메뉴 건너뛰기




Volumn 57, Issue 6, 2013, Pages 2801-2808

Heteroresistance to fosfomycin is predominant in streptococcus pneumoniae and depends on the murA1 gene

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FOSFOMYCIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE ENOLPYRUVYLTRANSFERASE;

EID: 84877857787     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00223-13     Document Type: Article
Times cited : (32)

References (50)
  • 1
    • 0032815561 scopus 로고    scopus 로고
    • Lactam resistance in Streptococcus pneumoniae: Penicillin-binding proteins and nonpenicillin-binding proteins
    • Hakenbeck R, Grebe T, Zahner D, Stock JB. 1999.-Lactam resistance in Streptococcus pneumoniae: Penicillin-binding proteins and nonpenicillin-binding proteins. Mol. Microbiol. 33:673-678.
    • (1999) Mol. Microbiol. , vol.33 , pp. 673-678
    • Hakenbeck, R.1    Grebe, T.2    Zahner, D.3    Stock, J.B.4
  • 3
    • 62949215691 scopus 로고    scopus 로고
    • An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: Mutational analysis of Thr338
    • Zerfass I, Hakenbeck R, Denapaite D. 2009. An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: Mutational analysis of Thr338. Antimicrob. Agents Chemother. 53:1107-1115.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1107-1115
    • Zerfass, I.1    Hakenbeck, R.2    Denapaite, D.3
  • 4
    • 35348861380 scopus 로고    scopus 로고
    • Heteroresistance to penicillin in Streptococcus pneumoniae
    • Morand B, Mühlemann K. 2007. Heteroresistance to penicillin in Streptococcus pneumoniae. Proc. Natl. Acad. Sci. U. S. A. 104:14098-14103.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 14098-14103
    • Morand, B.1    Mühlemann, K.2
  • 7
    • 84863155296 scopus 로고    scopus 로고
    • Heteroresistance to cephalosporins and penicillins in Acinetobacter baumannii
    • Hung KH, Wang MC, Huang AH, Yan JJ, Wu JJ. 2012. Heteroresistance to cephalosporins and penicillins in Acinetobacter baumannii. J. Clin. Microbiol. 50:721-726.
    • (2012) J. Clin. Microbiol. , vol.50 , pp. 721-726
    • Hung, K.H.1    Wang, M.C.2    Huang, A.H.3    Yan, J.J.4    Wu, J.J.5
  • 10
    • 0028077273 scopus 로고
    • Reassessment of the number of auxiliary genes essential for expression of high-level methicillin resistance in Staphylococcus aureus
    • de Lencastre H, Tomasz A. 1994. Reassessment of the number of auxiliary genes essential for expression of high-level methicillin resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 38:2590-2598.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2590-2598
    • De Lencastre, H.1    Tomasz, A.2
  • 11
    • 62849120772 scopus 로고    scopus 로고
    • A novel DNA-binding protein modulating methicillin resistance in Staphylococcus aureus
    • doi:10.1186/1471-2180-9-15
    • Ender M, Berger-Bächi B, McCallum N. 2009. A novel DNA-binding protein modulating methicillin resistance in Staphylococcus aureus. BMC Microbiol. 9:15. doi:10.1186/1471-2180-9-15.
    • (2009) BMC Microbiol. , vol.9 , pp. 15
    • Ender, M.1    Berger-Bächi, B.2    McCallum, N.3
  • 12
    • 0036136723 scopus 로고    scopus 로고
    • Conversion of oxacillin-resistant staphylococci from heterotypic to homotypic resistance expression
    • Finan JE, Rosato AE, Dickinson TM, Ko D, Archer GL. 2002. Conversion of oxacillin-resistant staphylococci from heterotypic to homotypic resistance expression. Antimicrob. Agents Chemother. 46:24-30.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 24-30
    • Finan, J.E.1    Rosato, A.E.2    Dickinson, T.M.3    Ko, D.4    Archer, G.L.5
  • 13
    • 0022651448 scopus 로고
    • Expression of methicillin resistance in heterogeneous strains of Staphylococcus aureus
    • Hartman BJ, Tomasz A. 1986. Expression of methicillin resistance in heterogeneous strains of Staphylococcus aureus. Antimicrob. Agents Chemother. 29:85-92.
