메뉴 건너뛰기




Volumn 49, Issue 10, 2005, Pages 4227-4233

Glycopeptide resistance vanA operons in Paenibacillus strains isolated from soil

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; FUSIDIC ACID; GLYCOPEPTIDE; PEPTIDOGLYCAN; PLASMID DNA; RIFAMPICIN; TEICOPLANIN; VANCOMYCIN;

EID: 25844514318     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.49.10.4227-4233.2005     Document Type: Article
Times cited : (48)

References (39)
  • 1
    • 0030036676 scopus 로고    scopus 로고
    • Quantitative analysis of the metabolism of soluble cytoplasmic peptidoglycan precursors of glycopeptide-resistant enterococci
    • Arthur, M., F. Depardieu, P. Reynolds, and P. Courvalin. 1996. Quantitative analysis of the metabolism of soluble cytoplasmic peptidoglycan precursors of glycopeptide-resistant enterococci. Mol. Microbiol. 21:33-44.
    • (1996) Mol. Microbiol. , vol.21 , pp. 33-44
    • Arthur, M.1    Depardieu, F.2    Reynolds, P.3    Courvalin, P.4
  • 2
    • 0027391961 scopus 로고
    • Characterization of Tn1546, a Tn3-related transposon conferring glycopeptide resistance by synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147
    • Arthur, M., C. Molinas, F. Depardieu, and P. Courvalin. 1993. Characterization of Tn1546, a Tn3-related transposon conferring glycopeptide resistance by synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J. Bacteriol. 175:117-127.
    • (1993) J. Bacteriol. , vol.175 , pp. 117-127
    • Arthur, M.1    Molinas, C.2    Depardieu, F.3    Courvalin, P.4
  • 4
    • 11244279103 scopus 로고    scopus 로고
    • Comparison of three PCR primer sets for identification of vanB gene carriage in feces and correlation with carriage of vancomycin-resistant enterococci: Interference by vanB-containing anaerobic bacilli
    • Ballard, S. A., E. A. Grabsch, P. D. Johnson, and M. L. Grayson. 2005. Comparison of three PCR primer sets for identification of vanB gene carriage in feces and correlation with carriage of vancomycin-resistant enterococci: interference by vanB-containing anaerobic bacilli. Antimicrob. Agents Chemother. 49:77-81.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 77-81
    • Ballard, S.A.1    Grabsch, E.A.2    Johnson, P.D.3    Grayson, M.L.4
  • 5
    • 0028286852 scopus 로고
    • Modification of peptidoglycan precursors is a common feature of the low-level vancomycin-resistant VANB-type enterococcus D366 and of the naturally glycopeptide-resistant species Lactobacillus casei, Pediococcus pentosaceus, Leuconostoc mesenteroides, and Enterococcus gallinarum
    • Billot-Klein, D., L. Gutmann, S. Sable, E. Guittet, and J. van Heijenoort. 1994. Modification of peptidoglycan precursors is a common feature of the low-level vancomycin-resistant VANB-type enterococcus D366 and of the naturally glycopeptide-resistant species Lactobacillus casei, Pediococcus pentosaceus, Leuconostoc mesenteroides, and Enterococcus gallinarum. J. Bacteriol. 176:2398-2405.
    • (1994) J. Bacteriol. , vol.176 , pp. 2398-2405
    • Billot-Klein, D.1    Gutmann, L.2    Sable, S.3    Guittet, E.4    Van Heijenoort, J.5
  • 6
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 7
    • 0031783527 scopus 로고    scopus 로고
    • Genetic linkage and cotransfer of a novel, vanB-containing transposon (Tn5382) and a low-affinity penicillin-binding protein 5 gene in a clinical vancomycin-resistant Enterococcus faecium isolate
    • Carias, L. L., S. D. Rudin, C. J. Donskey, and L. B. Rice. 1998. Genetic linkage and cotransfer of a novel, vanB-containing transposon (Tn5382) and a low-affinity penicillin-binding protein 5 gene in a clinical vancomycin-resistant Enterococcus faecium isolate. J. Bacteriol. 180:4426-4434.
    • (1998) J. Bacteriol. , vol.180 , pp. 4426-4434
    • Carias, L.L.1    Rudin, S.D.2    Donskey, C.J.3    Rice, L.B.4
  • 8
    • 11244262829 scopus 로고    scopus 로고
    • Comparison of Tn1546-like elements in vancomycin-resistant Staphylococcus aureus isolates from Michigan and Pennsylvania
    • Clark, N. C., L. M. Weigel, J. B. Patel, and F. C. Tenover. 2005. Comparison of Tn1546-like elements in vancomycin-resistant Staphylococcus aureus isolates from Michigan and Pennsylvania. Antimicrob. Agents Chemother. 49:470-472.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 470-472
    • Clark, N.C.1    Weigel, L.M.2    Patel, J.B.3    Tenover, F.C.4
  • 9
    • 0242606104 scopus 로고    scopus 로고
    • The vanG glycopeptide resistance operon from Enterococcus faecalis revisited
    • Depardieu, F., M. G. Bonora, P. E. Reynolds, and P. Courvalin. 2003. The vanG glycopeptide resistance operon from Enterococcus faecalis revisited. Mol. Microbiol. 50:931-948.
