메뉴 건너뛰기




Volumn 156, Issue 8, 2010, Pages 2327-2335

Induction of β-lactamase production in Aeromonas hydrophila is responsive to β-lactam-mediated changes in peptidoglycan composition

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAM; BETA LACTAMASE; CARBOXYPEPTIDASE; PENICILLIN BINDING PROTEIN; PENTAPEPTIDE; PEPTIDOGLYCAN; PROTEIN BIRB; PROTEIN KINASE; PROTEINASE; UNCLASSIFIED DRUG; VANCOMYCIN; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN;

EID: 77955347337     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.035220-0     Document Type: Article
Times cited : (48)

References (41)
  • 1
    • 0030941680 scopus 로고    scopus 로고
    • Expression of AsbA1, OXA-12 and AsbM1 β-lactamases in Aeromonas jandaei AER14 is coordinated by a two-component regulon
    • Alksne, L. E. & Rasmussen, B. A. (1997). Expression of AsbA1, OXA-12 and AsbM1 β-lactamases in Aeromonas jandaei AER14 is coordinated by a two-component regulon. J Bacteriol 179, 2006-2013.
    • (1997) J Bacteriol , vol.179 , pp. 2006-2013
    • Alksne, L.E.1    Rasmussen, B.A.2
  • 3
    • 0034924241 scopus 로고    scopus 로고
    • Determination of minimum inhibitory concentrations
    • Andrews, J.M. (2001). Determination of minimum inhibitory concentrations. J Antimicrob Chemother 48 (Suppl. S1), 5-16.
    • (2001) J Antimicrob Chemother , vol.48 , Issue.SUPPL. S1 , pp. 5-16
    • Andrews, J.M.1
  • 4
    • 0033626172 scopus 로고    scopus 로고
    • The Aeromonas hydrophila AmpH and CepH β-lactamases: Increased expression in mutants of Escherichia coli lacking creB
    • Avison, M. B., Niumsup, P., Walsh, T. R. & Bennett, P. M. (2000a). The Aeromonas hydrophila AmpH and CepH β-lactamases: increased expression in mutants of Escherichia coli lacking creB. J Antimicrob Chemother 46, 695-702.
    • (2000) J Antimicrob Chemother , vol.46 , pp. 695-702
    • Avison, M.B.1    Niumsup, P.2    Walsh, T.R.3    Bennett, P.M.4
  • 5
    • 0034353183 scopus 로고    scopus 로고
    • A TEM β-lactamase encoded on an active Tn1-like transposon in the genome of a clinical isolate of Stenotrophomonas maltophilia
    • Avison, M. B., von Heldreich, C. J., Higgins, C. S., Bennett, P. M. & Walsh, T. R. (2000b). A TEM β-lactamase encoded on an active Tn1-like transposon in the genome of a clinical isolate of Stenotrophomonas maltophilia. J Antimicrob Chemother 46, 879-884.
    • (2000) J Antimicrob Chemother , vol.46 , pp. 879-884
    • Avison, M.B.1    Von Heldreich, C.J.2    Higgins, C.S.3    Bennett, P.M.4    Walsh, T.R.5
  • 6
    • 0035920119 scopus 로고    scopus 로고
    • Escherichia coli CreBC is a global regulator of gene expression that responds to growth in minimal media
    • Avison, M. B., Horton, R. E., Walsh, T. R. & Bennett, P. M. (2001). Escherichia coli CreBC is a global regulator of gene expression that responds to growth in minimal media. J Biol Chem 276, 26955-26961.
    • (2001) J Biol Chem , vol.276 , pp. 26955-26961
    • Avison, M.B.1    Horton, R.E.2    Walsh, T.R.3    Bennett, P.M.4
  • 8
    • 1242285445 scopus 로고    scopus 로고
    • Role of the 'cre/blr-tag' DNA sequence in regulation of gene expression by the Aeromonas hydrophila β-lactamase regulator, BlrA
    • Avison, M. B., Niumsup, P., Nurmahomed, K., Walsh, T. R. & Bennett, P. M. (2004). Role of the 'cre/blr-tag' DNA sequence in regulation of gene expression by the Aeromonas hydrophila β-lactamase regulator, BlrA. J Antimicrob Chemother 53, 197-202.
    • (2004) J Antimicrob Chemother , vol.53 , pp. 197-202
    • Avison, M.B.1    Niumsup, P.2    Nurmahomed, K.3    Walsh, T.R.4    Bennett, P.M.5
  • 9
    • 27644534247 scopus 로고    scopus 로고
    • Penicillin-binding proteins of Bacteroides fragilis and their role in the resistance to imipenem of clinical isolates
    • Ayala, J., Quesada, A., Vadillo, S., Criado, J. & Piriz, S. (2005). Penicillin-binding proteins of Bacteroides fragilis and their role in the resistance to imipenem of clinical isolates. J Med Microbiol 54, 1055-1064.
