메뉴 건너뛰기




Volumn 39, Issue , 2017, Pages 96-105

Inhibitors of metallo-β-lactamases

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE INHIBITOR; METALLO BETA LACTAMASE; ZINC; ANTIINFECTIVE AGENT; BETA LACTAM;

EID: 85034094152     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2017.10.026     Document Type: Review
Times cited : (93)

References (50)
  • 1
    • 0025128056 scopus 로고
    • Evolution of isopenicillin N synthase genes may have involved horizontal gene transfer
    • Landan, G., Cohen, G., Aharonowitz, Y., Shuali, Y., Graur, D., Shiffman, D., Evolution of isopenicillin N synthase genes may have involved horizontal gene transfer. Mol Biol Evol 7 (1990), 399–406.
    • (1990) Mol Biol Evol , vol.7 , pp. 399-406
    • Landan, G.1    Cohen, G.2    Aharonowitz, Y.3    Shuali, Y.4    Graur, D.5    Shiffman, D.6
  • 2
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity
    • Fisher, J.F., Meroueh, S.O., Mobashery, S., Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity. Chem Rev 105 (2005), 395–424.
    • (2005) Chem Rev , vol.105 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 3
    • 84960157138 scopus 로고    scopus 로고
    • One ring to rule them all: current trends in combating bacterial resistance to the β-lactams
    • Excellent review of the molecular spectrum of β-lactam resistance.
    • King, D.T., Sobhanifar, S., Strynadka, N.C.J., One ring to rule them all: current trends in combating bacterial resistance to the β-lactams. Protein Sci 25 (2016), 787–803 Excellent review of the molecular spectrum of β-lactam resistance.
    • (2016) Protein Sci , vol.25 , pp. 787-803
    • King, D.T.1    Sobhanifar, S.2    Strynadka, N.C.J.3
  • 4
    • 84926035587 scopus 로고    scopus 로고
    • The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria
    • Li, X-Z., Plésiat, P., Nikaido, H., The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria. Clin Microbiol Rev 28 (2015), 337–418.
    • (2015) Clin Microbiol Rev , vol.28 , pp. 337-418
    • Li, X.-Z.1    Plésiat, P.2    Nikaido, H.3
  • 5
    • 84856729230 scopus 로고    scopus 로고
    • Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria
    • Nikaido, H., Pagès, J-M., Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria. FEMS Microbiol Rev 36 (2012), 340–363.
    • (2012) FEMS Microbiol Rev , vol.36 , pp. 340-363
    • Nikaido, H.1    Pagès, J.-M.2
  • 6
    • 84928320829 scopus 로고    scopus 로고
    • Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
    • Fishovitz, J., Hermoso, J.A., Chang, M., Mobashery, S., Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus. IUBMB Life 66 (2014), 572–577.
    • (2014) IUBMB Life , vol.66 , pp. 572-577
    • Fishovitz, J.1    Hermoso, J.A.2    Chang, M.3    Mobashery, S.4
  • 8
    • 84946567642 scopus 로고    scopus 로고
    • A resurgence of β-lactamase inhibitor combinations effective against multidrug-resistant Gram-negative pathogens
    • Bush, K., A resurgence of β-lactamase inhibitor combinations effective against multidrug-resistant Gram-negative pathogens. Int J Antimicrob Agents 46 (2015), 483–493.
    • (2015) Int J Antimicrob Agents , vol.46 , pp. 483-493
    • Bush, K.1
  • 9
    • 85018162548 scopus 로고    scopus 로고
    • Structure, genetics and worldwide spread of New Delhi Metallo-β-lactamase (NDM): a threat to public health
    • Khan, A.U., Maryam, L., Zarrilli, R., Structure, genetics and worldwide spread of New Delhi Metallo-β-lactamase (NDM): a threat to public health. BMC Microbiol, 17, 2017, 101.
