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Volumn 3, Issue 4, 2014, Pages 572-594

Old and new glycopeptide antibiotics: Action and resistance

Author keywords

Dalbavancin; Glycopeptides; Nonomuraea sp. ATCC 39727; Resistance; Van genes

Indexed keywords

AVOPARCIN; BALHIMYCIN; DALBAVANCIN; ORITAVANCIN; PENICILLIN BINDING PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; RISTOCETIN; TEICOPLANIN; TELAVANCIN; VANCOMYCIN;

EID: 84979847575     PISSN: None     EISSN: 20796382     Source Type: Journal    
DOI: 10.3390/antibiotics3040572     Document Type: Review
Times cited : (125)

References (96)
  • 1
    • 84930246069 scopus 로고    scopus 로고
    • Novel infectious diseases and emerging gram-positive multiresistant pathogens in hospital and community acquired infections
    • Marinelli, F., Genilloud, O., Eds.; Springer Verlag: Berlin Heidelberg, Germany
    • Rossolini, G. M.; Arena, F.; Pollini, S. Novel infectious diseases and emerging gram-positive multiresistant pathogens in hospital and community acquired infections. In Antimicrobials; Marinelli, F., Genilloud, O., Eds.; Springer Verlag: Berlin Heidelberg, Germany, 2014.
    • (2014) Antimicrobials
    • Rossolini, G.M.1    Arena, F.2    Pollini, S.3
  • 3
    • 14844339524 scopus 로고    scopus 로고
    • Glycopeptide and lipoglycopeptide antibiotics
    • Kahne, D.; Leimkuhler, C.; Lu, W.; Walsh, C. Glycopeptide and lipoglycopeptide antibiotics. Chem. Rev. 2005, 105, 425-448.
    • (2005) Chem. Rev , vol.105 , pp. 425-448
    • Kahne, D.1    Leimkuhler, C.2    Lu, W.3    Walsh, C.4
  • 4
    • 78149466664 scopus 로고    scopus 로고
    • β-Lactam and glycopeptide antibiotics: First and last line of defense?
    • Jovetic, S.; Zhu, Y.; Marcone, G. L.; Marinelli, F.; Tramper, J. β-Lactam and glycopeptide antibiotics: First and last line of defense? Trends Biotechnol. 2010, 28, 596-604.
    • (2010) Trends Biotechnol , vol.28 , pp. 596-604
    • Jovetic, S.1    Zhu, Y.2    Marcone, G.L.3    Marinelli, F.4    Tramper, J.5
  • 5
    • 84930246642 scopus 로고    scopus 로고
    • Glycopeptides: An old but up to date successful antibiotic class
    • Marinelli, F., Genilloud, O., Eds.; Springer Verlag: Berlin Heidelberg, Germany
    • Marcone, G. L.; Marinelli, F. Glycopeptides: An old but up to date successful antibiotic class. In Antimicrobials; Marinelli, F., Genilloud, O., Eds.; Springer Verlag: Berlin Heidelberg, Germany, 2014.
    • (2014) Antimicrobials
    • Marcone, G.L.1    Marinelli, F.2
  • 6
  • 8
    • 84925633044 scopus 로고    scopus 로고
    • Opportunities for synthetic biology in antibiotics: Expanding glycopeptide chemical diversity
    • Thaker, M. N.; Wright, G. D. Opportunities for synthetic biology in antibiotics: Expanding glycopeptide chemical diversity. ACS Synth. Biol. 2012, doi: 10. 1021/sb300092n.
    • (2012) ACS Synth. Biol
    • Thaker, M.N.1    Wright, G.D.2
  • 10
    • 56249128990 scopus 로고    scopus 로고
    • Cloning and characterization of new glycopeptide gene clusters found in an environmental DNA megalibrary
    • Banik, J. J.; Brady, S. F. Cloning and characterization of new glycopeptide gene clusters found in an environmental DNA megalibrary. Proc. Natl. Acad. Sci. USA 2008, 105, 17273-17277.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17273-17277
    • Banik, J.J.1    Brady, S.F.2
  • 11
    • 77957774503 scopus 로고    scopus 로고
    • Recent application of metagenomic approaches toward the discovery of antimicrobials and other bioactive small molecules
    • Banik, J. J.; Brady, S. F. Recent application of metagenomic approaches toward the discovery of antimicrobials and other bioactive small molecules. Curr. Opin. Microbiol. 2010, 13, 603-609.