    • (2005) J Med Microbiol , vol.54 , pp. 1055-1064
    • Ayala, J.1    Quesada, A.2    Vadillo, S.3    Criado, J.4    Piriz, S.5
  • 10
    • 0036889483 scopus 로고    scopus 로고
    • Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides
    • Cheng, Q. & Park, J. T. (2002). Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides. J Bacteriol 184, 6434-6436.
    • (2002) J Bacteriol , vol.184 , pp. 6434-6436
    • Cheng, Q.1    Park, J.T.2
  • 11
    • 0025195680 scopus 로고
    • Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gramnegative Eubacteria
    • de Lorenzo, V., Herrero, M., Jakubzik, U. & Timmis, K. N. (1990). Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gramnegative Eubacteria. J Bacteriol 172, 6568-6572.
    • (1990) J Bacteriol , vol.172 , pp. 6568-6572
    • De Lorenzo, V.1    Herrero, M.2    Jakubzik, U.3    Timmis, K.N.4
  • 12
    • 0030802782 scopus 로고    scopus 로고
    • The signal molecule for β-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide
    • Dietz, H., Pfeifle, D. & Wiedemann, B. (1997). The signal molecule for β-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide. Antimicrob Agents Chemother 41, 2113-2120.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 2113-2120
    • Dietz, H.1    Pfeifle, D.2    Wiedemann, B.3
  • 13
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner, B. (1988). Separation and quantification of muropeptides with high-performance liquid chromatography. Anal Biochem 172, 451-464.
    • (1988) Anal Biochem , vol.172 , pp. 451-464
    • Glauner, B.1
  • 14
    • 0030610494 scopus 로고    scopus 로고
    • Studies on the repressor (BlaI) of β-lactamase synthesis in Staphylococcus aureus
    • Gregory, P. D., Lewis, R. A., Curnock, S. P. & Dyke, K. G. (1997). Studies on the repressor (BlaI) of β-lactamase synthesis in Staphylococcus aureus. Mol Microbiol 24, 1025-1037.
    • (1997) Mol Microbiol , vol.24 , pp. 1025-1037
    • Gregory, P.D.1    Lewis, R.A.2    Curnock, S.P.3    Dyke, K.G.4
  • 15
    • 0032700851 scopus 로고    scopus 로고
    • Regulation of inducible AmpC β-lactamase expression among Enterobacteriaceae
    • Hanson, N. D. & Sanders, C. C. (1999). Regulation of inducible AmpC β-lactamase expression among Enterobacteriaceae. Curr Pharm Des 5, 881-894.
    • (1999) Curr Pharm des , vol.5 , pp. 881-894
    • Hanson, N.D.1    Sanders, C.C.2
  • 17
    • 0343632366 scopus 로고    scopus 로고
    • Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in Gram-negative bacteria
    • Jacobs, C., Frere, J. M. & Normark, S. (1997). Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in Gram-negative bacteria. Cell 88, 823-832.
    • (1997) Cell , vol.88 , pp. 823-832
    • Jacobs, C.1    Frere, J.M.2    Normark, S.3
  • 18
    • 27644463418 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB β-lactamases, proteases, quorum sensing, and other virulence factors
    • Kong, K. F., Jayawardena, S. R., Indulkar, S. D., Del Puerto, A., Koh, C. L., Høiby, N. & Mathee, K. (2005). Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB β-lactamases, proteases, quorum sensing, and other virulence factors. Antimicrob Agents Chemother 49, 4567-4575.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4567-4575
    • Kong, K.F.1    Jayawardena, S.R.2    Indulkar, S.D.3    Del Puerto, A.4    Koh, C.L.5    Høiby, N.6    Mathee, K.7
  • 19
    • 33845731273 scopus 로고    scopus 로고
    • Genetic relationships of Aeromonas strains inferred from 16S rRNA, gyrB and rpoB gene sequences
    • Küpfer, M., Kuhnert, P., Korczak, B. M., Peduzzi, R. & Demarta, A. (2006). Genetic relationships of Aeromonas strains inferred from 16S rRNA, gyrB and rpoB gene sequences. Int J Syst Evol Microbiol 56, 2743-2751.