    • (2017) BMC Microbiol , vol.17 , pp. 101
    • Khan, A.U.1    Maryam, L.2    Zarrilli, R.3
  • 10
    • 84899511797 scopus 로고    scopus 로고
    • Worldwide dissemination of the NDM-type carbapenemases in Gram-negative bacteria
    • Dortet, L., Poirel, L., Nordmann, P., Worldwide dissemination of the NDM-type carbapenemases in Gram-negative bacteria. Biomed Res Int, 2014, 2014, 249856.
    • (2014) Biomed Res Int , vol.2014 , pp. 249856
    • Dortet, L.1    Poirel, L.2    Nordmann, P.3
  • 11
    • 85010399975 scopus 로고    scopus 로고
    • Notes from the field: pan-resistant New Delhi Metallo-beta-lactamase-producing Klebsiella pneumoniae — Washoe County, Nevada, 2016
    • Chen, L., Todd, R., Kiehlbauch, J., Walters, M., Kallen, A., Notes from the field: pan-resistant New Delhi Metallo-beta-lactamase-producing Klebsiella pneumoniae — Washoe County, Nevada, 2016. MMWR Morb Mortal Wkly Rep, 66, 2017, 33.
    • (2017) MMWR Morb Mortal Wkly Rep , vol.66 , pp. 33
    • Chen, L.1    Todd, R.2    Kiehlbauch, J.3    Walters, M.4    Kallen, A.5
  • 12
    • 84959127341 scopus 로고    scopus 로고
    • Plasmid-mediated carbapenem and colistin resistance in a clinical isolate of Escherichia coli
    • Poirel, L., Kieffer, N., Liassine, N., Thanh, D., Plasmid-mediated carbapenem and colistin resistance in a clinical isolate of Escherichia coli. Lancet Infect Dis, 16, 2016, 281.
    • (2016) Lancet Infect Dis , vol.16 , pp. 281
    • Poirel, L.1    Kieffer, N.2    Liassine, N.3    Thanh, D.4
  • 13
    • 84872871981 scopus 로고    scopus 로고
    • Metallo-β-lactamase structure and function
    • Comprehensive overview of MLB structure and function.
    • Palzkill, T., Metallo-β-lactamase structure and function. Ann N Y Acad Sci 1277 (2013), 91–104 Comprehensive overview of MLB structure and function.
    • (2013) Ann N Y Acad Sci , vol.1277 , pp. 91-104
    • Palzkill, T.1
  • 14
    • 84937138142 scopus 로고    scopus 로고
    • Antibiotic resistance in the opportunistic pathogen Stenotrophomonas maltophilia
    • Sánchez, M.B., Antibiotic resistance in the opportunistic pathogen Stenotrophomonas maltophilia. Front Microbiol, 6, 2015, 658.
    • (2015) Front Microbiol , vol.6 , pp. 658
    • Sánchez, M.B.1
  • 15
    • 84858689683 scopus 로고    scopus 로고
    • Carbapenem resistance in Elizabethkingia meningoseptica is mediated by metallo-β-lactamase BlaB
    • González, L.J., Vila, A.J., Carbapenem resistance in Elizabethkingia meningoseptica is mediated by metallo-β-lactamase BlaB. Antimicrob Agents Chemother 56 (2012), 1686–1692.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 1686-1692
    • González, L.J.1    Vila, A.J.2
  • 16
    • 84973598896 scopus 로고    scopus 로고
    • B1-metallo-β-lactamases: where do we stand?
    • Insightful and comprehensive review on MBL structure, diversity and distribution.
    • Mojica, M.F., Bonomo, R.A., Fast, W., B1-metallo-β-lactamases: where do we stand?. Curr Drug Targets 17 (2016), 1029–1050 Insightful and comprehensive review on MBL structure, diversity and distribution.
    • (2016) Curr Drug Targets , vol.17 , pp. 1029-1050
    • Mojica, M.F.1    Bonomo, R.A.2    Fast, W.3
  • 19
    • 85019545774 scopus 로고    scopus 로고
    • Global Priority List of Antibiotic-Resistant Bacteria to Guide Research, Discovery, and Development of New Antibiotics
    • World Health Organization, Global Priority List of Antibiotic-Resistant Bacteria to Guide Research, Discovery, and Development of New Antibiotics. 2017.