    • (2010) Curr. Opin. Microbiol , vol.13 , pp. 603-609
    • Banik, J.J.1    Brady, S.F.2
  • 12
    • 84880370987 scopus 로고    scopus 로고
    • Mapping gene clusters within arrayed metagenomic libraries to expand the structural diversity of biomedically relevant natural products
    • Owen, J. G.; Reddy, B. V.; Ternei, M. A.; Charlop-Powers, Z.; Calle, P. Y.; Kim, J. H.; Brady, S. F. Mapping gene clusters within arrayed metagenomic libraries to expand the structural diversity of biomedically relevant natural products. Proc. Natl. Acad. Sci. USA 2013, 110, 11797-11802.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 11797-11802
    • Owen, J.G.1    Reddy, B.V.2    Ternei, M.A.3    Charlop-Powers, Z.4    Calle, P.Y.5    Kim, J.H.6    Brady, S.F.7
  • 13
    • 0026019412 scopus 로고
    • Factors affecting the normal and branched-chain acyl moieties of teicoplanin components produced by Actinoplanes teichomyceticus
    • Borghi, A.; Edwards, D.; Zerilli, L. F.; Lancini, G. C. Factors affecting the normal and branched-chain acyl moieties of teicoplanin components produced by Actinoplanes teichomyceticus. J. Gen. Microbiol. 1991, 137, 587-592.
    • (1991) J. Gen. Microbiol , vol.137 , pp. 587-592
    • Borghi, A.1    Edwards, D.2    Zerilli, L.F.3    Lancini, G.C.4
  • 15
    • 0033485286 scopus 로고    scopus 로고
    • Binding of glycopeptide antibiotics to a model of a vancomycin-resistant bacterium
    • Cooper, M. A.; Williams, D. H. Binding of glycopeptide antibiotics to a model of a vancomycin-resistant bacterium. Chem. Biol. 1999, 6, 891-899.
    • (1999) Chem. Biol , vol.6 , pp. 891-899
    • Cooper, M.A.1    Williams, D.H.2
  • 16
    • 33747605341 scopus 로고    scopus 로고
    • Glycopeptides and glycodepsipeptides in clinical development: A comparative review of their antibacterial spectrum, pharmacokinetics and clinical efficacy
    • Van Bambeke, F. Glycopeptides and glycodepsipeptides in clinical development: A comparative review of their antibacterial spectrum, pharmacokinetics and clinical efficacy. Curr. Opin. Investig. Drugs 2006, 7, 740-749.
    • (2006) Curr. Opin. Investig. Drugs , vol.7 , pp. 740-749
    • Van Bambeke, F.1
  • 17
    • 79960002430 scopus 로고    scopus 로고
    • Glycopeptide antibiotics and their novel semi-synthetic derivatives
    • Jeya, M.; Moon, H. J.; Lee, K. M.; Kim, I. W.; Lee, J. K. Glycopeptide antibiotics and their novel semi-synthetic derivatives. Curr. Pharm. Biotechnol. 2011, 12, 1194-1204.
    • (2011) Curr. Pharm. Biotechnol , vol.12 , pp. 1194-1204
    • Jeya, M.1    Moon, H.J.2    Lee, K.M.3    Kim, I.W.4    Lee, J.K.5
  • 18
    • 0020028616 scopus 로고
    • Comparison of the in vitro activities of teichomycin A2 and vancomycin against staphylococci and enterococci
    • Cynamon, M. H.; Granato, P. A. Comparison of the in vitro activities of teichomycin A2 and vancomycin against staphylococci and enterococci. Antimicrob. Agents Chemother. 1982, 21, 504-505.
    • (1982) Antimicrob. Agents Chemother , vol.21 , pp. 504-505
    • Cynamon, M.H.1    Granato, P.A.2
  • 19
    • 0027936628 scopus 로고
    • Glycopeptide antibiotic activity and the possible role of dimerization: A model for biological signaling
    • Mackay, J. P.; Gerhard, U.; Beauregard, D. A.; Westwell, M. S.; Searle, M. S.; Williams, D. H. Glycopeptide antibiotic activity and the possible role of dimerization: A model for biological signaling. J. Am. Chem. Soc. 1994, 116, 4581-4590.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 4581-4590
    • Mackay, J.P.1    Gerhard, U.2    Beauregard, D.A.3    Westwell, M.S.4    Searle, M.S.5    Williams, D.H.6
  • 20
    • 84855919835 scopus 로고    scopus 로고
    • Recent advances in the synthesis of new glycopeptide antibiotics
    • Ashford, P. A.; Bew, S. P. Recent advances in the synthesis of new glycopeptide antibiotics. Chem. Soc. Rev. 2012, 41, 957-978.
    • (2012) Chem. Soc. Rev , vol.41 , pp. 957-978
    • Ashford, P.A.1    Bew, S.P.2
  • 22
    • 20044363986 scopus 로고    scopus 로고
    • Telavancin, a multifunctional lipoglycopeptide, disrupts both cell wall synthesis and cell membrane integrity in methicillin-resistant Staphylococcus aureus
    • Higgins, D. L.; Chang, R.; Debabov, D. V.; Leung, J.; Wu, T.; Krause, K. M.; Sandvik, E.; Hubbard, J. M.; Kaniga, K.; Schmidt, D. E.; et al. Telavancin, a multifunctional lipoglycopeptide, disrupts both cell wall synthesis and cell membrane integrity in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 2005, 49, 1127-1134.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 1127-1134
    • Higgins, D.L.1    Chang, R.2    Debabov, D.V.3    Leung, J.4    Wu, T.5    Krause, K.M.6    Sandvik, E.7    Hubbard, J.M.8    Kaniga, K.9    Schmidt, D.E.10
  • 23
    • 84893821116 scopus 로고    scopus 로고
    • (accessed on 23 October 2014)
    • U. S. Food and Drug Administration. Available online: http://www. fda. gov/(accessed on 23 October 2014).
