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Volumn 60, Issue 3, 2016, Pages 1509-1514

Membrane-bound PenA β-lactamase of Burkholderia pseudomallei

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMPICILLIN; BETA LACTAMASE; CARBENICILLIN; CEFTAZIDIME; CYSTEINE; GLOBOMYCIN; IMIPENEM; ISOLEUCINE; LIPOPROTEIN; MEMBRANE BOUND PENA BETA LACTAMASE; SERINE; SIGNAL PEPTIDASE I; SIGNAL PEPTIDE; TRITON X 114; UNCLASSIFIED DRUG; MACROGOL DERIVATIVE; NONIDET P-40; PEPTIDE;

EID: 84960157192     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02444-15     Document Type: Article
Times cited : (22)

References (39)
  • 3
    • 84871009951 scopus 로고    scopus 로고
    • Mechanisms of antibiotic resistance in Burkholderia pseudomallei: Implications for treatment of melioidosis
    • Schweizer HP. 2012. Mechanisms of antibiotic resistance in Burkholderia pseudomallei: implications for treatment of melioidosis. Future Microbiol 7:1389-1399. http://dx.doi.org/10.2217/fmb.12.116.
    • (2012) Future Microbiol , vol.7 , pp. 1389-1399
    • Schweizer, H.P.1
  • 4
    • 84897998841 scopus 로고    scopus 로고
    • Treatment and prophylaxis of melioidosis
    • Dance D. 2014. Treatment and prophylaxis of melioidosis. Int J Antimicrob Agents 43:310-318. http://dx.doi.org/10.1016/j.ijantimicag.2014.01.005.
    • (2014) Int J Antimicrob Agents , vol.43 , pp. 310-318
    • Dance, D.1
  • 8
    • 0038338497 scopus 로고    scopus 로고
    • Burkholderia pseudomallei class A beta-lactamase mutations that confer selective resistance against ceftazidime or clavulanic acid inhibition
    • Tribuddharat C, Moore RA, Baker P, Woods DE. 2003. Burkholderia pseudomallei class A beta-lactamase mutations that confer selective resistance against ceftazidime or clavulanic acid inhibition. Antimicrob Agents Chemother 47:2082-2087. http://dx.doi.org/10.1128/AAC.47.7.2082-2087.2003.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2082-2087
    • Tribuddharat, C.1    Moore, R.A.2    Baker, P.3    Woods, D.E.4
  • 9
    • 66149139711 scopus 로고    scopus 로고
    • Variations in ceftazidime and amoxicillin-clavulanate susceptibilities within a clonal infection of Burkholderia pseudomallei
    • Sam IC, See KH, Puthucheary SD. 2009. Variations in ceftazidime and amoxicillin-clavulanate susceptibilities within a clonal infection of Burkholderia pseudomallei. J Clin Microbiol 47:1556-1558. http://dx.doi.org/10.1128/JCM.01657-08.
    • (2009) J Clin Microbiol , vol.47 , pp. 1556-1558
    • Sam, I.C.1    See, K.H.2    Puthucheary, S.D.3
  • 14
    • 84879594832 scopus 로고    scopus 로고
    • Insights into beta-lactamases from Burkholderia species, two phylogenetically related yet distinct resistance determinants
    • Papp-Wallace KM, Taracila MA, Gatta JA, Ohuchi N, Bonomo RA, Nukaga M. 2013. Insights into beta-lactamases from Burkholderia species, two phylogenetically related yet distinct resistance determinants. J Biol Chem 288:19090-19102. http://dx.doi.org/10.1074/jbc. M113.458315.
    • (2013) J Biol Chem , vol.288 , pp. 19090-19102
    • Papp-Wallace, K.M.1    Taracila, M.A.2    Gatta, J.A.3    Ohuchi, N.4    Bonomo, R.A.5    Nukaga, M.6
  • 15
    • 0023182272 scopus 로고
    • Beta-lactamase of Pseudomonas pseudomallei and its contribution to antibiotic resistance
    • Livermore DM, Chau PY, Wong AI, Leung YK. 1987. Beta-lactamase of Pseudomonas pseudomallei and its contribution to antibiotic resistance. J Antimicrob Chemother 20:313-321. http://dx.doi.org/10.1093/jac/20.3.313.
    • (1987) J Antimicrob Chemother , vol.20 , pp. 313-321
    • Livermore, D.M.1    Chau, P.Y.2    Wong, A.I.3    Leung, Y.K.4
  • 16
    • 77953939501 scopus 로고    scopus 로고
    • A Burkholderia pseudomallei ΔpurM mutant is avirulent in immunocompetent and immunodeficient animals: Candidate strain for exclusion from select-agent lists