    • (2006) Int J Syst Evol Microbiol , vol.56 , pp. 2743-2751
    • Küpfer, M.1    Kuhnert, P.2    Korczak, B.M.3    Peduzzi, R.4    Demarta, A.5
  • 20
    • 0027328960 scopus 로고
    • Investigation of the Pseudomonas aeruginosa ampR gene and its role in the chromosomal ampC β-lactamase promoter
    • Lodge, J., Busby, S. & Piddock, L. (1993). Investigation of the Pseudomonas aeruginosa ampR gene and its role in the chromosomal ampC β-lactamase promoter. FEMS Microbiol Lett 111, 315-320.
    • (1993) FEMS Microbiol Lett , vol.111 , pp. 315-320
    • Lodge, J.1    Busby, S.2    Piddock, L.3
  • 21
    • 0023787932 scopus 로고
    • pACYC184-derived cloning vectors containing the multiple cloning site and lacZ-alpha reporter gene of pUC8/9 and pUC18/19
    • Martinez, E., Bartolome, B. & de la Cruz, F. (1988). pACYC184-derived cloning vectors containing the multiple cloning site and lacZ-alpha reporter gene of pUC8/9 and pUC18/19. Gene 68, 159-162.
    • (1988) Gene , vol.68 , pp. 159-162
    • Martinez, E.1    Bartolome, B.2    De La Cruz, F.3
  • 22
    • 63449128597 scopus 로고    scopus 로고
    • β-Lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein
    • Moya, B., Dötsch, A., Juan, C., Blázquez, J., Zamorano, L., Haussler, S. & Oliver, A. (2009). β-Lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein. PLoS Pathog 5, e1000353.
    • (2009) PLoS Pathog , vol.5
    • Moya, B.1    Dötsch, A.2    Juan, C.3    Blázquez, J.4    Zamorano, L.5    Haussler, S.6    Oliver, A.7
  • 23
    • 0038647815 scopus 로고    scopus 로고
    • Genetic linkage of the penicillinase gene, amp, and blrAB, encoding the regulator of β-lactamase expression in Aeromonas spp.
    • Niumsup, P., Simm, A. M., Nurmahomed, K., Walsh, T. R., Bennett, P. M. & Avison, M. B. (2003). Genetic linkage of the penicillinase gene, amp, and blrAB, encoding the regulator of β-lactamase expression in Aeromonas spp. J Antimicrob Chemother 51, 1351-1358.
    • (2003) J Antimicrob Chemother , vol.51 , pp. 1351-1358
    • Niumsup, P.1    Simm, A.M.2    Nurmahomed, K.3    Walsh, T.R.4    Bennett, P.M.5    Avison, M.B.6
  • 24
    • 0013852879 scopus 로고
    • The genetic determinant of staphylococcal penicillinase
    • Novick, R. P. (1965). The genetic determinant of staphylococcal penicillinase. Ann N Y Acad Sci 128, 165-182.
    • (1965) Ann N Y Acad Sci , vol.128 , pp. 165-182
    • Novick, R.P.1
  • 25
    • 42049088493 scopus 로고    scopus 로고
    • Induction of L1 and L2 β-lactamase production in Stenotrophomonas maltophilia is dependent on an AmpR-type regulator
    • Okazaki, A. & Avison, M. B. (2008). Induction of L1 and L2 β-lactamase production in Stenotrophomonas maltophilia is dependent on an AmpR-type regulator. Antimicrob Agents Chemother 52, 1525-1528.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 1525-1528
    • Okazaki, A.1    Avison, M.B.2
  • 26
    • 0025953798 scopus 로고
    • Induction of class I blactamase from Citrobacter freundii in Escherichia coli requires active ftsZ but not ftsA or ftsQ products
    • Ottolenghi, A. C. & Ayala, J. A. (1991). Induction of class I blactamase from Citrobacter freundii in Escherichia coli requires active ftsZ but not ftsA or ftsQ products. Antimicrob Agents Chemother 35, 2359-2365.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 2359-2365
    • Ottolenghi, A.C.1    Ayala, J.A.2
  • 27
    • 0003040750 scopus 로고
    • Strategies for cloning in plasmid vectors
    • 2nd edn, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Strategies for cloning in plasmid vectors. In Molecular Cloning, a Laboratory Manual, vol. 1, 2nd edn, pp. 53-104. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1989) Molecular Cloning, a Laboratory Manual , vol.1 , pp. 53-104
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 29
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis
    • Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A. & Charlier, P. (2008). The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 32, 234-258.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 31
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bacteria
    • Simon, R., Priefer, U. B. & Puhler, A. (1983). A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Biotechnology 1, 784-791.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.B.2    Puhler, A.3
  • 32
    • 0343683423 scopus 로고    scopus 로고
    • Characterization of the penA and penR genes of Burkholderia cepacia 249 which encode the chromosomal class A penicillinase and its LysR-type transcriptional regulator
    • Trepanier, S., Prince, A. & Huletsky, A. (1997). Characterization of the penA and penR genes of Burkholderia cepacia 249 which encode the chromosomal class A penicillinase and its LysR-type transcriptional regulator. Antimicrob Agents Chemother 41, 2399-2405.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 2399-2405
    • Trepanier, S.1    Prince, A.2    Huletsky, A.3
  • 33
    • 0026035965 scopus 로고
    • Coordinate regulation of β-lactamase induction and peptidoglycan composition by the amp operon
    • Tuomanen, E., Lindquist, S., Sande, S., Galleni, M., Light, K., Gage, D. & Normark, S. (1991). Coordinate regulation of β-lactamase induction and peptidoglycan composition by the amp operon. Science 251, 201-204.