    • U.S. Food and Drug Administration
  • 24
    • 77957679579 scopus 로고    scopus 로고
    • Oritavancin: A novel lipoglycopeptide active against gram-positive pathogens including multiresistant strains
    • Bouza, E.; Burillo, A. Oritavancin: A novel lipoglycopeptide active against gram-positive pathogens including multiresistant strains. Int. J. Antimicrob. Agents 2010, 36, 401-407.
    • (2010) Int. J. Antimicrob. Agents , vol.36 , pp. 401-407
    • Bouza, E.1    Burillo, A.2
  • 25
    • 78649671049 scopus 로고    scopus 로고
    • Oritavancin disrupts membrane integrity of Staphylococcus aureus and vancomycin-resistant enterococci to effect rapid bacterial killing
    • Belley, A.; McKay, G. A.; Arhin, F. F.; Sarmiento, I.; Beaulieu, S.; Fadhil, I.; Parr, T. R.; Moeck, G. Oritavancin disrupts membrane integrity of Staphylococcus aureus and vancomycin-resistant enterococci to effect rapid bacterial killing. Antimicrob. Agents Chemother. 2010, 54, 5369-5371.
    • (2010) Antimicrob. Agents Chemother , vol.54 , pp. 5369-5371
    • Belley, A.1    McKay, G.A.2    Arhin, F.F.3    Sarmiento, I.4    Beaulieu, S.5    Fadhil, I.6    Parr, T.R.7    Moeck, G.8
  • 28
    • 15844426950 scopus 로고    scopus 로고
    • Origin, structure, and activity in vitro and in vivo of dalbavancin
    • Malabarba, A.; Goldstein, B. P. Origin, structure, and activity in vitro and in vivo of dalbavancin. J. Antimicrob. Chemother. 2005, 55, 15-20.
    • (2005) J. Antimicrob. Chemother , vol.55 , pp. 15-20
    • Malabarba, A.1    Goldstein, B.P.2
  • 32
    • 84858398621 scopus 로고    scopus 로고
    • The rise of the enterococcus: Beyond vancomycin resistance
    • Arias, C. A.; Murray, B. E. The rise of the enterococcus: Beyond vancomycin resistance. Nat. Rev. Microbiol. 2012, 10, 266-278.
    • (2012) Nat. Rev. Microbiol , vol.10 , pp. 266-278
    • Arias, C.A.1    Murray, B.E.2
  • 33
    • 29244441170 scopus 로고    scopus 로고
    • Vancomycin resistance in gram-positive cocci
    • Courvalin, P. Vancomycin resistance in gram-positive cocci. Clin. Infect. Dis. 2006, 42, S25-S34.
    • (2006) Clin. Infect. Dis , vol.42 , pp. S25-S34
    • Courvalin, P.1
  • 34
    • 0026355435 scopus 로고
    • Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: Biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA
    • Bugg, T. D.; Wright, G. D.; Dutka-Malen, S.; Arthur, M.; Courvalin, P.; Walsh, C. T. Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: Biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. Biochemistry 1991, 30, 10408-10415.
    • (1991) Biochemistry , vol.30 , pp. 10408-10415
    • Bugg, T.D.1    Wright, G.D.2    Dutka-Malen, S.3    Arthur, M.4    Courvalin, P.5    Walsh, C.T.6
  • 35
    • 0345192358 scopus 로고    scopus 로고
    • Determinants for differential effects on D-ala-D-lactate vs. D-ala-D-ala formation by the VanA ligase from vancomycin-resistant enterococci
    • Lessard, I. A.; Healy, V. L.; Park, I. S.; Walsh, C. T. Determinants for differential effects on D-ala-D-lactate vs. D-ala-D-ala formation by the VanA ligase from vancomycin-resistant enterococci. Biochemistry 1999, 38, 14006-14022.
    • (1999) Biochemistry , vol.38 , pp. 14006-14022
    • Lessard, I.A.1    Healy, V.L.2    Park, I.S.3    Walsh, C.T.4
  • 37
    • 0026506576 scopus 로고
    • Evidence for in vivo incorporation of D-lactate into peptidoglycan precursors of vancomycin-resistant enterococci
    • Arthur, M.; Molinas, C.; Bugg, T. D.; Wright, G. D.; Walsh, C. T.; Courvalin, P. Evidence for in vivo incorporation of D-lactate into peptidoglycan precursors of vancomycin-resistant enterococci. Antimicrob. Agents Chemother. 1992, 36, 867-869.
