메뉴 건너뛰기




Volumn 11, Issue , 2011, Pages

Deletion of the glycosyltransferase bgsB of Enterococcus faecalis leads to a complete loss of glycolipids from the cell membrane and to impaired biofilm formation

Author keywords

[No Author keywords available]

Indexed keywords

BIOFILM ASSOCIATED GLYCOLIPID SYNTHESIS A; BIOFILM ASSOCIATED GLYCOLIPID SYNTHESIS B; GLUCOSYLTRANSFERASE; GLYCEROPHOSPHATE; GLYCOLIPID; GLYCOSYLTRANSFERASE; LIPOTEICHOIC ACID; POLYPEPTIDE ANTIBIOTIC AGENT; POLYSTYRENE; UNCLASSIFIED DRUG; LIPOPOLYSACCHARIDE; TEICHOIC ACID;

EID: 79953644934     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-11-67     Document Type: Article
Times cited : (33)

References (35)
  • 1
    • 40949089662 scopus 로고    scopus 로고
    • Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions
    • DOI 10.1038/nrmicro1861, PII NRMICRO1861
    • Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions. C Weidenmaier A Peschel, Nat Rev Microbiol 2008 6 4 276 287 10.1038/nrmicro1861 18327271 (Pubitemid 351404772)
    • (2008) Nature Reviews Microbiology , vol.6 , Issue.4 , pp. 276-287
    • Weidenmaier, C.1    Peschel, A.2
  • 2
    • 79952790266 scopus 로고    scopus 로고
    • Serodiversity of Opsonic Antibodies against Enterococcus faecalis -Glycans of the Cell Wall Revisited
    • 10.1371/journal.pone.0017839. 21437253
    • Serodiversity of Opsonic Antibodies against Enterococcus faecalis -Glycans of the Cell Wall Revisited. C Theilacker Z Kaczynski A Kropec I Sava L Ye A Bychowska O Holst J Huebner, PLoS ONE 2011 6 3 17839 10.1371/journal.pone. 0017839 21437253
    • (2011) PLoS ONE , vol.6 , Issue.3 , pp. 517839
    • Theilacker, C.1    Kaczynski, Z.2    Kropec, A.3    Sava, I.4    Ye, L.5    Bychowska, A.6    Holst, O.7    Huebner, J.8
  • 3
    • 69049095027 scopus 로고    scopus 로고
    • Further characterization of the epa gene cluster and Epa polysaccharides of Enterococcus faecalis
    • 10.1128/IAI.00149-09. 19581393
    • Further characterization of the epa gene cluster and Epa polysaccharides of Enterococcus faecalis. F Teng KV Singh A Bourgogne J Zeng BE Murray, Infect Immun 2009 77 9 3759 3767 10.1128/IAI.00149-09 19581393
    • (2009) Infect Immun , vol.77 , Issue.9 , pp. 3759-3767
    • Teng, F.1    Singh, K.V.2    Bourgogne, A.3    Zeng, J.4    Murray, B.E.5
  • 4
    • 33749266224 scopus 로고    scopus 로고
    • Opsonic antibodies to Enterococcus faecalis strain 12030 are directed against lipoteichoic acid
    • DOI 10.1128/IAI.00570-06
    • Opsonic antibodies to Enterococcus faecalis strain 12030 are directed against lipoteichoic acid. C Theilacker Z Kaczynski A Kropec F Fabretti T Sange O Holst J Huebner, Infect Immun 2006 74 10 5703 5712 10.1128/IAI.00570-06 16988246 (Pubitemid 44484554)
    • (2006) Infection and Immunity , vol.74 , Issue.10 , pp. 5703-5712
    • Theilacker, C.1    Kaczynski, Z.2    Kropec, A.3    Fabretti, F.4    Sange, T.5    Holst, O.6    Huebner, J.7
  • 5
    • 60349126579 scopus 로고    scopus 로고
    • Glycolipids are involved in biofilm accumulation and prolonged bacteraemia in Enterococcus faecalis
