메뉴 건너뛰기




Volumn 7, Issue 1, 2017, Pages

Interaction of lipopolysaccharides at intermolecular sites of the periplasmic Lpt transport assembly

Author keywords

[No Author keywords available]

Indexed keywords

LIPOPOLYSACCHARIDE; PERIPLASMIC PROTEIN; PROTEIN BINDING;

EID: 85028461943     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-017-10136-0     Document Type: Article
Times cited : (35)

References (52)
  • 2
    • 84902202570 scopus 로고    scopus 로고
    • Biosynthesis and export of bacterial lipopolysaccharides
    • Whitfield, C. & Trent, M. S. Biosynthesis and export of bacterial lipopolysaccharides. Annu. Rev. Biochem. 83, 99-128 (2014).
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 99-128
    • Whitfield, C.1    Trent, M.S.2
  • 3
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67, 593-656 (2003).
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 4
    • 84896724035 scopus 로고    scopus 로고
    • The lipopolysaccharide export pathway in Escherichia coli: Structure, organization and regulated assembly of the Lpt machinery
    • Polissi, A. & Sperandeo, P. The lipopolysaccharide export pathway in Escherichia coli: Structure, organization and regulated assembly of the Lpt machinery. Mar. Drugs 12, 1023-1042 (2014).
    • (2014) Mar. Drugs , vol.12 , pp. 1023-1042
    • Polissi, A.1    Sperandeo, P.2
  • 5
    • 77953084208 scopus 로고    scopus 로고
    • Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex
    • Chng, S. S., Gronenberg, L. S. & Kahne, D. Proteins required for lipopolysaccharide assembly in escherichia coli form a transenvelope complex. Biochemistry 49, 4565-4567 (2010).
    • (2010) Biochemistry , vol.49 , pp. 4565-4567
    • Chng, S.S.1    Gronenberg, L.S.2    Kahne, D.3
  • 7
    • 33845950113 scopus 로고    scopus 로고
    • Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli
    • Sperandeo, P. et al. Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli. J. Bacteriol. 189, 244-253 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 244-253
    • Sperandeo, P.1
  • 8
    • 46049106143 scopus 로고    scopus 로고
    • Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Sperandeo, P. et al. Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli. J. Bacteriol. 190, 4460-4469 (2008).
    • (2008) J. Bacteriol. , vol.190 , pp. 4460-4469
    • Sperandeo, P.1
  • 9
    • 44449176988 scopus 로고    scopus 로고
    • Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Ruiz, N., Gronenberg, L. S., Kahne, D. & Silhavy, T. J. Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA. 105, 5537-42 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 5537-5542
    • Ruiz, N.1    Gronenberg, L.S.2    Kahne, D.3    Silhavy, T.J.4
  • 10
    • 67649367532 scopus 로고    scopus 로고
    • Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides
    • Narita, S. & Tokuda, H. Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides. FEBS Letters 583 (2009).
    • (2009) FEBS Letters , vol.583
    • Narita, S.1    Tokuda, H.2
  • 11
    • 84870243063 scopus 로고    scopus 로고
    • Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. Coli
    • Okuda, S., Freinkman, E. & Kahne, D. Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli. Science 338, 1214-7 (2012).
    • (2012) Science , vol.338 , pp. 1214-1217
    • Okuda, S.1    Freinkman, E.2    Kahne, D.3
  • 12
    • 85017231417 scopus 로고    scopus 로고
    • Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG
    • Luo, Q. et al. Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG. Nat. Struct. Mol. Biol. doi:10.1038/nsmb.3399 (2017).
    • (2017) Nat. Struct. Mol. Biol.
    • Luo, Q.1
  • 13
    • 0036046150 scopus 로고    scopus 로고
    • Imp/OstA is required for cell envelope biogenesis in Escherichia coli
    • Braun, M. & Silhavy, T. J. Imp/OstA is required for cell envelope biogenesis in Escherichia coli. Mol. Microbiol. 45, 1289-1302 (2002).