    • (2017)
    • World Health Organization1
  • 21
    • 33750624074 scopus 로고    scopus 로고
    • Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria
    • Crowder, M.W., Spencer, J., Vila, A.J., Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria. Acc Chem Res 39 (2006), 721–728.
    • (2006) Acc Chem Res , vol.39 , pp. 721-728
    • Crowder, M.W.1    Spencer, J.2    Vila, A.J.3
  • 23
    • 85011000691 scopus 로고    scopus 로고
    • NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitors
    • First report of non-metal interacting MBL inhibitors.
    • Li, G-B., Abboud, M.I., Brem, J., Someya, H., Lohans, C.T., Yang, S-Y., Spencer, J., Wareham, D.W., McDonough, M.A., Schofield, C.J., NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitors. Chem Sci 8 (2017), 928–937 First report of non-metal interacting MBL inhibitors.
    • (2017) Chem Sci , vol.8 , pp. 928-937
    • Li, G.-B.1    Abboud, M.I.2    Brem, J.3    Someya, H.4    Lohans, C.T.5    Yang, S.-Y.6    Spencer, J.7    Wareham, D.W.8    McDonough, M.A.9    Schofield, C.J.10
  • 24
    • 84881291707 scopus 로고    scopus 로고
    • Antibiotic resistance in Zn(II)-deficient environments: metallo-β-lactamase activation in the periplasm
    • Meini, M-R., González, L.J., Vila, A.J., Antibiotic resistance in Zn(II)-deficient environments: metallo-β-lactamase activation in the periplasm. Future Microbiol 8 (2013), 947–979.
    • (2013) Future Microbiol , vol.8 , pp. 947-979
    • Meini, M.-R.1    González, L.J.2    Vila, A.J.3
  • 25
    • 84897918689 scopus 로고    scopus 로고
    • Competition for zinc binding in the host-pathogen interaction
    • Cerasi, M., Ammendola, S., Battistoni, A., Competition for zinc binding in the host-pathogen interaction. Front Cell Infect Microbiol, 3, 2013, 10.3389/fcimb.2013.00108/abstract.
    • (2013) Front Cell Infect Microbiol , vol.3
    • Cerasi, M.1    Ammendola, S.2    Battistoni, A.3
  • 26
    • 84879302319 scopus 로고    scopus 로고
    • An update on the status of potent inhibitors of metallo-β-lactamases
    • Faridoon, Ul Islam, N., An update on the status of potent inhibitors of metallo-β-lactamases. Sci Pharm 81 (2013), 309–327.
    • (2013) Sci Pharm , vol.81 , pp. 309-327
    • Faridoon1    Ul Islam, N.2
  • 28
    • 84957867042 scopus 로고    scopus 로고
    • Structural basis of metallo-β-lactamase inhibition by captopril stereoisomers
    • Comprehensive chemical synthesis, enzymatic analysis, structural validation and microbiological study of MBL inhibition by captopril diastereomers.
    • Brem, J., van Berkel, S.S., Zollman, D., Lee, S.Y., Gileadi, O., McHugh, P.J., Walsh, T.R., McDonough, M.A., Schofield, C.J., Structural basis of metallo-β-lactamase inhibition by captopril stereoisomers. Antimicrob Agents Chemother 60 (2015), 142–150 Comprehensive chemical synthesis, enzymatic analysis, structural validation and microbiological study of MBL inhibition by captopril diastereomers.
    • (2015) Antimicrob Agents Chemother , vol.60 , pp. 142-150
    • Brem, J.1    van Berkel, S.S.2    Zollman, D.3    Lee, S.Y.4    Gileadi, O.5    McHugh, P.J.6    Walsh, T.R.7    McDonough, M.A.8    Schofield, C.J.9
  • 33
    • 84965002978 scopus 로고    scopus 로고
    • Triazolylthioacetamide: a valid scaffold for the development of New Delhi Metallo-β-lactmase-1 (NDM-1) Inhibitors
    • Zhai, L., Zhang, Y-L., Kang, J.S., Oelschlaeger, P., Xiao, L., Nie, S-S., Yang, K-W., Triazolylthioacetamide: a valid scaffold for the development of New Delhi Metallo-β-lactmase-1 (NDM-1) Inhibitors. ACS Med Chem Lett 7 (2016), 413–417.
