    Andersson, D.I.3
  • 24
    • 84896832898 scopus 로고    scopus 로고
    • In vitro activities of ceftazidimeavibactam and aztreonam-avibactam against 372 Gram-negative bacilli collected in 2011 and 2012 from 11 teaching hospitals in China
    • Wang X, Zhang F, Zhao C et al. In vitro activities of ceftazidimeavibactam and aztreonam-avibactam against 372 Gram-negative bacilli collected in 2011 and 2012 from 11 teaching hospitals in China. Antimicrob Agents Chemother 2014; 58: 1774-8.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 1774-1778
    • Wang, X.1    Zhang, F.2    Zhao, C.3
  • 25
    • 84940901399 scopus 로고    scopus 로고
    • In-vitro selection of ceftazidime-avibactam resistance in Enterobacteriaceae with KPC-3 carbapenemase
    • pii: AAC.00678-15
    • Livermore DM, Warner M, Jamrozy D et al. In-vitro selection of ceftazidime-avibactam resistance in Enterobacteriaceae with KPC-3 carbapenemase. Antimicrob Agents Chemother 2015; pii: AAC.00678-15.
    • (2015) Antimicrob Agents Chemother
    • Livermore, D.M.1    Warner, M.2    Jamrozy, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.