    • 10.1111/j.1365-2958.2008.06587.x. 19170884
    • Glycolipids are involved in biofilm accumulation and prolonged bacteraemia in Enterococcus faecalis. C Theilacker P Sanchez-Carballo I Toma F Fabretti I Sava A Kropec O Holst J Huebner, Mol Microbiol 2009 71 4 1055 1069 10.1111/j.1365-2958.2008.06587.x 19170884
    • (2009) Mol Microbiol , vol.71 , Issue.4 , pp. 1055-1069
    • Theilacker, C.1    Sanchez-Carballo, P.2    Toma, I.3    Fabretti, F.4    Sava, I.5    Kropec, A.6    Holst, O.7    Huebner, J.8
  • 6
    • 1642396318 scopus 로고    scopus 로고
    • Monoglucosyldiacylglycerol, a Foreign Lipid, Can Substitute for Phosphatidylethanolamine in Essential Membrane-associated Functions in Escherichia coli
    • DOI 10.1074/jbc.M310183200
    • Monoglucosyldiacylglycerol, a foreign lipid, can substitute for phosphatidylethanolamine in essential membrane-associated functions in Escherichia coli. M Wikström J Xie M Bogdanov E Mileykovskaya P Heacock A Wieslander W Dowhan, J Biol Chem 2004 279 11 10484 10493 14688287 (Pubitemid 38372658)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 10484-10493
    • Wikstrom, M.1    Xie, J.2    Bogdanov, M.3    Mileykovskaya, E.4    Heacock, P.5    Wieslander, A.6    Dowhan, W.7
  • 7
    • 0037424229 scopus 로고    scopus 로고
    • Structural features of glycosyltransferases synthesizing major bilayer and nonbilayer-prone membrane lipids in Acholeplasma laidlawii and Streptococcus pneumoniae
    • DOI 10.1074/jbc.M211492200
    • Structural features of glycosyltransferases synthesizing major bilayer and nonbilayer-prone membrane lipids in Acholeplasma laidlawii and Streptococcus pneumoniae. M Edman S Berg P Storm M Wikstrom S Vikstrom A Ohman A Wieslander, J Biol Chem 2003 278 10 8420 8428 10.1074/jbc.M211492200 12464611 (Pubitemid 36800592)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8420-8428
    • Edman, M.1    Berg, S.2    Storm, P.3    Wikstrom, M.4    Vikstrom, S.5    Ohman, A.6    Wieslander, A.7
  • 8
    • 0034737656 scopus 로고    scopus 로고
    • The nonbilayer/bilayer lipid balance in membranes. Regulatory enzyme in Acholeplasma laidlawii is stimulated by metabolic phosphates, activator phospholipids and double-stranded DNA
    • DOI 10.1074/jbc.275.13.9296
    • The nonbilayer/bilayer lipid balance in membranes. Regulatory enzyme in Acholeplasma laidlawii is stimulated by metabolic phosphates, activator phospholipids, and double-stranded DNA. S Vikström L Li A Wieslander, J Biol Chem 2000 275 13 9296 9302 10734070 (Pubitemid 30185151)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.13 , pp. 9296-9302
    • Vikstrom, S.1    Li, L.2    Wieslander, A.3
  • 9
    • 0032007891 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities
    • 9445404
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. J Campbell G Davies V Bulone B Henrissat, Biochem J 1998 329 Pt 3 719 9445404
    • (1998) Biochem J , vol.329 , Issue.PART 3 , pp. 719
    • Campbell, J.1    Davies, G.2    Bulone, V.3    Henrissat, B.4
  • 10
    • 66249119393 scopus 로고    scopus 로고
    • Lipoteichoic acid biosynthesis: Two steps forwards, one step sideways?