    • (2002) Mol. Microbiol. , vol.45 , pp. 1289-1302
    • Braun, M.1    Silhavy, T.J.2
  • 14
    • 8844219773 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos, M. P. & Tommassen, J. Biogenesis of the Gram-negative bacterial outer membrane. Curr. Opin. Microbiol. 7, 610-616 (2004).
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 610-616
    • Bos, M.P.1    Tommassen, J.2
  • 15
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • Wu, T. et al. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 103, 11754-11759 (2006).
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11754-11759
    • Wu, T.1
  • 16
    • 84862548484 scopus 로고    scopus 로고
    • Regulated assembly of the transenvelope protein complex required for lipopolysaccharide export
    • Freinkman, E., Okuda, S., Ruiz, N. & Kahne, D. Regulated assembly of the transenvelope protein complex required for lipopolysaccharide export. Biochemistry 51, 4800-6 (2012).
    • (2012) Biochemistry , vol.51 , pp. 4800-4806
    • Freinkman, E.1    Okuda, S.2    Ruiz, N.3    Kahne, D.4
  • 17
    • 84873564764 scopus 로고    scopus 로고
    • The Escherichia coli lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains
    • Villa, R. et al. The Escherichia coli lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains. J. Bacteriol. 195, 1100-1108 (2013).
    • (2013) J. Bacteriol. , vol.195 , pp. 1100-1108
    • Villa, R.1
  • 18
    • 51749125875 scopus 로고    scopus 로고
    • Novel structure of the conserved gram-negative lipopolysaccharide transport protein A and mutagenesis analysis
    • Suits, M. D. L., Sperandeo, P., Dehò, G., Polissi, A. & Jia, Z. Novel Structure of the Conserved Gram-Negative Lipopolysaccharide Transport Protein A and Mutagenesis Analysis. J. Mol. Biol. 380, 476-488 (2008).
    • (2008) J. Mol. Biol. , vol.380 , pp. 476-488
    • Suits, M.D.L.1    Sperandeo, P.2    Dehò, G.3    Polissi, A.4    Jia, Z.5
  • 19
    • 77958502198 scopus 로고    scopus 로고
    • Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli
    • Tran, A. X., Dong, C. & Whitfield, C. Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli. J. Biol. Chem. 285, 33529-33539 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 33529-33539
    • Tran, A.X.1    Dong, C.2    Whitfield, C.3
  • 20
    • 84903716134 scopus 로고    scopus 로고
    • Structural basis for lipopolysaccharide insertion in the bacterial outer membrane
    • Qiao, S., Luo, Q., Zhao, Y., Zhang, X. C. & Huang, Y. Structural basis for lipopolysaccharide insertion in the bacterial outer membrane. Nature 511, 108-11 (2014).
    • (2014) Nature , vol.511 , pp. 108-111
    • Qiao, S.1    Luo, Q.2    Zhao, Y.3    Zhang, X.C.4    Huang, Y.5
  • 21
    • 84961964762 scopus 로고    scopus 로고
    • Lipopolysaccharide transport and assembly at the outer membrane: The PEZ model
    • Okuda, S., Sherman, D. J., Silhavy, T. J., Ruiz, N. & Kahne, D. Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model. Nat. Rev. Microbiol. 14, 337-345 (2016).
    • (2016) Nat. Rev. Microbiol. , vol.14 , pp. 337-345
    • Okuda, S.1    Sherman, D.J.2    Silhavy, T.J.3    Ruiz, N.4    Kahne, D.5
  • 22
    • 84856173418 scopus 로고    scopus 로고
    • Concentration-dependent oligomerization and oligomeric arrangement of LptA
    • Merten, J. A., Schultz, K. M. & Klug, C. S. Concentration-dependent oligomerization and oligomeric arrangement of LptA. Protein Sci. 21, 211-218 (2012).
    • (2012) Protein Sci. , vol.21 , pp. 211-218
    • Merten, J.A.1    Schultz, K.M.2    Klug, C.S.3
  • 23
    • 84884562035 scopus 로고    scopus 로고
    • LptA assembles into rod-like oligomers involving disorder-to-order transitions
    • Santambrogio, C. et al. LptA assembles into rod-like oligomers involving disorder-to-order transitions. J. Am. Soc. Mass Spectrom. 24, 1593-1602 (2013).