    • (1992) Antimicrob. Agents Chemother , vol.36 , pp. 867-869
    • Arthur, M.1    Molinas, C.2    Bugg, T.D.3    Wright, G.D.4    Walsh, C.T.5    Courvalin, P.6
  • 38
    • 0028076784 scopus 로고
    • Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine
    • Reynolds, P. E.; Depardieu, F.; Dutka-Malen, S.; Arthur, M.; Courvalin, P. Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine. Mol. Microbiol. 1994, 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
  • 39
    • 0028959077 scopus 로고
    • Overexpression, purification, and characterization of VanX, a D, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147
    • Wu, Z.; Wright, G. D.; Walsh, C. T. Overexpression, purification, and characterization of VanX, a D, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147. Biochemistry 1995, 34, 2455-2463.
    • (1995) Biochemistry , vol.34 , pp. 2455-2463
    • Wu, Z.1    Wright, G.D.2    Walsh, C.T.3
  • 40
    • 0028870094 scopus 로고
    • The vanZ gene of Tn1546 from Enterococcus faecium BM4147 confers resistance to teicoplanin
    • Arthur, M.; Depardieu, F.; Molinas, C.; Reynolds, P.; Courvalin, P. The vanZ gene of Tn1546 from Enterococcus faecium BM4147 confers resistance to teicoplanin. Gene 1995, 154, 87-92.
    • (1995) Gene , vol.154 , pp. 87-92
    • Arthur, M.1    Depardieu, F.2    Molinas, C.3    Reynolds, P.4    Courvalin, P.5
  • 41
    • 0031735098 scopus 로고    scopus 로고
    • Requirement of the VanY and VanX D, D-peptidases for glycopeptide resistance in enterococci
    • Arthur, M.; Depardieu, F.; Cabanié, L.; Reynolds, P.; Courvalin, P. Requirement of the VanY and VanX D, D-peptidases for glycopeptide resistance in enterococci. Mol. Microbiol. 1998, 30, 819-830.
    • (1998) Mol. Microbiol , vol.30 , pp. 819-830
    • Arthur, M.1    Depardieu, F.2    Cabanié, L.3    Reynolds, P.4    Courvalin, P.5
  • 42
    • 0031026581 scopus 로고    scopus 로고
    • The VanS sensor negatively controls VanR-mediated transcriptional activation of glycopeptide resistance genes of Tn1546 and related elements in the absence of induction
    • Arthur, M.; Depardieu, F.; Gerbaud, G.; Galimand, M.; Leclercq, R.; Courvalin, P. The VanS sensor negatively controls VanR-mediated transcriptional activation of glycopeptide resistance genes of Tn1546 and related elements in the absence of induction. J. Bacteriol. 1997, 179, 97-106.
    • (1997) J. Bacteriol , vol.179 , pp. 97-106
    • Arthur, M.1    Depardieu, F.2    Gerbaud, G.3    Galimand, M.4    Leclercq, R.5    Courvalin, P.6
  • 43
    • 0032870104 scopus 로고    scopus 로고
    • Regulated interactions between partner and non-partner sensors and response regulators that control glycopeptide resistance gene expression in enterococci
    • Arthur, M.; Depardieu, F.; Courvalin, P. Regulated interactions between partner and non-partner sensors and response regulators that control glycopeptide resistance gene expression in enterococci. Microbiology 1999, 145, 1849-1858.
    • (1999) Microbiology , vol.145 , pp. 1849-1858
    • Arthur, M.1    Depardieu, F.2    Courvalin, P.3
  • 44
    • 0035145028 scopus 로고    scopus 로고
    • Regulation of VanA-and VanB-type glycopeptide resistance in enterococci
    • Arthur, M.; Quintiliani, R. Regulation of VanA-and VanB-type glycopeptide resistance in enterococci. Antimicrob. Agents Chemother. 2001, 45, 375-381.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 375-381
    • Arthur, M.1    Quintiliani, R.2
  • 45
    • 0027164115 scopus 로고
    • Purification and characterization of VanR and the cytosolic domain of VanS: A two-component regulatory system required for vancomycin resistance in Enterococcus faecium BM4147
    • Wright, G. D.; Holman, T. R.; Walsh, C. T. Purification and characterization of VanR and the cytosolic domain of VanS: A two-component regulatory system required for vancomycin resistance in Enterococcus faecium BM4147. Biochemistry 1993, 32, 5057-5063.
    • (1993) Biochemistry , vol.32 , pp. 5057-5063
    • Wright, G.D.1    Holman, T.R.2    Walsh, C.T.3
  • 46
    • 0034087501 scopus 로고    scopus 로고
    • Vancomycin resistance in enterococci: Reprogramming of the D-ala-D-ala ligases in bacterial peptidoglycan biosynthesis
    • Healy, V. L.; Lessard, I. A.; Roper, D. I.; Knox, J. R.; Walsh, C. T. Vancomycin resistance in enterococci: Reprogramming of the D-ala-D-ala ligases in bacterial peptidoglycan biosynthesis. Chem. Biol. 2000, 7, R109-R119.