    • (1986) Antimicrob. Agents Chemother. , vol.29 , pp. 85-92
    • Hartman, B.J.1    Tomasz, A.2
  • 14
    • 0024586553 scopus 로고
    • Involvement of multiple genetic determinants in high-level methicillin resistance in Staphylococcus aureus
    • Murakami K, Tomasz A. 1989. Involvement of multiple genetic determinants in high-level methicillin resistance in Staphylococcus aureus. J. Bacteriol. 171:874-879.
    • (1989) J. Bacteriol. , vol.171 , pp. 874-879
    • Murakami, K.1    Tomasz, A.2
  • 16
    • 0026085381 scopus 로고
    • Stable classes of phenotypic expression in methicillin-resistant clinical isolates of staphylococci
    • Tomasz A, Nachman S, Leaf H. 1991. Stable classes of phenotypic expression in methicillin-resistant clinical isolates of staphylococci. Antimicrob. Agents Chemother. 35:124-129.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 124-129
    • Tomasz, A.1    Nachman, S.2    Leaf, H.3
  • 17
    • 33747174575 scopus 로고    scopus 로고
    • Microbial cell individuality and the underlying sources of heterogeneity
    • Avery SV. 2006. Microbial cell individuality and the underlying sources of heterogeneity. Nat. Rev. Microbiol. 4:577-587.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 577-587
    • Avery, S.V.1
  • 20
    • 0029311742 scopus 로고
    • Effects of combination of benzylpenicillin and fosfomycin on penicillinresistant Streptococcus pneumoniae
    • Kikuchi K, Totsuka K, Shimizu K, Ishii T, Yoshida T, Orikasa Y. 1995. Effects of combination of benzylpenicillin and fosfomycin on penicillinresistant Streptococcus pneumoniae. Microb. Drug Resist. 1:185-189.
    • (1995) Microb. Drug Resist. , vol.1 , pp. 185-189
    • Kikuchi, K.1    Totsuka, K.2    Shimizu, K.3    Ishii, T.4    Yoshida, T.5    Orikasa, Y.6
  • 22
    • 0014410142 scopus 로고
    • Biosynthesis of uridine diphospho-Nacetylmuramic acid. II. Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine diphospho-N-acetylenopyruvylglucosamine
    • Gunetileke KG, Anwar RA. 1968. Biosynthesis of uridine diphospho-Nacetylmuramic acid. II. Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine diphospho-N-acetylenopyruvylglucosamine. J. Biol. Chem. 243: 5770-5778.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5770-5778
    • Gunetileke, K.G.1    Anwar, R.A.2
  • 23
    • 0030073022 scopus 로고    scopus 로고
    • The versatility of phosphoenolpyruvate and its vinyl ether products in biosynthesis
    • Walsh CT, Benson TE, Kim DH, Lees WJ. 1996. The versatility of phosphoenolpyruvate and its vinyl ether products in biosynthesis. Chem. Biol. 3:83-91.
    • (1996) Chem. Biol. , vol.3 , pp. 83-91
    • Walsh, C.T.1    Benson, T.E.2    Kim, D.H.3    Lees, W.J.4
  • 25
    • 0027130834 scopus 로고
    • Evidence that the reaction of the UDP-Nacetylglucosamine 1-carboxyvinyltransferase proceeds through the Ophosphothioketal of pyruvic acid bound to Cys115 of the enzyme
    • Wanke C, Amrhein N. 1993. Evidence that the reaction of the UDP-Nacetylglucosamine 1-carboxyvinyltransferase proceeds through the Ophosphothioketal of pyruvic acid bound to Cys115 of the enzyme. Eur. J. Biochem. 218:861-870.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 861-870
    • Wanke, C.1    Amrhein, N.2
  • 26
    • 0028070055 scopus 로고
    • Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycin
    • Marquardt JL, Brown ED, Lane WS, Haley TM, Ichikawa Y, Wong CH, Walsh CT. 1994. Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycin. Biochemistry 33:10646-10651.