    • Propst KL, Mima T, Choi KH, Dow SW, Schweizer HP. 2010. A Burkholderia pseudomallei ΔpurM mutant is avirulent in immunocompetent and immunodeficient animals: candidate strain for exclusion from select-agent lists. Infect Immun 78:3136-3143. http://dx.doi.org/10.1128/IAI.01313-09.
    • (2010) Infect Immun , vol.78 , pp. 3136-3143
    • Propst, K.L.1    Mima, T.2    Choi, K.H.3    Dow, S.W.4    Schweizer, H.P.5
  • 17
    • 70349907083 scopus 로고    scopus 로고
    • Versatile dualtechnology system for markerless allele replacement in Burkholderia pseudomallei
    • Lopez CM, Rholl DA, Trunck LA, Schweizer HP. 2009. Versatile dualtechnology system for markerless allele replacement in Burkholderia pseudomallei. Appl Environ Microbiol 75:6496-6503. http://dx.doi.org/10.1128/AEM.01669-09.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 6496-6503
    • Lopez, C.M.1    Rholl, D.A.2    Trunck, L.A.3    Schweizer, H.P.4
  • 20
    • 79251472718 scopus 로고    scopus 로고
    • Lipoproteins of bacterial pathogens
    • Kovacs-Simon A, Titball RW, Michell SL. 2011. Lipoproteins of bacterial pathogens. Infect Immun 79:548-561. http://dx.doi.org/10.1128/IAI.00682-10.
    • (2011) Infect Immun , vol.79 , pp. 548-561
    • Kovacs-Simon, A.1    Titball, R.W.2    Michell, S.L.3
  • 21
    • 0021800753 scopus 로고
    • Inhibition of prolipoprotein signal peptidase by globomycin
    • Dev IK, Harvey RJ, Ray PH. 1985. Inhibition of prolipoprotein signal peptidase by globomycin. J Biol Chem 260:5891-5894.
    • (1985) J Biol Chem , vol.260 , pp. 5891-5894
    • Dev, I.K.1    Harvey, R.J.2    Ray, P.H.3
  • 22
    • 0019309069 scopus 로고
    • Accumulation of glyceridecontaining precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin
    • Hussain M, Ichihara S, Mizushima S. 1980. Accumulation of glyceridecontaining precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin. J Biol Chem 255:3707-3712.
    • (1980) J Biol Chem , vol.255 , pp. 3707-3712
    • Hussain, M.1    Ichihara, S.2    Mizushima, S.3
  • 23
    • 0021711731 scopus 로고
    • Simple, rapid, and quantitative release of periplasmic proteins by chloroform
    • Ames GF-L, Prody C, Kustu S. 1984. Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J Bacteriol 160:1181-1183.
    • (1984) J Bacteriol , vol.160 , pp. 1181-1183
    • Ames, G.F.-L.1    Prody, C.2    Kustu, S.3
  • 24
    • 0023840684 scopus 로고
    • Identification and localization of integral membrane proteins of virulent Treponema pallidum subsp. Pallidum by phase partitioning with the nonionic detergent Triton X-114
    • Radolf JD, Chamberlain NR, Clausell A, Norgard MV. 1988. Identification and localization of integral membrane proteins of virulent Treponema pallidum subsp. pallidum by phase partitioning with the nonionic detergent Triton X-114. Infect Immun 56:490-498.
    • (1988) Infect Immun , vol.56 , pp. 490-498
    • Radolf, J.D.1    Chamberlain, N.R.2    Clausell, A.3    Norgard, M.V.4
  • 25
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem 256:1604-1607.
    • (1981) J Biol Chem , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 26
    • 0025784566 scopus 로고
    • The T-cell-stimulating 17-kilodalton protein of Francisella tularensis LVS is a lipoprotein
    • Sjostedt A, Tarnvik A, Sandstrom G. 1991. The T-cell-stimulating 17-kilodalton protein of Francisella tularensis LVS is a lipoprotein. Infect Immun 59:3163-3168.
    • (1991) Infect Immun , vol.59 , pp. 3163-3168
    • Sjostedt, A.1    Tarnvik, A.2    Sandstrom, G.3
  • 27
    • 0026575959 scopus 로고
    • Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein
    • Janson H, Heden LO, Forsgren A. 1992. Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein. Infect Immun 60:1336-1342.
    • (1992) Infect Immun , vol.60 , pp. 1336-1342