    • (2016) ACS Med Chem Lett , vol.7 , pp. 413-417
    • Zhai, L.1    Zhang, Y.-L.2    Kang, J.S.3    Oelschlaeger, P.4    Xiao, L.5    Nie, S.-S.6    Yang, K.-W.7
  • 34
    • 84927600380 scopus 로고    scopus 로고
    • Azolylthioacetamide: a highly promising scaffold for the development of metallo-β-lactamase inhibitors
    • Yang, S-K., Kang, J.S., Oelschlaeger, P., Yang, K-W., Azolylthioacetamide: a highly promising scaffold for the development of metallo-β-lactamase inhibitors. ACS Med Chem Lett 6 (2015), 455–460.
    • (2015) ACS Med Chem Lett , vol.6 , pp. 455-460
    • Yang, S.-K.1    Kang, J.S.2    Oelschlaeger, P.3    Yang, K.-W.4
  • 35
    • 84994791387 scopus 로고    scopus 로고
    • The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor
    • Christopeit, T., Yang, K.W., Yang, S.K., Leiros, H.K.S., The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor. Acta Cryst 72 (2016), 1–7.
    • (2016) Acta Cryst , vol.72 , pp. 1-7
    • Christopeit, T.1    Yang, K.W.2    Yang, S.K.3    Leiros, H.K.S.4
  • 36
    • 84960192048 scopus 로고    scopus 로고
    • Fragment-based discovery of inhibitor scaffolds targeting the metallo-β-lactamases NDM-1 and VIM-2
    • Christopeit, T., Leiros, H-K.S., Fragment-based discovery of inhibitor scaffolds targeting the metallo-β-lactamases NDM-1 and VIM-2. Bioorg Med Chem Lett 26 (2016), 1973–1977.
    • (2016) Bioorg Med Chem Lett , vol.26 , pp. 1973-1977
    • Christopeit, T.1    Leiros, H.-K.S.2
  • 37
    • 84947213893 scopus 로고    scopus 로고
    • Discovery of novel inhibitor scaffolds against the metallo-β-lactamase VIM-2 by surface plasmon resonance (SPR) based fragment screening
    • Christopeit, T., Carlsen, T.J.O., Helland, R., Leiros, H-K.S., Discovery of novel inhibitor scaffolds against the metallo-β-lactamase VIM-2 by surface plasmon resonance (SPR) based fragment screening. J Med Chem 58 (2015), 8671–8682.
    • (2015) J Med Chem , vol.58 , pp. 8671-8682
    • Christopeit, T.1    Carlsen, T.J.O.2    Helland, R.3    Leiros, H.-K.S.4
  • 38
    • 84966508471 scopus 로고    scopus 로고
    • Discovery of a novel covalent non-β-lactam inhibitor of the metallo-β-lactamase NDM-1
    • Christopeit, T., Albert, A., Leiros, H-K.S., Discovery of a novel covalent non-β-lactam inhibitor of the metallo-β-lactamase NDM-1. Bioorg Med Chem 24 (2016), 2947–2953.
    • (2016) Bioorg Med Chem , vol.24 , pp. 2947-2953
    • Christopeit, T.1    Albert, A.2    Leiros, H.-K.S.3
  • 41
    • 84981356473 scopus 로고    scopus 로고
    • Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
    • Demonstration of efficacy and molecular analysis of cyclic-boronate inhibitors of MBLs.
    • Brem, J., Cain, R., Cahill, S., McDonough, M.A., Clifton, I.J., Jiménez-Castellanos, J-C., Avison, M.B., Spencer, J., Fishwick, C.W.G., Schofield, C.J., Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates. Nat Commun, 7, 2016, 12406 Demonstration of efficacy and molecular analysis of cyclic-boronate inhibitors of MBLs.