    • (2000) Chem. Biol , vol.7 , pp. R109-R119
    • Healy, V.L.1    Lessard, I.A.2    Roper, D.I.3    Knox, J.R.4    Walsh, C.T.5
  • 50
    • 0028605482 scopus 로고
    • Association constants for the binding of vancomycin and teicoplanin to N-acetyl-D-alanyl-D-alanine and N-acetyl-D-alanyl-D-serine
    • Billot-Klein, D.; Blanot, D.; Gutmann, L.; van Heijenoort, J. Association constants for the binding of vancomycin and teicoplanin to N-acetyl-D-alanyl-D-alanine and N-acetyl-D-alanyl-D-serine. Biochem. J. 1994, 304, 1021-1022.
    • (1994) Biochem. J , vol.304 , pp. 1021-1022
    • Billot-Klein, D.1    Blanot, D.2    Gutmann, L.3    van Heijenoort, J.4
  • 51
    • 11244307455 scopus 로고    scopus 로고
    • Vancomycin resistance in enterococci due to synthesis of precursors terminating in D-alanyl-D-serine
    • Reynolds, P. E.; Courvalin, P. Vancomycin resistance in enterococci due to synthesis of precursors terminating in D-alanyl-D-serine. Antimicrob. Agents Chemother. 2005, 49, 21-25.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 21-25
    • Reynolds, P.E.1    Courvalin, P.2
  • 52
    • 0030796911 scopus 로고    scopus 로고
    • Mutations leading to increased levels of resistance to glycopeptide antibiotics in VanB-type enterococci
    • Baptista, M.; Depardieu, F.; Reynolds, P.; Courvalin, P.; Arthur, M. Mutations leading to increased levels of resistance to glycopeptide antibiotics in VanB-type enterococci. Mol. Microbiol. 1997, 25, 93-105.
    • (1997) Mol. Microbiol , vol.25 , pp. 93-105
    • Baptista, M.1    Depardieu, F.2    Reynolds, P.3    Courvalin, P.4    Arthur, M.5
  • 54
    • 46249111916 scopus 로고    scopus 로고
    • Molecular characterization of Enterococcus faecalis N06-0364 with low-level vancomycin resistance harboring a novel D-ala-D-ser gene cluster, VanL
    • Boyd, D. A.; Willey, B. M.; Fawcett, D.; Gillani, N.; Mulvey, M. R. Molecular characterization of Enterococcus faecalis N06-0364 with low-level vancomycin resistance harboring a novel D-ala-D-ser gene cluster, VanL. Antimicrob. Agents Chemother. 2008, 52, 2667-2672.
    • (2008) Antimicrob. Agents Chemother , vol.52 , pp. 2667-2672
    • Boyd, D.A.1    Willey, B.M.2    Fawcett, D.3    Gillani, N.4    Mulvey, M.R.5
  • 57
    • 84869231875 scopus 로고    scopus 로고
    • Identification of VanN-type vancomycin resistance in an Enterococcus faecium isolate from chicken meat in Japan
    • Nomura, T.; Tanimoto, K.; Shibayama, K.; Arakawa, Y.; Fujimoto, S.; Ike, Y.; Tomita, H. Identification of VanN-type vancomycin resistance in an Enterococcus faecium isolate from chicken meat in Japan. Antimicrob. Agents Chemother. 2012, 56, 6389-6392.
    • (2012) Antimicrob. Agents Chemother , vol.56 , pp. 6389-6392
    • Nomura, T.1    Tanimoto, K.2    Shibayama, K.3    Arakawa, Y.4    Fujimoto, S.5    Ike, Y.6    Tomita, H.7
  • 58
    • 0036674819 scopus 로고    scopus 로고
    • First case of VRSA identified in Michigan
    • Bartley, J. First case of VRSA identified in Michigan. Infect. Control Hosp. Epidemiol. 2002, 23, 480.
    • (2002) Infect. Control Hosp. Epidemiol , vol.23 , pp. 480
    • Bartley, J.1
  • 62
    • 67049086956 scopus 로고    scopus 로고
    • Fitness cost of VanA-type vancomycin resistance in methicillin-resistant Staphylococcus aureus
    • Foucault, M. L.; Courvalin, P.; Grillot-Courvalin, C. Fitness cost of VanA-type vancomycin resistance in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 2009, 53, 2354-2359.
    • (2009) Antimicrob. Agents Chemother , vol.53 , pp. 2354-2359
    • Foucault, M.L.1    Courvalin, P.2    Grillot-Courvalin, C.3
  • 63
    • 70350292185 scopus 로고    scopus 로고
    • VanA-type vancomycin-resistant Staphylococcus aureus
    • Périchon, B.; Courvalin, P. VanA-type vancomycin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 2009, 53, 4580-4587.
