메뉴 건너뛰기




Volumn 60, Issue 3, 2016, Pages 1377-1384

Comparison of verona integron-borne metallo-β-lactamase (VIM) variants reveals differences in stability and inhibition profiles

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; BETA LACTAM; BETA LACTAMASE; CEFALOTIN; CEFOXITIN; CEFTAZIDIME; IMIPENEM; METALLO BETA LACTAMASE; PENICILLIN DERIVATIVE; BACTERIAL PROTEIN; BETA LACTAMASE INHIBITOR; BETA-LACTAMASE BLA(VIM-4), PSEUDOMONAS AERUGINOSA; BETA-LACTAMASE VIM-5, PSEUDOMONAS AERUGINOSA; RECOMBINANT PROTEIN; VIM-1 METALLO-BETA-LACTAMASE; VIM-2 BETA-LACTAMASE;

EID: 84960155881     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01768-15     Document Type: Article
Times cited : (35)

References (54)
  • 2
    • 0019326853 scopus 로고
    • The structure of β-lactamases
    • Ambler RP. 1980. The structure of β-lactamases. Philos Trans R Soc Lond B 289:321-331. http://dx.doi.org/10.1098/rstb.1980.0049.
    • (1980) Philos Trans R Soc Lond B , vol.289 , pp. 321-331
    • Ambler, R.P.1
  • 3
    • 45349100770 scopus 로고    scopus 로고
    • The mechanisms of catalysis by metallo-β-lactamases
    • Page MI, Badarau A. 2008. The mechanisms of catalysis by metallo-β-lactamases. Bioinorg Chem Appl 2008:576297. http://dx.doi.org/10.1155/2008/576297.
    • (2008) Bioinorg Chem Appl , vol.2008 , pp. 576297
    • Page, M.I.1    Badarau, A.2
  • 4
    • 84872871981 scopus 로고    scopus 로고
    • Metallo-β-lactamase structure and function
    • Palzkill T. 2013. Metallo-β-lactamase structure and function. Ann N Y Acad Sci 1277:91-104. http://dx.doi.org/10.1111/j.1749-6632.2012.06796.x.
    • (2013) Ann N Y Acad Sci , vol.1277 , pp. 91-104
    • Palzkill, T.1
  • 5
    • 84908025454 scopus 로고    scopus 로고
    • Carbapenemase genes and genetic platforms in Gram-negative bacilli: Enterobacteriaceae, Pseudomonas and Acinetobacter species
    • Diene SM, Rolain JM. 2014. Carbapenemase genes and genetic platforms in Gram-negative bacilli: Enterobacteriaceae, Pseudomonas and Acinetobacter species. Clin Microbiol Infect 20:831-838. http://dx.doi.org/10.1111/1469-0691.12655.
    • (2014) Clin Microbiol Infect , vol.20 , pp. 831-838
    • Diene, S.M.1    Rolain, J.M.2
  • 7
    • 0036592476 scopus 로고    scopus 로고
    • Emerging carbapenemases in Gramnegative aerobes
    • Nordmann P, Poirel L. 2002. Emerging carbapenemases in Gramnegative aerobes. Clin Microbiol Infect 8:321-331. http://dx.doi.org/10.1046/j.1469-0691.2002.00401.x.
    • (2002) Clin Microbiol Infect , vol.8 , pp. 321-331
    • Nordmann, P.1    Poirel, L.2
  • 8
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone C. 2007. Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem Pharmacol 74:1686-1701. http://dx.doi.org/10.1016/j.bcp. 2007.05.021.
    • (2007) Biochem Pharmacol , vol.74 , pp. 1686-1701
    • Bebrone, C.1
  • 9
    • 0035839131 scopus 로고    scopus 로고
    • Expansion of the zinc metallo-hydrolase family of the β-lactamase fold
    • Daiyasu H, Osaka K, Ishino Y, Toh H. 2001. Expansion of the zinc metallo-hydrolase family of the β-lactamase fold. FEBS Lett 503:1-6. http://dx.doi.org/10.1016/S0014-5793 (01) 02686-2.
    • (2001) FEBS Lett , vol.503 , pp. 1-6
    • Daiyasu, H.1    Osaka, K.2    Ishino, Y.3    Toh, H.4
  • 11
    • 79957618735 scopus 로고    scopus 로고
    • Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
    • Zhang H, Hao Q. 2011. Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism. FASEB J 25:2574-2582. http://dx.doi.org/10.1096/fj.11-184036.
    • (2011) FASEB J , vol.25 , pp. 2574-2582
    • Zhang, H.1    Hao, Q.2
  • 12
    • 84863976350 scopus 로고    scopus 로고
    • New Delhi metallo-β-lactamase: Structural insights into β-lactam recognition and inhibition
    • King DT, Worrall LJ, Gruninger R, Strynadka NC. 2012. New Delhi metallo-β-lactamase: structural insights into β-lactam recognition and inhibition. J Am Chem Soc 134:11362-11365. http://dx.doi.org/10.1021/ja303579d.
    • (2012) J Am Chem Soc , vol.134 , pp. 11362-11365
    • King, D.T.1    Worrall, L.J.2    Gruninger, R.3    Strynadka, N.C.4
  • 15
    • 37349007671 scopus 로고    scopus 로고
    • The three-dimensional structure of VIM-2, a Zn-β-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form
    • Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O. 2008. The three-dimensional structure of VIM-2, a Zn-β-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form. J Mol Biol 375:604-611. http://dx.doi.org/10.1016/j.jmb.2007.11.012.
    • (2008) J Mol Biol , vol.375 , pp. 604-611
    • Garcia-Saez, I.1    Docquier, J.D.2    Rossolini, G.M.3    Dideberg, O.4
  • 16
    • 0347992025 scopus 로고    scopus 로고
    • aVIM-7, an evolutionarily distinct metallo-β-lactamase gene in a Pseudomonas aeruginosa isolate from the United States
    • aVIM-7, an evolutionarily distinct metallo-β-lactamase gene in a Pseudomonas aeruginosa isolate from the United States. Antimicrob Agents Chemother 48:329-332. http://dx.doi.org/10.1128/AAC.48.1.329-332.2004.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 329-332
    • Toleman, M.A.1    Rolston, K.2    Jones, R.N.3    Walsh, T.R.4
  • 17
    • 36048929194 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of VIM-12, a novel hybrid VIM-1/VIM-2 metallo-β-lactamase from a Klebsiella pneumoniae clinical isolate, reveal atypical substrate specificity
    • Kontou M, Pournaras S, Kristo I, Ikonomidis A, Maniatis AN, Stathopoulos C. 2007. Molecular cloning and biochemical characterization of VIM-12, a novel hybrid VIM-1/VIM-2 metallo-β-lactamase from a Klebsiella pneumoniae clinical isolate, reveal atypical substrate specificity. Biochemistry 46:13170-13178. http://dx.doi.org/10.1021/bi701258w.
    • (2007) Biochemistry , vol.46 , pp. 13170-13178
    • Kontou, M.1    Pournaras, S.2    Kristo, I.3    Ikonomidis, A.4    Maniatis, A.N.5    Stathopoulos, C.6
  • 18
    • 54049088985 scopus 로고    scopus 로고
    • Characterization of the new metallo-β-lactamase VIM-13 and its integron-borne gene from a Pseudomonas aeruginosa clinical isolate in Spain
    • Juan C, Beceiro A, Gutierrez O, Alberti S, Garau M, Perez JL, Bou G, Oliver A. 2008. Characterization of the new metallo-β-lactamase VIM-13 and its integron-borne gene from a Pseudomonas aeruginosa clinical isolate in Spain. Antimicrob Agents Chemother 52:3589-3596. http://dx.doi.org/10.1128/AAC.00465-08.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 3589-3596
    • Juan, C.1    Beceiro, A.2    Gutierrez, O.3    Alberti, S.4    Garau, M.5    Perez, J.L.6    Bou, G.7    Oliver, A.8
  • 21
    • 0034023159 scopus 로고    scopus 로고
    • Characterization of VIM-2, a carbapenem-hydrolyzing metallo-β-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France
    • Poirel L, Naas T, Nicolas D, Collet L, Bellais S, Cavallo JD, Nordmann P. 2000. Characterization of VIM-2, a carbapenem-hydrolyzing metallo-β-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France. Antimicrob Agents Chemother 44:891-897. http://dx.doi.org/10.1128/AAC.44.4.891-897.2000.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 891-897
    • Poirel, L.1    Naas, T.2    Nicolas, D.3    Collet, L.4    Bellais, S.5    Cavallo, J.D.6    Nordmann, P.7
  • 22
    • 0035916418 scopus 로고    scopus 로고
    • VIM-2-containing integrons from Pseudomonas aeruginosa plasmids encoding the VIM-2 metallo-β-lactamase
    • VIM-2-containing integrons from Pseudomonas aeruginosa plasmids encoding the VIM-2 metallo-β-lactamase. FEMS Microbiol Lett 195:145-150. http://dx.doi.org/10.1111/j.1574-6968.2001.tb10512.x.
    • (2001) FEMS Microbiol Lett , vol.195 , pp. 145-150
    • Pallecchi, L.1    Riccio, M.L.2    Docquier, J.D.3    Fontana, R.4    Rossolini, G.M.5
  • 24
    • 3543070187 scopus 로고    scopus 로고
    • A new variant of metallo-β-lactamase detected in a Klebsiella pneumoniae strain: VIM-5, abstr S-21
    • Istanbul, Turkey
    • Midilli K, Aygün G, Kuskucu M. 2003. A new variant of metallo-β-lactamase detected in a Klebsiella pneumoniae strain: VIM-5, abstr S-21, p 275. Abstr KLIMIK Congr, Istanbul, Turkey.
    • (2003) Abstr KLIMIK Congr , pp. 275
    • Midilli, K.1    Aygün, G.2    Kuskucu, M.3
  • 27
    • 84893745009 scopus 로고    scopus 로고
    • Characterization of novel VIM carbapenemase, VIM-38, and first detection of GES-5 carbapenem-hydrolyzing β-lactamases in Pseudomonas aeruginosa in Turkey
    • Iraz M, Duzgun AO, Cicek AC, Bonnin RA, Ceylan A, Saral A, Nordmann P, Sandalli C. 2014. Characterization of novel VIM carbapenemase, VIM-38, and first detection of GES-5 carbapenem-hydrolyzing β-lactamases in Pseudomonas aeruginosa in Turkey. Diagn Microbiol Infect Dis 78:292-294. http://dx.doi.org/10.1016/j.diagmicrobio.2013.12.003.