    • (2003) Mol. Microbiol. , vol.50 , pp. 931-948
    • Depardieu, F.1    Bonora, M.G.2    Reynolds, P.E.3    Courvalin, P.4
  • 10
    • 0027518660 scopus 로고
    • The vanB gene of vancomycin-resistant Enterococcus faecalis V583 is structurally related to genes encoding D-Ala:D-Ala ligases and glycopeptide-resistance proteins VanA and VanC
    • Evers, S., D. F. Sahm, and P. Courvalin. 1993. The vanB gene of vancomycin-resistant Enterococcus faecalis V583 is structurally related to genes encoding D-Ala:D-Ala ligases and glycopeptide-resistance proteins VanA and VanC. Gene 124:143-144.
    • (1993) Gene , vol.124 , pp. 143-144
    • Evers, S.1    Sahm, D.F.2    Courvalin, P.3
  • 11
    • 0019578458 scopus 로고
    • Reverse-phase high-pressure liquid chromatography of uridine diphosphate N-acetylmuramyl peptide precursors of bacterial cell wall peptidoglycan
    • Flouret, B., D. Mengin-Lecreulx, and J. van Hegenoort. 1981. Reverse-phase high-pressure liquid chromatography of uridine diphosphate N-acetylmuramyl peptide precursors of bacterial cell wall peptidoglycan. Anal. Biochem. 114:59-63.
    • (1981) Anal. Biochem. , vol.114 , pp. 59-63
    • Flouret, B.1    Mengin-Lecreulx, D.2    Van Hegenoort, J.3
  • 12
    • 21444436742 scopus 로고    scopus 로고
    • Putative VanRS-like two-component regulatory system associated with the inducible glycopeptide resistance cluster of Paenibacillus popilliae
    • Fraimow, H., C. Knob, I. A. Herrero, and R. Patel. 2005. Putative VanRS-like two-component regulatory system associated with the inducible glycopeptide resistance cluster of Paenibacillus popilliae. Antimicrob. Agents Chemother. 49:2625-2633.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2625-2633
    • Fraimow, H.1    Knob, C.2    Herrero, I.A.3    Patel, R.4
  • 13
    • 0034045195 scopus 로고    scopus 로고
    • Characterization of transposon Tn1549, conferring VanB-type resistance in Enterococcus spp
    • Garnier, F., S. Taourit, P. Glaser, P. Courvalin, and M. Galimand. 2000. Characterization of transposon Tn1549, conferring VanB-type resistance in Enterococcus spp. Microbiology 146:1481-1489.
    • (2000) Microbiology , vol.146 , pp. 1481-1489
    • Garnier, F.1    Taourit, S.2    Glaser, P.3    Courvalin, P.4    Galimand, M.5
  • 14
    • 0034536220 scopus 로고    scopus 로고
    • Acquired and intrinsic glycopeptide resistance in enterococci
    • Gholizadeh, Y., and P. Courvalin. 2000. Acquired and intrinsic glycopeptide resistance in enterococci. Int. J. Antimicrob. Agents 16(Suppl. 1):S11-S17.
    • (2000) Int. J. Antimicrob. Agents , vol.16 , Issue.SUPPL. 1
    • Gholizadeh, Y.1    Courvalin, P.2
  • 15
    • 9644252836 scopus 로고    scopus 로고
    • Members of the genera Paenibacillus and Rhodococcus harbor genes homologous to enterococcal glycopeptide resistance genes vanA and vanB
    • Guardabassi, L., H. Christensen, H. Hasman, and A. Dalsgaard. 2004. Members of the genera Paenibacillus and Rhodococcus harbor genes homologous to enterococcal glycopeptide resistance genes vanA and vanB. Antimicrob. Agents Chemother. 48:4915-4918.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4915-4918
    • Guardabassi, L.1    Christensen, H.2    Hasman, H.3    Dalsgaard, A.4
  • 16
    • 0033754208 scopus 로고    scopus 로고
    • Paenibacillus associated with milky disease in Central and South American scarabs
    • Harrison, H., R. Patel, and A. A. Yousten. 2000. Paenibacillus associated with milky disease in Central and South American scarabs. J. Invertebr. Pathol. 76:169-175.