    • Janson, H.1    Heden, L.O.2    Forsgren, A.3
  • 28
    • 0032773958 scopus 로고    scopus 로고
    • Outer membrane proteins Omp10, Omp16, and Omp19 of Brucella spp. Are lipoproteins
    • Tibor A, Decelle B, Letesson JJ. 1999. Outer membrane proteins Omp10, Omp16, and Omp19 of Brucella spp. are lipoproteins. Infect Immun 67:4960-4962.
    • (1999) Infect Immun , vol.67 , pp. 4960-4962
    • Tibor, A.1    Decelle, B.2    Letesson, J.J.3
  • 31
    • 34447267263 scopus 로고    scopus 로고
    • The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide
    • Valente FM, Pereira PM, Venceslau SS, Regalla M, Coelho AV, Pereira IA. 2007. The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide. FEBS Lett 581:3341-3344. http://dx.doi.org/10.1016/j.febslet.2007.06.020.
    • (2007) FEBS Lett , vol.581 , pp. 3341-3344
    • Valente, F.M.1    Pereira, P.M.2    Venceslau, S.S.3    Regalla, M.4    Coelho, A.V.5    Pereira, I.A.6
  • 33
    • 84860389616 scopus 로고    scopus 로고
    • Crystal structure of New Delhi metallo-betalactamase reveals molecular basis for antibiotic resistance
    • King D, Strynadka N. 2011. Crystal structure of New Delhi metallo-betalactamase reveals molecular basis for antibiotic resistance. Protein Sci 20:1484-1491. http://dx.doi.org/10.1002/pro.697.
    • (2011) Protein Sci , vol.20 , pp. 1484-1491
    • King, D.1    Strynadka, N.2
  • 34
    • 84959511443 scopus 로고    scopus 로고
    • Membrane anchoring of carbapenemase Ndm-1 favors protein stability and resistance transfer, abstr C162c
    • American Society for Microbiology, Washington, DC
    • Gonzalez L, Bahr G, Bonomo RA, Vila A. 2014. Membrane anchoring of carbapenemase Ndm-1 favors protein stability and resistance transfer, abstr C162c. Abstr 54th Intersci Conf Antimicrob Agents Chemother. American Society for Microbiology, Washington, DC.
    • (2014) Abstr 54th Intersci Conf Antimicrob Agents Chemother
    • Gonzalez, L.1    Bahr, G.2    Bonomo, R.A.3    Vila, A.4
  • 36
    • 27244446613 scopus 로고    scopus 로고
    • Type I signal peptidase: An overview
    • Tuteja R. 2005. Type I signal peptidase: an overview. Arch Biochem Biophys 441:107-111. http://dx.doi.org/10.1016/j.abb.2005.07.013.
    • (2005) Arch Biochem Biophys , vol.441 , pp. 107-111
    • Tuteja, R.1
  • 37
    • 50049089468 scopus 로고    scopus 로고
    • Novel mechanism of outer membrane targeting of proteins in Gram-negative bacteria
    • Ferrandez Y, Condemine G. 2008. Novel mechanism of outer membrane targeting of proteins in Gram-negative bacteria. Mol Microbiol 69:1349-1357. http://dx.doi.org/10.1111/j.1365-2958.2008.06366.x.
    • (2008) Mol Microbiol , vol.69 , pp. 1349-1357
    • Ferrandez, Y.1    Condemine, G.2
  • 38
    • 71749120639 scopus 로고    scopus 로고
    • HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor
    • Viarre V, Cascales E, Ball G, Michel GP, Filloux A, Voulhoux R. 2009. HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor. J Biol Chem 284:33815-33823. http://dx.doi.org/10.1074/jbc. M109.065938.
    • (2009) J Biol Chem , vol.284 , pp. 33815-33823
    • Viarre, V.1    Cascales, E.2    Ball, G.3    Michel, G.P.4    Filloux, A.5    Voulhoux, R.6
  • 39
    • 56649123517 scopus 로고    scopus 로고
    • The Burkholderia Genome Database: Facilitating flexible queries and comparative analyses
    • Winsor GL, Khaira B, Van Rossum T, Lo R, Whiteside MD, Brinkman FSL. 2008. The Burkholderia Genome Database: facilitating flexible queries and comparative analyses. Bioinformatics 24:2803-2804. http://dx.doi.org/10.1093/bioinformatics/btn524.
    • (2008) Bioinformatics , vol.24 , pp. 2803-2804
    • Winsor, G.L.1    Khaira, B.2    Van Rossum, T.3    Lo, R.4    Whiteside, M.D.5    Brinkman, F.S.L.6


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