    • (1991) Science , vol.251 , pp. 201-204
    • Tuomanen, E.1    Lindquist, S.2    Sande, S.3    Galleni, M.4    Light, K.5    Gage, D.6    Normark, S.7
  • 34
    • 4944223117 scopus 로고    scopus 로고
    • Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli
    • Ursinus, A., van den Ent, F., Brechtel, S., de Pedro, M. A., Höltje, J.-V. & Vollmer, W. (2004). Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli. J Bacteriol 186, 6728-6737.
    • (2004) J Bacteriol , vol.186 , pp. 6728-6737
    • Ursinus, A.1    Van Den Ent, F.2    Brechtel, S.3    De Pedro, M.A.4    Höltje, J.-V.5    Vollmer, W.6
  • 35
    • 0034671524 scopus 로고    scopus 로고
    • Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction
    • Vötsch, W. & Templin, M. F. (2000). Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction. J Biol Chem 275, 39032-39038.
    • (2000) J Biol Chem , vol.275 , pp. 39032-39038
    • Vötsch, W.1    Templin, M.F.2
  • 36
    • 0028964736 scopus 로고
    • A clinical isolate of Aeromonas sobria with three chromosomally mediated inducible β-lactamases: A cephalosporinase, a penicillinase and a third enzyme, displaying carbapenemase activity
    • Walsh, T. R., Payne, D. J., MacGowan, A. P. & Bennett, P. M. (1995). A clinical isolate of Aeromonas sobria with three chromosomally mediated inducible β-lactamases: a cephalosporinase, a penicillinase and a third enzyme, displaying carbapenemase activity. J Antimicrob Chemother 35, 271-279.
    • (1995) J Antimicrob Chemother , vol.35 , pp. 271-279
    • Walsh, T.R.1    Payne, D.J.2    MacGowan, A.P.3    Bennett, P.M.4
  • 38
    • 0021624644 scopus 로고
    • Mode of action and in-vitro activity of vancomycin
    • Watanakunakorn, C. (1984). Mode of action and in-vitro activity of vancomycin. J Antimicrob Chemother 14 (Suppl. D), 7-18.
    • (1984) J Antimicrob Chemother , vol.14 , Issue.SUPPL. D , pp. 7-18
    • Watanakunakorn, C.1
  • 39
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West, A. H. & Stock, A. M. (2001). Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem Sci 26, 369-376.
    • (2001) Trends Biochem Sci , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 40
    • 8744251330 scopus 로고    scopus 로고
    • Crystal structures of the Apo and penicillin-acylated forms of the BlaR1 β-lactam sensor of Staphylococcus aureus
    • Wilke, M. S., Hills, T. L., Zhang, H. Z., Chambers, H. F. & Strynadka, N. C. (2004). Crystal structures of the Apo and penicillin-acylated forms of the BlaR1 β-lactam sensor of Staphylococcus aureus. J Biol Chem 279, 47278-47287.
    • (2004) J Biol Chem , vol.279 , pp. 47278-47287
    • Wilke, M.S.1    Hills, T.L.2    Zhang, H.Z.3    Chambers, H.F.4    Strynadka, N.C.5
  • 41
    • 0035831262 scopus 로고    scopus 로고
    • A proteolytic transmembrane signalling pathway and resistance to β-lactams in Staphylococci
    • Zhang, H. Z., Hackbarth, C. J., Chansky, K. M. & Chambers, H. F. (2001). A proteolytic transmembrane signalling pathway and resistance to β-lactams in Staphylococci. Science 291, 1962-1965.
    • (2001) Science , vol.291 , pp. 1962-1965
    • Zhang, H.Z.1    Hackbarth, C.J.2    Chansky, K.M.3    Chambers, H.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.