    • 10.1016/j.tim.2009.03.003. 19464183
    • Lipoteichoic acid biosynthesis: two steps forwards, one step sideways? O Rahman LG Dover IC Sutcliffe, Trends Microbiol 2009 17 6 219 225 10.1016/j.tim.2009.03.003 19464183
    • (2009) Trends Microbiol , vol.17 , Issue.6 , pp. 219-225
    • Rahman, O.1    Dover, L.G.2    Sutcliffe, I.C.3
  • 11
    • 0347479228 scopus 로고    scopus 로고
    • A Continuum of Anionic Charge: Structures and Functions of D-Alanyl-Teichoic Acids in Gram-Positive Bacteria
    • DOI 10.1128/MMBR.67.4.686-723.2003
    • A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. FC Neuhaus J Baddiley, Microbiol Mol Biol Rev 2003 67 4 686 723 10.1128/MMBR.67.4.686-723.2003 14665680 (Pubitemid 37549774)
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.4 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 12
    • 34547682153 scopus 로고    scopus 로고
    • A Staphylococcus aureus ypfP mutant with strongly reduced lipoteichoic acid (LTA) content: LTA governs bacterial surface properties and autolysin activity
    • DOI 10.1111/j.1365-2958.2007.05854.x
    • A Staphylococcus aureus ypfP mutant with strongly reduced lipoteichoic acid (LTA) content: LTA governs bacterial surface properties and autolysin activity. I Fedtke D Mader T Kohler H Moll G Nicholson R Biswas K Henseler F Götz U Zähringer A Peschel, Mol Microbiol 2007 65 4 1078 1091 10.1111/j.1365-2958.2007.05854.x 17640274 (Pubitemid 47221088)
    • (2007) Molecular Microbiology , vol.65 , Issue.4 , pp. 1078-1091
    • Fedtke, I.1    Mader, D.2    Kohler, T.3    Moll, H.4    Nicholson, G.5    Biswas, R.6    Henseler, K.7    Gotz, F.8    Zahringer, U.9    Peschel, A.10
  • 13
    • 33947170440 scopus 로고    scopus 로고
    • Genes required for glycolipid synthesis and lipoteichoic acid anchoring in Staphylococcus aureus
    • DOI 10.1128/JB.01683-06
    • Genes required for glycolipid synthesis and lipoteichoic acid anchoring in Staphylococcus aureus. A Grundling O Schneewind, J Bacteriol 2007 189 6 2521 2530 10.1128/JB.01683-06 17209021 (Pubitemid 46411366)
    • (2007) Journal of Bacteriology , vol.189 , Issue.6 , pp. 2521-2530
    • Grundling, A.1    Schneewind, O.2
  • 14
    • 0035933799 scopus 로고    scopus 로고
    • Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes. Recognition of a large group of lipid glycosyltransferases in eubacteria and archaea
    • 10.1074/jbc.M102576200. 11294844
    • Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes. Recognition of a large group of lipid glycosyltransferases in eubacteria and archaea. S Berg M Edman L Li M Wikstrom A Wieslander, J Biol Chem 2001 276 25 22056 22063 10.1074/jbc.M102576200 11294844
    • (2001) J Biol Chem , vol.276 , Issue.25 , pp. 22056-22063
    • Berg, S.1    Edman, M.2    Li, L.3    Wikstrom, M.4    Wieslander, A.5
  • 15
    • 70349900174 scopus 로고    scopus 로고
    • Two-enzyme systems for glycolipid and polyglycerolphosphate lipoteichoic acid synthesis in Listeria monocytogenes
    • 10.1111/j.1365-2958.2009.06829.x. 19682249
    • Two-enzyme systems for glycolipid and polyglycerolphosphate lipoteichoic acid synthesis in Listeria monocytogenes. AJ Webb M Karatsa-Dodgson A Grundling, Mol Microbiol 2009 74 2 299 314 10.1111/j.1365-2958.2009.06829.x 19682249
    • (2009) Mol Microbiol , vol.74 , Issue.2 , pp. 299-314
    • Webb, A.J.1    Karatsa-Dodgson, M.2    Grundling, A.3
  • 16
    • 0035026895 scopus 로고    scopus 로고