    • (2009) Antimicrob. Agents Chemother , vol.53 , pp. 4580-4587
    • Périchon, B.1    Courvalin, P.2
  • 64
    • 64249124472 scopus 로고    scopus 로고
    • Chapter 2. From microbial products to novel drugs that target a multitude of disease indications
    • Marinelli, F. Chapter 2. From microbial products to novel drugs that target a multitude of disease indications. Methods Enzymol. 2009, 458, 29-58.
    • (2009) Methods Enzymol , vol.458 , pp. 29-58
    • Marinelli, F.1
  • 65
    • 85012819682 scopus 로고    scopus 로고
    • Small molecules, microbial secondary metabolites
    • 2nd ed.; Moo-Young, M., Ed.; Elsevier: Amsterdam, The Netherlands
    • Marinelli, F.; Marcone, G. Small molecules, microbial secondary metabolites. In Comprehensive Biotechnology, 2nd ed.; Moo-Young, M., Ed.; Elsevier: Amsterdam, The Netherlands, 2011; Volume 3, pp. 285-297.
    • (2011) Comprehensive Biotechnology , vol.3 , pp. 285-297
    • Marinelli, F.1    Marcone, G.2
  • 66
    • 77954689755 scopus 로고    scopus 로고
    • Avoidance of suicide in antibiotic-producing microbes
    • Cundliffe, E.; Demain, A. L. Avoidance of suicide in antibiotic-producing microbes. J. Ind. Microbiol. Biotechnol. 2010, 37, 643-672.
    • (2010) J. Ind. Microbiol. Biotechnol , vol.37 , pp. 643-672
    • Cundliffe, E.1    Demain, A.L.2
  • 67
    • 0030911603 scopus 로고    scopus 로고
    • D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are highly homologous to the enterococcal vancomycin-resistance ligases VanA and VanB
    • Marshall, C. G.; Broadhead, G.; Leskiw, B. K.; Wright, G. D. D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are highly homologous to the enterococcal vancomycin-resistance ligases VanA and VanB. Proc. Natl. Acad. Sci. USA 1997, 94, 6480-6483.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6480-6483
    • Marshall, C.G.1    Broadhead, G.2    Leskiw, B.K.3    Wright, G.D.4
  • 68
    • 0031663280 scopus 로고    scopus 로고
    • Glycopeptide antibiotic resistance genes in glycopeptide-producing organisms
    • Marshall, C. G.; Lessard, I. A.; Park, I.; Wright, G. D. Glycopeptide antibiotic resistance genes in glycopeptide-producing organisms. Antimicrob. Agents Chemother. 1998, 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
  • 70
    • 1142306159 scopus 로고    scopus 로고
    • Biosynthetic gene cluster of the glycopeptide antibiotic teicoplanin: Characterization of two glycosyltransferases and the key acyltransferase
    • Li, T. L.; Huang, F.; Haydock, S. F.; Mironenko, T.; Leadlay, P. F.; Spencer, J. B. Biosynthetic gene cluster of the glycopeptide antibiotic teicoplanin: Characterization of two glycosyltransferases and the key acyltransferase. Chem. Biol. 2004, 11, 107-119.
    • (2004) Chem. Biol , vol.11 , pp. 107-119
    • Li, T.L.1    Huang, F.2    Haydock, S.F.3    Mironenko, T.4    Leadlay, P.F.5    Spencer, J.B.6
  • 73
    • 0035831448 scopus 로고    scopus 로고
    • Femabx family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets
    • Hegde, S. S.; Shrader, T. E. Femabx family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets. J. Biol. Chem. 2001, 276, 6998-7003.
    • (2001) J. Biol. Chem , vol.276 , pp. 6998-7003
    • Hegde, S.S.1    Shrader, T.E.2
  • 74
    • 0035873560 scopus 로고    scopus 로고
    • Inhibition of sporulation, glycopeptide antibiotic production and resistance in Streptomyces toyocaensis NRRL15009 by protein kinase inhibitors
    • Neu, J. M.; Wright, G. D. Inhibition of sporulation, glycopeptide antibiotic production and resistance in Streptomyces toyocaensis NRRL15009 by protein kinase inhibitors. FEMS Microbiol. Lett. 2001, 199, 15-20.
    • (2001) FEMS Microbiol. Lett , vol.199 , pp. 15-20
    • Neu, J.M.1    Wright, G.D.2
  • 75
    • 7044274648 scopus 로고    scopus 로고
    • Glycopeptide resistance determinants from the teicoplanin producer Actinoplanes teichomyceticus
    • Serina, S.; Radice, F.; Maffioli, S.; Donadio, S.; Sosio, M. Glycopeptide resistance determinants from the teicoplanin producer Actinoplanes teichomyceticus. FEMS Microbiol. Lett. 2004, 240, 69-74.