    • (2013) J. Am. Soc. Mass Spectrom. , vol.24 , pp. 1593-1602
    • Santambrogio, C.1
  • 24
    • 77149159117 scopus 로고    scopus 로고
    • Peptidomimetic antibiotics target outer-membrane biogenesis in pseudomonas aeruginosa
    • Srinivas, N. et al. Peptidomimetic Antibiotics Target Outer-Membrane Biogenesis in Pseudomonas aeruginosa. Science (80-.). 327, 1010-1013 (2010).
    • (2010) Science (80-.) , vol.327 , pp. 1010-1013
    • Srinivas, N.1
  • 25
    • 84864751101 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide transport to the outer membrane in Pseudomonas aeruginosa by peptidomimetic antibiotics
    • Werneburg, M. et al. Inhibition of lipopolysaccharide transport to the outer membrane in Pseudomonas aeruginosa by peptidomimetic antibiotics. Chembiochem 13, 1767-75 (2012).
    • (2012) Chembiochem , vol.13 , pp. 1767-1775
    • Werneburg, M.1
  • 26
    • 84892738005 scopus 로고    scopus 로고
    • Disruption of LptA oligomerization and affinity of the LptA-LptC interaction
    • Schultz, K. M., Feix, J. B. & Klug, C. S. Disruption of LptA oligomerization and affinity of the LptA-LptC interaction. Protein Sci. 22, 1639-1645 (2013).
    • (2013) Protein Sci. , vol.22 , pp. 1639-1645
    • Schultz, K.M.1    Feix, J.B.2    Klug, C.S.3
  • 27
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez, C., Boelens, R. & Bonvin, A. M. J. J. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125, 1731-1737 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 28
    • 84884483881 scopus 로고    scopus 로고
    • Advances in integrative modeling of biomolecular complexes
    • Karaca, E. & Bonvin, A. M. J. J. Advances in integrative modeling of biomolecular complexes. Methods 59, 372-381 (2013).
    • (2013) Methods , vol.59 , pp. 372-381
    • Karaca, E.1    Bonvin, A.M.J.J.2
  • 29
    • 57849140551 scopus 로고    scopus 로고
    • NMR spectral mapping of Lipid A molecular patterns affected by interaction with the innate immune receptor CD14
    • Albright, S., Agrawal, P. & Jain, N. U. NMR spectral mapping of Lipid A molecular patterns affected by interaction with the innate immune receptor CD14. Biochem. Biophys. Res. Commun. 378, 721-726 (2009).
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 721-726
    • Albright, S.1    Agrawal, P.2    Jain, N.U.3
  • 30
    • 0141994975 scopus 로고    scopus 로고
    • Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa
    • Matias, V. R. F., Al-Amoudi, A., Dubochet, J. & Beveridge, T. J. Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa. J. Bacteriol. 185, 6112-6118 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 6112-6118
    • Matias, V.R.F.1    Al-Amoudi, A.2    Dubochet, J.3    Beveridge, T.J.4
  • 31
    • 84982798409 scopus 로고    scopus 로고
    • Functional interaction between the cytoplasmic ABC protein LptB and the inner membrane LptC protein, components of the lipopolysaccharide transport machinery in Escherichia coli
    • Martorana, A. M. et al. Functional interaction between the cytoplasmic ABC protein LptB and the inner membrane LptC protein, components of the lipopolysaccharide transport machinery in Escherichia coli. J. Bacteriol. 198, 2192-2203 (2016).
    • (2016) J. Bacteriol. , vol.198 , pp. 2192-2203
    • Martorana, A.M.1
  • 32
    • 84896402386 scopus 로고    scopus 로고
    • Functional characterization of E. Coli LptC: Interaction with LPS and a synthetic ligand
    • Sestito, S. E. et al. Functional characterization of E. coli LptC: Interaction with LPS and a synthetic ligand. ChemBioChem 15, 734-742 (2014).