    • (1994) Biochemistry , vol.33 , pp. 10646-10651
    • Marquardt, J.L.1    Brown, E.D.2    Lane, W.S.3    Haley, T.M.4    Ichikawa, Y.5    Wong, C.H.6    Walsh, C.T.7
  • 27
    • 0001166924 scopus 로고
    • Stereochemical analysis of the tetrahedral adduct formed at the active site of UDP-GlcNAc enolpyruvyl transferase from the pseudosubstrates, (E)-and (Z)-3-fluorophosphoenolpyruvate, in D2O
    • Kim DH, Lees WJ, Walsh CT. 1995. Stereochemical analysis of the tetrahedral adduct formed at the active site of UDP-GlcNAc enolpyruvyl transferase from the pseudosubstrates, (E)-and (Z)-3-fluorophosphoenolpyruvate, in D2O. J. Am. Chem. Soc. 117:6380-6381.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6380-6381
    • Kim, D.H.1    Lees, W.J.2    Walsh, C.T.3
  • 28
    • 77952329483 scopus 로고    scopus 로고
    • The fungal product terreic acid is a covalent inhibitor of the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA)
    • Han H, Yang Y, Olesen SH, Becker A, Betzi S, Schonbrunn E. 2010. The fungal product terreic acid is a covalent inhibitor of the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA). Biochemistry 49:4276-4282.
    • (2010) Biochemistry , vol.49 , pp. 4276-4282
    • Han, H.1    Yang, Y.2    Olesen, S.H.3    Becker, A.4    Betzi, S.5    Schonbrunn, E.6
  • 29
    • 1542467723 scopus 로고    scopus 로고
    • A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states
    • Eschenburg S, Kabsch W, Healy ML, Schonbrunn E. 2003. A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states. J. Biol. Chem. 278:49215-49222.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49215-49222
    • Eschenburg, S.1    Kabsch, W.2    Healy, M.L.3    Schonbrunn, E.4
  • 30
    • 84859749022 scopus 로고    scopus 로고
    • Functional consequence of covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA)
    • Zhu JY, Yang Y, Han H, Betzi S, Olesen SH, Marsilio F, Schonbrunn E. 2012. Functional consequence of covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA). J. Biol. Chem. 287:12657-12667.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12657-12667
    • Zhu, J.Y.1    Yang, Y.2    Han, H.3    Betzi, S.4    Olesen, S.H.5    Marsilio, F.6    Schonbrunn, E.7
  • 31
    • 0030587522 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
    • Schönbrunn E, Sack S, Eschenburg S, Perrakis A, Krekel F, Amrhein N, Mandelkow E. 1996. Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin. Structure 4:1065-1075.
    • (1996) Structure , vol.4 , pp. 1065-1075
    • Schönbrunn, E.1    Sack, S.2    Eschenburg, S.3    Perrakis, A.4    Krekel, F.5    Amrhein, N.6    Mandelkow, E.7
  • 32
    • 0030589610 scopus 로고    scopus 로고
    • Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin
    • Skarzynski T, Mistry A, Wonacott A, Hutchinson SE, Kelly VA, Duncan K. 1996. Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Structure 4:1465-1474.