    • (2004) FEMS Microbiol. Lett , vol.240 , pp. 69-74
    • Serina, S.1    Radice, F.2    Maffioli, S.3    Donadio, S.4    Sosio, M.5
  • 76
    • 34247170305 scopus 로고    scopus 로고
    • Resistance to glycopeptide antibiotics in the teicoplanin producer is mediated by van gene homologue expression directing the synthesis of a modified cell wall peptidoglycan
    • Beltrametti, F.; Consolandi, A.; Carrano, L.; Bagatin, F.; Rossi, R.; Leoni, L.; Zennaro, E.; Selva, E.; Marinelli, F. Resistance to glycopeptide antibiotics in the teicoplanin producer is mediated by van gene homologue expression directing the synthesis of a modified cell wall peptidoglycan. Antimicrob. Agents Chemother. 2007, 51, 1135-1141.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 1135-1141
    • Beltrametti, F.1    Consolandi, A.2    Carrano, L.3    Bagatin, F.4    Rossi, R.5    Leoni, L.6    Zennaro, E.7    Selva, E.8    Marinelli, F.9
  • 77
    • 33645050677 scopus 로고    scopus 로고
    • The vancomycin resistance VanRS two-component signal transduction system of Streptomyces coelicolor
    • Hutchings, M. I.; Hong, H. J.; Buttner, M. J. The vancomycin resistance VanRS two-component signal transduction system of Streptomyces coelicolor. Mol. Microbiol. 2006, 59, 923-935.
    • (2006) Mol. Microbiol , vol.59 , pp. 923-935
    • Hutchings, M.I.1    Hong, H.J.2    Buttner, M.J.3
  • 78
    • 3142743426 scopus 로고    scopus 로고
    • Characterization of an inducible vancomycin resistance system in Streptomyces coelicolor reveals a novel gene (vanK) required for drug resistance
    • Hong, H. J.; Hutchings, M. I.; Neu, J. M.; Wright, G. D.; Paget, M. S.; Buttner, M. J. Characterization of an inducible vancomycin resistance system in Streptomyces coelicolor reveals a novel gene (vanK) required for drug resistance. Mol. Microbiol. 2004, 52, 1107-1121.
    • (2004) Mol. Microbiol , vol.52 , pp. 1107-1121
    • Hong, H.J.1    Hutchings, M.I.2    Neu, J.M.3    Wright, G.D.4    Paget, M.S.5    Buttner, M.J.6
  • 80
    • 84882312630 scopus 로고    scopus 로고
    • In vivo studies suggest that induction of VanS-dependent vancomycin resistance requires binding of the drug to D-Ala-D-Ala termini in the peptidoglycan cell wall
    • Kwun, M. J.; Novotna, G.; Hesketh, A. R.; Hill, L.; Hong, H. J. In vivo studies suggest that induction of VanS-dependent vancomycin resistance requires binding of the drug to D-Ala-D-Ala termini in the peptidoglycan cell wall. Antimicrob. Agents Chemother. 2013, 57, 4470-4480.
    • (2013) Antimicrob. Agents Chemother , vol.57 , pp. 4470-4480
    • Kwun, M.J.1    Novotna, G.2    Hesketh, A.R.3    Hill, L.4    Hong, H.J.5
  • 82
    • 84906084022 scopus 로고    scopus 로고
    • The relationship between glycopeptide production and resistance in the actinomycete Nonomuraea sp. ATCC 39727
    • Marcone, G. L.; Binda, E.; Carrano, L.; Bibb, M.; Marinelli, F. The relationship between glycopeptide production and resistance in the actinomycete Nonomuraea sp. ATCC 39727. Antimicrob. Agents Chemother. 2014, 58, doi: 10. 1128/AAC. 02626-14.
    • (2014) Antimicrob. Agents Chemother , vol.58
    • Marcone, G.L.1    Binda, E.2    Carrano, L.3    Bibb, M.4    Marinelli, F.5
  • 83
    • 16844374518 scopus 로고    scopus 로고
    • The role of the novel Fem protein VanK in vancomycin resistance in Streptomyces coelicolor
    • Hong, H. J.; Hutchings, M. I.; Hill, L. M.; Buttner, M. J. The role of the novel Fem protein VanK in vancomycin resistance in Streptomyces coelicolor. J. Biol. Chem. 2005, 280, 13055-13061.
    • (2005) J. Biol. Chem , vol.280 , pp. 13055-13061
    • Hong, H.J.1    Hutchings, M.I.2    Hill, L.M.3    Buttner, M.J.4
  • 85
    • 0038167479 scopus 로고    scopus 로고
    • The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by Nonomuraea species
    • Sosio, M.; Stinchi, S.; Beltrametti, F.; Lazzarini, A.; Donadio, S. The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by Nonomuraea species. Chem. Biol. 2003, 10, 541-549.