    • Biosynthesis of the glycolipid anchor in lipoteichoic acid of Staphylococcus aureus RN4220: Role of YpfP, the diglucosyldiacylglycerol synthase
    • DOI 10.1128/JB.183.11.3506-3514.2001
    • Biosynthesis of the glycolipid anchor in lipoteichoic acid of Staphylococcus aureus RN4220: role of YpfP, the diglucosyldiacylglycerol synthase. MY Kiriukhin DV Debabov DL Shinabarger FC Neuhaus, J Bacteriol 2001 183 11 3506 3514 10.1128/JB.183.11.3506-3514.2001 11344159 (Pubitemid 32448614)
    • (2001) Journal of Bacteriology , vol.183 , Issue.11 , pp. 3506-3514
    • Kiriukhin, M.Y.1    Debabov, D.V.2    Shinabarger, D.L.3    Neuhaus, F.C.4
  • 17
    • 0031848910 scopus 로고    scopus 로고
    • A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: Expression of ypfP in Escherichia coil and structural analysis of its reaction products
    • DOI 10.1046/j.1365-2958.1998.00930.x
    • A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products. P Jorasch FP Wolter U Zähringer E Heinz, Mol Microbiol 1998 29 2 419 430 10.1046/j.1365-2958.1998.00930.x 9720862 (Pubitemid 28330778)
    • (1998) Molecular Microbiology , vol.29 , Issue.2 , pp. 419-430
    • Jorasch, P.1    Wolter, F.P.2    Zahringer, U.3    Heinz, E.4
  • 19
    • 0000705051 scopus 로고
    • Bacterial phosphoglycolipids and lipoteichoic acids
    • New York: Plenum Press Hanahan DJ
    • Bacterial phosphoglycolipids and lipoteichoic acids. W Fischer, Handbook of Lipid Research New York: Plenum Press, Hanahan DJ, 1990 6 123 234
    • (1990) Handbook of Lipid Research , vol.6 , pp. 123-234
    • Fischer, W.1
  • 20
    • 37249055056 scopus 로고    scopus 로고
    • Biofilm formation by enterococci
    • DOI 10.1099/jmm.0.47331-0
    • Biofilm formation by enterococci. JA Mohamed DB Huang, J Med Microbiol 2007 56 Pt 12 1581 1588 10.1099/jmm.0.47331-0 18033823 (Pubitemid 350276505)
    • (2007) Journal of Medical Microbiology , vol.56 , Issue.12 , pp. 1581-1588
    • Mohamed, J.A.1    Huang, D.B.2
  • 21
    • 2542610000 scopus 로고    scopus 로고
    • Influence of origin of isolates, especially endocarditis isolates, and various genes on biofilm formation by Enterococcus faecalis
    • DOI 10.1128/IAI.72.6.3658-3663.2004
    • Influence of origin of isolates, especially endocarditis isolates, and various genes on biofilm formation by Enterococcus faecalis. JA Mohamed W Huang SR Nallapareddy F Teng BE Murray, Infect Immun 2004 72 6 3658 3663 10.1128/IAI.72.6.3658-3663.2004 15155680 (Pubitemid 38697799)
    • (2004) Infection and Immunity , vol.72 , Issue.6 , pp. 3658-3663
    • Mohamed, J.A.1    Huang, W.2    Nallapareddy, S.R.3    Teng, F.4    Murray, B.E.5
  • 22
    • 0032898403 scopus 로고    scopus 로고
    • Physico-chemistry of initial microbial adhesive interactions - Its mechanisms and methods for study
    • 10234844
    • Physico-chemistry of initial microbial adhesive interactions - its mechanisms and methods for study. R Bos HC van der Mei HJ Busscher, FEMS Microbiol Rev 1999 23 2 179 230 10234844
    • (1999) FEMS Microbiol Rev , vol.23 , Issue.2 , pp. 179-230
    • Bos, R.1    Van Der Mei, H.C.2    Busscher, H.J.3
  • 23
    • 58349111705 scopus 로고    scopus 로고
    • Relationship between expression of the family of M proteins and lipoteichoic acid to hydrophobicity and biofilm formation in Streptococcus pyogenes
    • 10.1371/journal.pone.0004166. 19132104