    • (2000) J. Invertebr. Pathol. , vol.76 , pp. 169-175
    • Harrison, H.1    Patel, R.2    Yousten, A.A.3
  • 18
    • 0031927586 scopus 로고    scopus 로고
    • vanA gene cluster in a vancomycin-resistant clinical isolate of Bacillus circulons
    • Ligozzi, M., G. Lo Cascio, and R. Fontana. 1998. vanA gene cluster in a vancomycin-resistant clinical isolate of Bacillus circulons. Antimicrob. Agents Chemother. 42:2055-2059.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2055-2059
    • Ligozzi, M.1    Lo Cascio, G.2    Fontana, R.3
  • 19
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu, Y. G., and R. F. Whittier. 1995. Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25:674-681.
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.G.1    Whittier, R.F.2
  • 20
    • 0031663280 scopus 로고    scopus 로고
    • Glycopeptide antibiotic resistance genes in glycopeptide-producing organisms
    • Marshall, C. G., I. A. Lessard, I. Park, and G. D. Wright. 1998. Glycopeptide antibiotic resistance genes in glycopeptide-producing organisms. Antimicrob. Agents Chemother. 42:2215-2220.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2215-2220
    • Marshall, C.G.1    Lessard, I.A.2    Park, I.3    Wright, G.D.4
  • 21
    • 0020458828 scopus 로고
    • Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli
    • Mengin-Lecreulx, D., B. Flouret, and J. van Heijenoort. 1982. Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 151:1109-1117.
    • (1982) J. Bacteriol. , vol.151 , pp. 1109-1117
    • Mengin-Lecreulx, D.1    Flouret, B.2    Van Heijenoort, J.3
  • 23
    • 0034177382 scopus 로고    scopus 로고
    • Enterococcal-type glycopeptide resistance genes in non-enterococcal organisms
    • Patel, R. 2000. Enterococcal-type glycopeptide resistance genes in non-enterococcal organisms. FEMS Microbiol. Lett. 185:1-7.
    • (2000) FEMS Microbiol. Lett. , vol.185 , pp. 1-7
    • Patel, R.1
  • 24
    • 0033994788 scopus 로고    scopus 로고
    • The biopesticide Paenibacillus popilliae has a vancomycin resistance gene cluster homologous to the enterococcal VanA vancomycin resistance gene cluster
    • Patel, R., K. Piper, F. R. Cockerill III, J. M. Steckelberg, and A. A. Yousten. 2000. The biopesticide Paenibacillus popilliae has a vancomycin resistance gene cluster homologous to the enterococcal VanA vancomycin resistance gene cluster. Antimicrob. Agents Chemother. 44:705-709.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 705-709
    • Patel, R.1    Piper, K.2    Cockerill III, F.R.3    Steckelberg, J.M.4    Yousten, A.A.5
  • 26
    • 0028825954 scopus 로고
    • vanA genes in vancomycin-resistant clinical isolates of Oerskovia turbata and Arcanobacterium (Corynebacterium) haemolyticum
    • Power, E. G., Y. H. Abdulla, H. G. Talsania, W. Spice, S. Aathithan, and G. L. French. 1995. vanA genes in vancomycin-resistant clinical isolates of Oerskovia turbata and Arcanobacterium (Corynebacterium) haemolyticum. J. Antimicrob. Chemother. 36:595-606.
    • (1995) J. Antimicrob. Chemother. , vol.36 , pp. 595-606
    • Power, E.G.1    Abdulla, Y.H.2    Talsania, H.G.3    Spice, W.4    Aathithan, S.5    French, G.L.6
  • 27
    • 0031038389 scopus 로고    scopus 로고
    • Emergence of vancomycin resistance in the genus Streptococcus: Characterization of a vanB transferable determinant in Streptococcus bovis
    • Poyart, C., C. Pierre, G. Quesne, B. Pron, P. Berche, and P. Trieu-Cuot. 1997. Emergence of vancomycin resistance in the genus Streptococcus: characterization of a vanB transferable determinant in Streptococcus bovis. Antimicrob. Agents Chemother. 41:24-29.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 24-29
    • Poyart, C.1    Pierre, C.2    Quesne, G.3    Pron, B.4    Berche, P.5    Trieu-Cuot, P.6
  • 28
    • 0029889580 scopus 로고    scopus 로고
    • Characterization of Tn1547, a composite transposon flanked by the IS16 and IS256-like elements, that confers vancomycin resistance in Enterococcus faecalis BM4281
    • Quintiliani, R., Jr., and P. Courvalin. 1996. Characterization of Tn1547, a composite transposon flanked by the IS16 and IS256-like elements, that confers vancomycin resistance in Enterococcus faecalis BM4281. Gene 172:1-8.