    • (2014) ChemBioChem , vol.15 , pp. 734-742
    • Sestito, S.E.1
  • 33
    • 0026457866 scopus 로고
    • Genetic analysis of the immunity region of phage-plasmid P4
    • Ghisotti, D. et al. Genetic analysis of the immunity region of phage-plasmid P4. Mol. Microbiol. 6, 3405-3413 (1992).
    • (1992) Mol. Microbiol. , vol.6 , pp. 3405-3413
    • Ghisotti, D.1
  • 34
    • 0019486545 scopus 로고
    • Catabolism of pseudocumene and 3-ethyltoluene by Pseudomonas putida (arvilla) mt-2: Evidence for new functions of the TOL (pWWO) plasmid
    • Kunz, D. A. & Chapman, P. J. Catabolism of pseudocumene and 3-ethyltoluene by Pseudomonas putida (arvilla) mt-2: Evidence for new functions of the TOL (pWWO) plasmid. J. Bacteriol. 146, 179-191 (1981).
    • (1981) J. Bacteriol. , vol.146 , pp. 179-191
    • Kunz, D.A.1    Chapman, P.J.2
  • 35
    • 0014531184 scopus 로고
    • A new method for the extraction of R lipopolysaccharides
    • Galanos, C., Lüderitz, O. & Westphal, O. A New Method for the Extraction of R Lipopolysaccharides. Eur. J. Biochem. 9, 245-249 (1969).
    • (1969) Eur. J. Biochem. , vol.9 , pp. 245-249
    • Galanos, C.1    Lüderitz, O.2    Westphal, O.3
  • 36
    • 79951599665 scopus 로고    scopus 로고
    • New insights into the Lpt machinery for lipopolysaccharide transport to the cell surface: LptA-LptC interaction and LptA stability as sensors of a properly assembled transenvelope complex
    • Sperandeo, P. et al. New insights into the Lpt machinery for lipopolysaccharide transport to the cell surface: LptA-LptC interaction and LptA stability as sensors of a properly assembled transenvelope complex. J. Bacteriol. 193, 1042-1053 (2011).
    • (2011) J. Bacteriol. , vol.193 , pp. 1042-1053
    • Sperandeo, P.1
  • 37
    • 84904168802 scopus 로고    scopus 로고
    • Elongated structure of the outer-membrane activator of peptidoglycan synthesis LpoA: Implications for PBP1A stimulation
    • Jean, N. L. et al. Elongated structure of the outer-membrane activator of peptidoglycan synthesis LpoA: Implications for PBP1A stimulation. Structure 22, 1047-1054 (2014).
    • (2014) Structure , vol.22 , pp. 1047-1054
    • Jean, N.L.1
  • 38
    • 58149463865 scopus 로고    scopus 로고
    • An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein
    • Ayala, I., Sounier, R., Usé, N., Gans, P. & Boisbouvier, J. An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein. J. Biomol. NMR 43, 111-119 (2009).
    • (2009) J. Biomol. NMR , vol.43 , pp. 111-119
    • Ayala, I.1    Sounier, R.2    Usé, N.3    Gans, P.4    Boisbouvier, J.5
  • 39
    • 84890111683 scopus 로고    scopus 로고
    • Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins
    • Mas, G., Crublet, E., Hamelin, O., Gans, P. & Boisbouvier, J. Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins. J. Biomol. NMR 57, 251-262 (2013).
    • (2013) J. Biomol. NMR , vol.57 , pp. 251-262
    • Mas, G.1    Crublet, E.2    Hamelin, O.3    Gans, P.4    Boisbouvier, J.5
  • 40
    • 84957959996 scopus 로고    scopus 로고
    • CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample
    • Kerfah, R., Hamelin, O., Boisbouvier, J. & Marion, D. CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample. J. Biomol. NMR 63, 389-402 (2015).