    • Relationship between expression of the family of M proteins and lipoteichoic acid to hydrophobicity and biofilm formation in Streptococcus pyogenes. HS Courtney I Ofek T Penfound V Nizet MA Pence B Kreikemeyer A Podbielski A Podbielbski DL Hasty JB Dale, PLoS ONE 2009 4 1 4166 10.1371/journal.pone.0004166 19132104
    • (2009) PLoS ONE , vol.4 , Issue.1 , pp. 54166
    • Courtney, H.S.1    Ofek, I.2    Penfound, T.3    Nizet, V.4    Pence, M.A.5    Kreikemeyer, B.6    Podbielski, A.7    Podbielbski, A.8    Hasty, D.L.9    Dale, J.B.10
  • 24
    • 33745625880 scopus 로고    scopus 로고
    • Alanine esters of enterococcal lipoteichoic acid play a role in biofilm formation and resistance to antimicrobial peptides
    • DOI 10.1128/IAI.00111-06
    • Alanine esters of enterococcal lipoteichoic acid play a role in biofilm formation and resistance to antimicrobial peptides. F Fabretti C Theilacker L Baldassarri Z Kaczynski A Kropec O Holst J Huebner, Infect Immun 2006 74 7 4164 4171 10.1128/IAI.00111-06 16790791 (Pubitemid 43993350)
    • (2006) Infection and Immunity , vol.74 , Issue.7 , pp. 4164-4171
    • Fabretti, F.1    Theilacker, C.2    Baldassarri, L.3    Kaczynski, Z.4    Kropec, A.5    Holst, O.6    Huebner, J.7
  • 25
    • 0035059332 scopus 로고    scopus 로고
    • Key role of teichoic acid net charge in Staphylococcus aureus colonization of artificial surfaces
    • DOI 10.1128/IAI.69.5.3423-3426.2001
    • Key role of teichoic acid net charge in Staphylococcus aureus colonization of artificial surfaces. M Gross SE Cramton F Götz A Peschel, Infect Immun 2001 69 5 3423 3426 10.1128/IAI.69.5.3423-3426.2001 11292767 (Pubitemid 32332242)
    • (2001) Infection and Immunity , vol.69 , Issue.5 , pp. 3423-3426
    • Gross, M.1    Cramton, S.E.2    Gotz, F.3    Peschel, A.4
  • 26
    • 0029980555 scopus 로고    scopus 로고
    • Significance of bacterial surface-active compounds in interaction of bacteria with interfaces
    • Significance of bacterial surface-active compounds in interaction of bacteria with interfaces. TR Neu, Microbiol Rev 1996 60 1 151 166 8852899 (Pubitemid 26087766)
    • (1996) Microbiological Reviews , vol.60 , Issue.1 , pp. 151-166
    • Neu, T.R.1
  • 27
    • 36148995456 scopus 로고    scopus 로고
    • Comparative study of the physiological roles of three peroxidases (NADH peroxidase, Alkyl hydroperoxide reductase and Thiol peroxidase) in oxidative stress response, survival inside macrophages and virulence of Enterococcus faecalis
    • DOI 10.1111/j.1365-2958.2007.05987.x
    • Comparative study of the physiological roles of three peroxidases (NADH peroxidase, Alkyl hydroperoxide reductase and Thiol peroxidase) in oxidative stress response, survival inside macrophages and virulence of Enterococcus faecalis. S La Carbona N Sauvageot JC Giard A Benachour B Posteraro Y Auffray M Sanguinetti A Hartke, Mol Microbiol 2007 66 5 1148 1163 10.1111/j.1365-2958. 2007.05987.x 17971082 (Pubitemid 350115023)
    • (2007) Molecular Microbiology , vol.66 , Issue.5 , pp. 1148-1163
    • La Carbona, S.1    Sauvageot, N.2    Giard, J.-C.3    Benachour, A.4    Posteraro, B.5    Auffray, Y.6    Sanguinetti, M.7    Hartke, A.8
  • 28
    • 67650528820 scopus 로고    scopus 로고
    • Novel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells
    • 10.1074/jbc.M901460200. 19395379
    • Novel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells. IG Sava F Zhang I Toma C Theilacker B Li TF Baumert O Holst RJ Linhardt J Huebner, J Biol Chem 2009 284 27 18194 18201 10.1074/jbc.M901460200 19395379