    • (1996) Gene , vol.172 , pp. 1-8
    • Quintiliani Jr., R.1    Courvalin, P.2
  • 29
    • 0024355483 scopus 로고
    • Structure, biochemistry and mechanism of action of glycopeptide antibiotics
    • Reynolds, P. E. 1989. Structure, biochemistry and mechanism of action of glycopeptide antibiotics. Eur. J. Clin. Microbiol. Infect. Dis. 8:943-950.
    • (1989) Eur. J. Clin. Microbiol. Infect. Dis. , vol.8 , pp. 943-950
    • Reynolds, P.E.1
  • 30
    • 0034802151 scopus 로고    scopus 로고
    • The VanY(D) DD-carboxypeptidase of Enterococcus faecium BM4339 is a penicillin-binding protein
    • Reynolds, P. E., O. H. Ambur, B. Casadewall, and P. Courvalin. 2001. The VanY(D) DD-carboxypeptidase of Enterococcus faecium BM4339 is a penicillin-binding protein. Microbiology 147:2571-2578.
    • (2001) Microbiology , vol.147 , pp. 2571-2578
    • Reynolds, P.E.1    Ambur, O.H.2    Casadewall, B.3    Courvalin, P.4
  • 31
    • 11244307455 scopus 로고    scopus 로고
    • Vancomycin resistance in enterococci due to synthesis of precursors terminating in D-alanyl-D-serine
    • Reynolds, P. E., and P. Courvalin. 2005. Vancomycin resistance in enterococci due to synthesis of precursors terminating in D-alanyl-D-serine. Antimicrob. Agents Chemother. 49:21-25.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 21-25
    • Reynolds, P.E.1    Courvalin, P.2
  • 32
    • 0028076784 scopus 로고
    • Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine
    • Reynolds, P. E., F. Depardieu, S. Dutka-Malen, M. Arthur, and P. Courvalin. 1994. Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine. Mol. Microbiol. 13:1065-1070.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1065-1070
    • Reynolds, P.E.1    Depardieu, F.2    Dutka-Malen, S.3    Arthur, M.4    Courvalin, P.5
  • 33
    • 0028235256 scopus 로고
    • Analysis of peptidoglycan precursors in vancomycin-resistant Enterococcus gallinarum BM4174
    • Reynolds, P. E., H. A. Snaith, A. J. Maguire, S. Dutka-Malen, and P. Courvalin. 1994. Analysis of peptidoglycan precursors in vancomycin-resistant Enterococcus gallinarum BM4174. Biochem. J. 301:5-8.
    • (1994) Biochem. J. , vol.301 , pp. 5-8
    • Reynolds, P.E.1    Snaith, H.A.2    Maguire, A.J.3    Dutka-Malen, S.4    Courvalin, P.5
  • 34
    • 0028293918 scopus 로고    scopus 로고
    • Cloning, expression, and nucleotide sequence of genes involved in production of lactococcin DR, a bacteriocin from Lactococcus lactis subsp. lactis
    • Rince, A., A. Dufour, S. Le Pogam, D. Thuault, C. M. Bourgeois, and J. P. Le Pennec. 2000. Cloning, expression, and nucleotide sequence of genes involved in production of lactococcin DR, a bacteriocin from Lactococcus lactis subsp. lactis. Appl. Environ. Microbiol. 60:1652-1657.
    • (2000) Appl. Environ. Microbiol. , vol.60 , pp. 1652-1657
    • Rince, A.1    Dufour, A.2    Le Pogam, S.3    Thuault, D.4    Bourgeois, C.M.5    Le Pennec, J.P.6
  • 35
    • 0030999754 scopus 로고    scopus 로고
    • Transfer of Bacillus alginolyticus, Bacillus chondroitinus, Bacillus curdlanolyticus, Bacillus glucanolyticus, Bacillus kobensis, and Bacillus thiaminolyticus to the genus Paenibacillus and emended description of the genus Paenibacillus
    • Shida, O., H. Takagi, K. Kadowaki, L. K. Nakamura, and K. Komagata. 1997. Transfer of Bacillus alginolyticus, Bacillus chondroitinus, Bacillus curdlanolyticus, Bacillus glucanolyticus, Bacillus kobensis, and Bacillus thiaminolyticus to the genus Paenibacillus and emended description of the genus Paenibacillus. Int. J. Syst. Bacteriol. 47:289-298.
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 289-298
    • Shida, O.1    Takagi, H.2    Kadowaki, K.3    Nakamura, L.K.4    Komagata, K.5
  • 36
    • 0020558202 scopus 로고
    • Changes in penicillin-binding proteins during sporulation of Bacillus subtilis
    • Sowell, M. O., and C. E. Buchanan. 1983. Changes in penicillin-binding proteins during sporulation of Bacillus subtilis. J. Bacteriol. 153:1331-1337.
    • (1983) J. Bacteriol. , vol.153 , pp. 1331-1337
    • Sowell, M.O.1    Buchanan, C.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.