    • (1996) Structure , vol.4 , pp. 1465-1474
    • Skarzynski, T.1    Mistry, A.2    Wonacott, A.3    Hutchinson, S.E.4    Kelly, V.A.5    Duncan, K.6
  • 33
    • 0035512266 scopus 로고    scopus 로고
    • An rpsL cassette, Janus, for gene replacement through negative selection in Streptococcus pneumoniae
    • Sung CK, Li H, Claverys JP, Morrison DA. 2001. An rpsL cassette, Janus, for gene replacement through negative selection in Streptococcus pneumoniae. Appl. Environ. Microbiol. 67:5190-5196.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 5190-5196
    • Sung, C.K.1    Li, H.2    Claverys, J.P.3    Morrison, D.A.4
  • 36
    • 66749083318 scopus 로고    scopus 로고
    • Detection of Streptococcus pneumoniae strain cocolonization in the nasopharynx
    • Brugger SD, Hathaway LJ, Mühlemann K. 2009. Detection of Streptococcus pneumoniae strain cocolonization in the nasopharynx. J. Clin. Microbiol. 47:1750-1756.
    • (2009) J. Clin. Microbiol. , vol.47 , pp. 1750-1756
    • Brugger, S.D.1    Hathaway, L.J.2    Mühlemann, K.3
  • 37
    • 34547911849 scopus 로고    scopus 로고
    • In vitro expression of the first capsule gene of Streptococcus pneumoniae, cpsA, is associated with serotype-specific colonization prevalence and invasiveness
    • Hathaway LJ, Battig P, Mühlemann K. 2007. In vitro expression of the first capsule gene of Streptococcus pneumoniae, cpsA, is associated with serotype-specific colonization prevalence and invasiveness. Microbiology 153:2465-2471.
    • (2007) Microbiology , vol.153 , pp. 2465-2471
    • Hathaway, L.J.1    Battig, P.2    Mühlemann, K.3
  • 38
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J. Mol. Biol. 33:491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 46
    • 0040805973 scopus 로고    scopus 로고
    • Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA
    • Schönbrunn E, Eschenburg S, Krekel F, Luger K, Amrhein N. 2000. Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA. Biochemistry 39:2164-2173.
    • (2000) Biochemistry , vol.39 , pp. 2164-2173
    • Schönbrunn, E.1    Eschenburg, S.2    Krekel, F.3    Luger, K.4    Amrhein, N.5
  • 48
    • 4344596774 scopus 로고    scopus 로고
    • An internationally spread clone of Streptococcus pneumoniae evolves from low-level to higher-level penicillin resistance by uptake of penicillin-binding protein gene fragments from nonencapsulated pneumococci
    • Hauser C, Aebi S, Mühlemann K. 2004. An internationally spread clone of Streptococcus pneumoniae evolves from low-level to higher-level penicillin resistance by uptake of penicillin-binding protein gene fragments from nonencapsulated pneumococci. Antimicrob. Agents Chemother. 48: 3563-3566.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 3563-3566
    • Hauser, C.1    Aebi, S.2    Mühlemann, K.3
  • 49
    • 2942548974 scopus 로고    scopus 로고
    • A homologue of aliB is found in the capsule region of nonencapsulated Streptococcus pneumoniae
    • Hathaway LJ, Stutzmann Meier P, Battig P, Aebi S, Mühlemann K. 2004. A homologue of aliB is found in the capsule region of nonencapsulated Streptococcus pneumoniae. J. Bacteriol. 186:3721-3729.
    • (2004) J. Bacteriol. , vol.186 , pp. 3721-3729
    • Hathaway, L.J.1    Stutzmann Meier, P.2    Battig, P.3    Aebi, S.4    Mühlemann, K.5
  • 50
    • 34447288927 scopus 로고    scopus 로고
    • Capsule genes of Streptococcus pneumoniae influence growth in vitro
    • Bättig P, Mühlemann K. 2007. Capsule genes of Streptococcus pneumoniae influence growth in vitro. FEMS Immunol. Med. Microbiol. 50: 324-329.
    • (2007) FEMS Immunol. Med. Microbiol. , vol.50 , pp. 324-329
    • Bättig, P.1    Mühlemann, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.