    • (2014) Diagn Microbiol Infect Dis , vol.78 , pp. 292-294
    • Iraz, M.1    Duzgun, A.O.2    Cicek, A.C.3    Bonnin, R.A.4    Ceylan, A.5    Saral, A.6    Nordmann, P.7    Sandalli, C.8
  • 30
    • 84925615027 scopus 로고    scopus 로고
    • Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamases
    • Leiros HK, Edvardsen KS, Bjerga GE, Samuelsen O. 2015. Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamases. FEBS J 282:1031-1042. http://dx.doi.org/10.1111/febs.13200.
    • (2015) FEBS J , vol.282 , pp. 1031-1042
    • Leiros, H.K.1    Edvardsen, K.S.2    Bjerga, G.E.3    Samuelsen, O.4
  • 32
    • 84935882101 scopus 로고    scopus 로고
    • The three-dimensional structure of VIM-31, a metallo-β-lactamase from Enterobacter cloacae in its native and oxidized form
    • Kupper MB, Herzog K, Bennink S, Schlomer P, Bogaerts P, Glupczynski Y, Fischer R, Bebrone C, Hoffmann KM. 2015. The three-dimensional structure of VIM-31, a metallo-β-lactamase from Enterobacter cloacae in its native and oxidized form. FEBS J 282:2352-2360. http://dx.doi.org/10.1111/febs.13283.
    • (2015) FEBS J , vol.282 , pp. 2352-2360
    • Kupper, M.B.1    Herzog, K.2    Bennink, S.3    Schlomer, P.4    Bogaerts, P.5    Glupczynski, Y.6    Fischer, R.7    Bebrone, C.8    Hoffmann, K.M.9
  • 33
    • 84905379594 scopus 로고    scopus 로고
    • His224 alters the R2 drug binding site and Phe218 influences the catalytic efficiency of the metallo-β-lactamase VIM-7
    • Leiros HK, Skagseth S, Edvardsen KS, Lorentzen MS, Bjerga GE, Leiros I, Samuelsen O. 2014. His224 alters the R2 drug binding site and Phe218 influences the catalytic efficiency of the metallo-β-lactamase VIM-7. Antimicrob Agents Chemother 58:4826-4836. http://dx.doi.org/10.1128/AAC.02735-13.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 4826-4836
    • Leiros, H.K.1    Skagseth, S.2    Edvardsen, K.S.3    Lorentzen, M.S.4    Bjerga, G.E.5    Leiros, I.6    Samuelsen, O.7
  • 38
    • 0037677275 scopus 로고    scopus 로고
    • Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method
    • Raussens V, Ruysschaert JM, Goormaghtigh E. 2003. Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method. Anal Biochem 319:114-121. http://dx.doi.org/10.1016/S0003-2697 (03) 00285-9.
    • (2003) Anal Biochem , vol.319 , pp. 114-121
    • Raussens, V.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 39
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore L, Wallace BA. 2008. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89:392-400. http://dx.doi.org/10.1002/bip. 20853.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 40
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, Woody RW. 2000. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287:252-260. http://dx.doi.org/10.1006/abio.2000.4880.
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 41
    • 84898079809 scopus 로고    scopus 로고
    • Modulating carnitine levels by targeting its biosynthesis-selective inhibition of γ-butyrobetaine hydroxylase
    • Rydzik AM, Chowdhury R, Kochan GT, Williams ST, McDonough MA, Kawamura K, Schofield CJ. 2014. Modulating carnitine levels by targeting its biosynthesis-selective inhibition of γ-butyrobetaine hydroxylase. Chem Sci 5:1765-1771. http://dx.doi.org/10.1039/c4sc00020j.
    • (2014) Chem Sci , vol.5 , pp. 1765-1771
    • Rydzik, A.M.1    Chowdhury, R.2    Kochan, G.T.3    Williams, S.T.4    McDonough, M.A.5    Kawamura, K.6    Schofield, C.J.7
  • 42
  • 45
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P. 2006. Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62:72-82. http://dx.doi.org/10.1107/S0907444 905036693.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 47
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossmann MG, Blow DM. 1962. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallogr 15:24-31. http://dx.doi.org/10.1107/S0365110X62000067.
    • (1962) Acta Crystallogr , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 48
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read RJ. 2001. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr D Biol Crystallogr 57:1373-1382. http://dx.doi.org/10.1107/S0907444901012471.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1373-1382
    • Read, R.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.