    • (2015) J. Biomol. NMR , vol.63 , pp. 389-402
    • Kerfah, R.1    Hamelin, O.2    Boisbouvier, J.3    Marion, D.4
  • 41
    • 75749113634 scopus 로고    scopus 로고
    • Guidelines for the use of band-selective radiofrequency pulses in hetero-nuclear NMR: Example of longitudinal-relaxation-enhanced BEST-type 1H-15N correlation experiments
    • Lescop, E., Kern, T. & Brutscher, B. Guidelines for the use of band-selective radiofrequency pulses in hetero-nuclear NMR: Example of longitudinal-relaxation-enhanced BEST-type 1H-15N correlation experiments. J. Magn. Reson. 203, 190-198 (2010).
    • (2010) J. Magn. Reson. , vol.203 , pp. 190-198
    • Lescop, E.1    Kern, T.2    Brutscher, B.3
  • 42
    • 84921813844 scopus 로고    scopus 로고
    • ISPyB for BioSAXS, the gateway to user autonomy in solution scattering experiments
    • Antolinos, D. M. A. et al. ISPyB for BioSAXS, the gateway to user autonomy in solution scattering experiments. Acta Crystallogr. Sect. D Biol. Crystallogr. 71, 76-85 (2015).
    • (2015) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.71 , pp. 76-85
    • Antolinos, D.M.A.1
  • 43
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • Petoukhov, M. V. et al. New developments in the ATSAS program package for small-angle scattering data analysis. J. Appl. Crystallogr. 45, 342-350 (2012).
    • (2012) J. Appl. Crystallogr. , vol.45 , pp. 342-350
    • Petoukhov, M.V.1
  • 44
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke, D. & Svergun, D. I. DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J. Appl. Crystallogr. 42, 342-346 (2009).
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 45
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C. & Koch, M. H. CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773 (1995).
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 46
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B. & Svergun, D. I. Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41 (2001).
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 47
    • 84959457637 scopus 로고    scopus 로고
    • The HADDOCK2.2 web server: User-friendly integrative modeling of biomolecular complexes
    • Van Zundert, G. C. P. et al. The HADDOCK2.2 Web Server: User-Friendly Integrative Modeling of Biomolecular Complexes. J. Mol. Biol. 428, 720-725 (2016).
    • (2016) J. Mol. Biol. , vol.428 , pp. 720-725
    • Van Zundert, G.C.P.1
  • 48
  • 49
    • 4444221565 scopus 로고    scopus 로고
    • UCSF chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-A Visualization System for Exploratory Research and Analysis. J Comput Chem 25, 1605-1612 (2004).
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 50
    • 77954262905 scopus 로고    scopus 로고
    • 3V: Cavity, channel and cleft volume calculator and extractor
    • Voss, N. R. & Gerstein, M. 3V: Cavity, channel and cleft volume calculator and extractor. Nucleic Acids Res. 38, W555-62 (2010).
    • (2010) Nucleic Acids Res. , vol.38 , pp. W555-W562
    • Voss, N.R.1    Gerstein, M.2
  • 51
    • 0033570004 scopus 로고    scopus 로고
    • Massive outbreak of Escherichia coli O157:H7 infection in schoolchildren in sakai city, Japan, associated with consumption of white radish sprouts
    • Michino, H. et al. Massive outbreak of Escherichia coli O157:H7 infection in schoolchildren in Sakai City, Japan, associated with consumption of white radish sprouts. Am. J. Epidemiol. 150, 787-96 (1999).
    • (1999) Am. J. Epidemiol. , vol.150 , pp. 787-796
    • Michino, H.1
  • 52
    • 84863846116 scopus 로고    scopus 로고
    • Lipopolysaccharide O-antigen of enterohemorrhagic Escherichia coli O157:H7 is required for killing both insects and mammals
    • Miyashita, A. et al. Lipopolysaccharide O-antigen of enterohemorrhagic Escherichia coli O157:H7 is required for killing both insects and mammals. FEMS Microbiol. Lett. 333, 59-68 (2012).
    • (2012) FEMS Microbiol. Lett. , vol.333 , pp. 59-68
    • Miyashita, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.