    • (2016) Nat Commun , vol.7 , pp. 12406
    • Brem, J.1    Cain, R.2    Cahill, S.3    McDonough, M.A.4    Clifton, I.J.5    Jiménez-Castellanos, J.-C.6    Avison, M.B.7    Spencer, J.8    Fishwick, C.W.G.9    Schofield, C.J.10
  • 44
    • 84903457328 scopus 로고    scopus 로고
    • Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance
    • First report of a natural product MBL inactivator demonstrating efficacy in vitro and in vivo.
    • King, A.M., Reid-Yu, S.A., Wang, W., King, D.T., De Pascale, G., Strynadka, N.C., Walsh, T.R., Coombes, B.K., Wright, G.D., Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance. Nature 510 (2014), 503–506 First report of a natural product MBL inactivator demonstrating efficacy in vitro and in vivo.
    • (2014) Nature , vol.510 , pp. 503-506
    • King, A.M.1    Reid-Yu, S.A.2    Wang, W.3    King, D.T.4    De Pascale, G.5    Strynadka, N.C.6    Walsh, T.R.7    Coombes, B.K.8    Wright, G.D.9
  • 46
    • 0021049908 scopus 로고
    • Novel microbial inhibitors of angiotensin-converting enzyme, aspergillomarasmines A and B
    • Mikami, Y., Suzuki, T., Novel microbial inhibitors of angiotensin-converting enzyme, aspergillomarasmines A and B. Agric Biol Chem 47 (1983), 2693–2695.
    • (1983) Agric Biol Chem , vol.47 , pp. 2693-2695
    • Mikami, Y.1    Suzuki, T.2
  • 47
    • 85007825474 scopus 로고
    • Aspergillomarasmine A and B, potent microbial inhibitors of endothelin-converting enzyme
    • Arai, K., Ashikawa, N., Nakakita, Y., Aspergillomarasmine A and B, potent microbial inhibitors of endothelin-converting enzyme. Bioscience 57 (1993), 1944–1945.
    • (1993) Bioscience , vol.57 , pp. 1944-1945
    • Arai, K.1    Ashikawa, N.2    Nakakita, Y.3
  • 48
    • 84947976362 scopus 로고    scopus 로고
    • Total synthesis and structural reassignment of aspergillomarasmine A
    • Liao, D., Yang, S., Wang, J., Zhang, J., Hong, B., Wu, F., Lei, X., Total synthesis and structural reassignment of aspergillomarasmine A. Angew Chem Int Ed Engl 55 (2016), 4291–4295.
    • (2016) Angew Chem Int Ed Engl , vol.55 , pp. 4291-4295
    • Liao, D.1    Yang, S.2    Wang, J.3    Zhang, J.4    Hong, B.5    Wu, F.6    Lei, X.7
  • 49
    • 84992093037 scopus 로고    scopus 로고
    • Total synthesis of aspergillomarasmine A and related compounds: a sulfamidate approach enables exploration of structure–activity relationships
    • Albu, S.A., Koteva, K., King, A.M., Al-Karmi, S., Wright, G.D., Capretta, A., Total synthesis of aspergillomarasmine A and related compounds: a sulfamidate approach enables exploration of structure–activity relationships. Angew Chem 55 (2016), 13259–13262.
    • (2016) Angew Chem , vol.55 , pp. 13259-13262
    • Albu, S.A.1    Koteva, K.2    King, A.M.3    Al-Karmi, S.4    Wright, G.D.5    Capretta, A.6
  • 50
    • 84957845289 scopus 로고    scopus 로고
    • Total synthesis and activity of the metallo-β-lactamase inhibitor aspergillomarasmine A
    • Koteva, K., King, A.M., Capretta, A., Total synthesis and activity of the metallo-β-lactamase inhibitor aspergillomarasmine A. Angew Chem 55 (2016), 2210–2212.
    • (2016) Angew Chem , vol.55 , pp. 2210-2212
    • Koteva, K.1    King, A.M.2    Capretta, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.