    • (2003) Chem. Biol , vol.10 , pp. 541-549
    • Sosio, M.1    Stinchi, S.2    Beltrametti, F.3    Lazzarini, A.4    Donadio, S.5
  • 87
    • 84865248615 scopus 로고    scopus 로고
    • Characterization of VanY(n), a novel D, D-peptidase/D, D-carboxypeptidase involved in glycopeptide antibiotic resistance in Nonomuraea sp. ATCC 39727
    • Binda, E.; Marcone, G. L.; Pollegioni, L.; Marinelli, F. Characterization of VanY(n), a novel D, D-peptidase/D, D-carboxypeptidase involved in glycopeptide antibiotic resistance in Nonomuraea sp. ATCC 39727. FEBS J. 2012, 279, 3203-3213.
    • (2012) FEBS J , vol.279 , pp. 3203-3213
    • Binda, E.1    Marcone, G.L.2    Pollegioni, L.3    Marinelli, F.4
  • 88
    • 84874931897 scopus 로고    scopus 로고
    • Streptomyces spp. as efficient expression system for a D, D-peptidase/D, D-carboxypeptidase involved in glycopeptide antibiotic resistance
    • Binda, E.; Marcone, G. L.; Berini, F.; Pollegioni, L.; Marinelli, F. Streptomyces spp. as efficient expression system for a D, D-peptidase/D, D-carboxypeptidase involved in glycopeptide antibiotic resistance. BMC Biotechnol. 2013, 13, e24.
    • (2013) BMC Biotechnol , vol.13
    • Binda, E.1    Marcone, G.L.2    Berini, F.3    Pollegioni, L.4    Marinelli, F.5
  • 89
    • 0026742240 scopus 로고
    • Characterization of VanY, a D, D-carboxypeptidase from vancomycin-resistant Enterococcus faecium BM4147
    • Wright, G. D.; Molinas, C.; Arthur, M.; Courvalin, P.; Walsh, C. T. Characterization of VanY, a D, D-carboxypeptidase from vancomycin-resistant Enterococcus faecium BM4147. Antimicrob. Agents Chemother. 1992, 36, 1514-1518.
    • (1992) Antimicrob. Agents Chemother , vol.36 , pp. 1514-1518
    • Wright, G.D.1    Molinas, C.2    Arthur, M.3    Courvalin, P.4    Walsh, C.T.5
  • 90
    • 0032585993 scopus 로고    scopus 로고
    • Gene vanxyc encodes D, D-dipeptidase (VanX) and D, D-carboxypeptidase (VanY) activities in vancomycin-resistant Enterococcus gallinarum BM4174
    • Reynolds, P. E.; Arias, C. A.; Courvalin, P. Gene vanxyc encodes D, D-dipeptidase (VanX) and D, D-carboxypeptidase (VanY) activities in vancomycin-resistant Enterococcus gallinarum BM4174. Mol. Microbiol. 1999, 34, 341-349.
    • (1999) Mol. Microbiol , vol.34 , pp. 341-349
    • Reynolds, P.E.1    Arias, C.A.2    Courvalin, P.3
  • 91
    • 39149095622 scopus 로고    scopus 로고
    • Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in gram-positive bacteria
    • Mainardi, J. L.; Villet, R.; Bugg, T. D.; Mayer, C.; Arthur, M. Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in gram-positive bacteria. FEMS Microbiol. Rev. 2008, 32, 386-408.
    • (2008) FEMS Microbiol. Rev , vol.32 , pp. 386-408
    • Mainardi, J.L.1    Villet, R.2    Bugg, T.D.3    Mayer, C.4    Arthur, M.5
  • 93
    • 77950292804 scopus 로고    scopus 로고
    • Protoplast preparation and reversion to the normal filamentous growth in antibiotic-producing uncommon actinomycetes
    • Marcone, G. L.; Carrano, L.; Marinelli, F.; Beltrametti, F. Protoplast preparation and reversion to the normal filamentous growth in antibiotic-producing uncommon actinomycetes. J. Antibiot. (Tokyo) 2010, 63, 83-88.
    • (2010) J. Antibiot. (Tokyo) , vol.63 , pp. 83-88
    • Marcone, G.L.1    Carrano, L.2    Marinelli, F.3    Beltrametti, F.4
  • 95
    • 84997831744 scopus 로고    scopus 로고
    • Genome sequence of the vancomycin-producing Amycolatopsis orientalis subsp. Orientalis strain KCTC 9412T
    • Jeong, H.; Sim, Y. M.; Kim, H. J.; Lee, D. W.; Lim, S. K.; Lee, S. J. Genome sequence of the vancomycin-producing Amycolatopsis orientalis subsp. Orientalis strain KCTC 9412T. Genome Announc. 2013, 1, doi: 10. 1128/genomeA. 00408-13.
    • (2013) Genome Announc , vol.1
    • Jeong, H.1    Sim, Y.M.2    Kim, H.J.3    Lee, D.W.4    Lim, S.K.5    Lee, S.J.6


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