    • (2009) J Biol Chem , vol.284 , Issue.27 , pp. 18194-18201
    • Sava, I.G.1    Zhang, F.2    Toma, I.3    Theilacker, C.4    Li, B.5    Baumert, T.F.6    Holst, O.7    Linhardt, R.J.8    Huebner, J.9
  • 31
    • 0026695485 scopus 로고
    • Comparison of contact angles and adhesion to hexadecane of urogenital, dairy, and poultry lactobacilli: Effect of serial culture passages
    • 1622224
    • Comparison of contact angles and adhesion to hexadecane of urogenital, dairy, and poultry lactobacilli: effect of serial culture passages. G Reid PL Cuperus AW Bruce HC van der Mei L Tomeczek AH Khoury HJ Busscher, Appl Environ Microbiol 1992 58 5 1549 1553 1622224
    • (1992) Appl Environ Microbiol , vol.58 , Issue.5 , pp. 1549-1553
    • Reid, G.1    Cuperus, P.L.2    Bruce, A.W.3    Van Der Mei, H.C.4    Tomeczek, L.5    Khoury, A.H.6    Busscher, H.J.7
  • 32
    • 1142309464 scopus 로고    scopus 로고
    • A Putative Sugar-Binding Transcriptional Regulator in a Novel Gene Locus in Enterococcus faecalis Contributes to Production of Biofilm and Prolonged Bacteremia in Mice
    • DOI 10.1086/381150
    • A putative sugar-binding transcriptional regulator in a novel gene locus in Enterococcus faecalis contributes to production of biofilm and prolonged bacteremia in mice. M Hufnagel S Koch R Creti L Baldassarri J Huebner, J Infect Dis 2004 189 3 420 430 10.1086/381150 14745699 (Pubitemid 38210578)
    • (2004) Journal of Infectious Diseases , vol.189 , Issue.3 , pp. 420-430
    • Hufnagel, M.1    Koch, S.2    Creti, R.3    Baldassarri, L.4    Huebner, J.5
  • 33
    • 0033052677 scopus 로고    scopus 로고
    • Isolation and chemical characterization of a capsular polysaccharide antigen shared by clinical isolates of Enterococcus faecalis and vancomycin- resistant Enterococcus faecium
    • Isolation and chemical characterization of a capsular polysaccharide antigen shared by clinical isolates of Enterococcus faecalis and vancomycin-resistant Enterococcus faecium. J Huebner Y Wang WA Krueger LC Madoff G Martirosian S Boisot DA Goldmann DL Kasper AO Tzianabos GB Pier, Infect Immun 1999 67 3 1213 1219 10024563 (Pubitemid 29108497)
    • (1999) Infection and Immunity , vol.67 , Issue.3 , pp. 1213-1219
    • Huebner, J.1    Wang, Y.2    Krueger, W.A.3    Madoff, L.C.4    Martirosian, G.5    Boisot, S.6    Goldmann, D.A.7    Kasper, D.L.8    Tzianabos, A.O.9    Pier, G.B.10
  • 34
    • 0032968219 scopus 로고    scopus 로고
    • Role of hemolysin BL in the pathogenesis of extraintestinal Bacillus cereus infection assessed in an endophthalmitis model
    • Role of hemolysin BL in the pathogenesis of extraintestinal Bacillus cereus infection assessed in an endophthalmitis model. MC Callegan BD Jett LE Hancock MS Gilmore, Infect Immun 1999 67 7 3357 3366 10377113 (Pubitemid 29291503)
    • (1999) Infection and Immunity , vol.67 , Issue.7 , pp. 3357-3366
    • Callegan, M.C.1    Jett, B.D.2    Hancock, L.E.3    Gilmore, M.S.4
  • 35
    • 8744309111 scopus 로고    scopus 로고
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria
    • DOI 10.1128/AEM.70.11.6887-6891.2004
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria. M Arnaud A Chastanet M Debarbouille, Appl Environ Microbiol 2004 70 11 6887 6891 10.1128/AEM.70.11. 6887-6891.2004 15528558 (Pubitemid 39518603)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.11 , pp. 6887-6891
    • Arnaud, M.1    Chastanet, A.2    Debarbouille, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.