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Volumn 180, Issue , 2015, Pages 1-10

Klebsiella pneumoniae O antigen loss alters the outer membrane protein composition and the selective packaging of proteins into secreted outer membrane vesicles

Author keywords

Nosocomial pathogen; O antigen; Outer membrane vesicles; Protein secretion

Indexed keywords

ANTIGENS; BACTERIA; MEMBRANES; SORTING;

EID: 84944876322     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2015.06.012     Document Type: Article
Times cited : (44)

References (67)
  • 1
    • 0033963553 scopus 로고    scopus 로고
    • Capsular polysaccharide is a major complement resistance factor in lipopolysaccharide O side chain-deficient Klebsiella pneumoniae clinical isolates
    • Alvarez D., Merino S., Tomas J.M., Benedi V.J., Alberti S. Capsular polysaccharide is a major complement resistance factor in lipopolysaccharide O side chain-deficient Klebsiella pneumoniae clinical isolates. Infect Immun 2000, 68(2):953-955.
    • (2000) Infect Immun , vol.68 , Issue.2 , pp. 953-955
    • Alvarez, D.1    Merino, S.2    Tomas, J.M.3    Benedi, V.J.4    Alberti, S.5
  • 2
    • 0033988220 scopus 로고    scopus 로고
    • Elongation factor Tu and DnaK are transferred from the cytoplasm to the periplasm of Escherichia coli during osmotic downshock presumably via the mechanosensitive channel mscL
    • Berrier C., Garrigues A., Richarme G., Ghazi A. Elongation factor Tu and DnaK are transferred from the cytoplasm to the periplasm of Escherichia coli during osmotic downshock presumably via the mechanosensitive channel mscL. J Bacteriol 2000, 182(1):248-251.
    • (2000) J Bacteriol , vol.182 , Issue.1 , pp. 248-251
    • Berrier, C.1    Garrigues, A.2    Richarme, G.3    Ghazi, A.4
  • 3
    • 84902288820 scopus 로고    scopus 로고
    • Protein selection and export via outer membrane vesicles
    • Bonnington K.E., Kuehn M.J. Protein selection and export via outer membrane vesicles. Biochim Biophys Acta 2014, 1843(8):1612-1619.
    • (2014) Biochim Biophys Acta , vol.1843 , Issue.8 , pp. 1612-1619
    • Bonnington, K.E.1    Kuehn, M.J.2
  • 4
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • Bulieris P.V., Behrens S., Holst O., Kleinschmidt J.H. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J Biol Chem 2003, 278(11):9092-9099.
    • (2003) J Biol Chem , vol.278 , Issue.11 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 6
    • 79960832704 scopus 로고    scopus 로고
    • Proteomic analysis of outer membrane vesicles derived from Pseudomonas aeruginosa
    • Choi D.S., Kim D.K., Choi S.J., Lee J., Choi J.P., Rho S., et al. Proteomic analysis of outer membrane vesicles derived from Pseudomonas aeruginosa. Proteomics 2011, 11(16):3424-3429.
    • (2011) Proteomics , vol.11 , Issue.16 , pp. 3424-3429
    • Choi, D.S.1    Kim, D.K.2    Choi, S.J.3    Lee, J.4    Choi, J.P.5    Rho, S.6
  • 7
    • 84879283912 scopus 로고    scopus 로고
    • Quantitative and qualitative preparations of bacterial outer membrane vesicles
    • Chutkan H., Macdonald I., Manning A., Kuehn M.J. Quantitative and qualitative preparations of bacterial outer membrane vesicles. Methods Mol Biol 2013, 966:259-272.
    • (2013) Methods Mol Biol , vol.966 , pp. 259-272
    • Chutkan, H.1    Macdonald, I.2    Manning, A.3    Kuehn, M.J.4
  • 8
    • 84875535533 scopus 로고    scopus 로고
    • Identification of the mutation responsible for the temperature-sensitive lipopolysaccharide O-antigen defect in the Pseudomonas aeruginosa cystic fibrosis isolate 2192
    • Davis M.R., Muszynski A., Lollett I.V., Pritchett C.L., Carlson R.W., Goldberg J.B. Identification of the mutation responsible for the temperature-sensitive lipopolysaccharide O-antigen defect in the Pseudomonas aeruginosa cystic fibrosis isolate 2192. J Bacteriol 2013, 195(7):1504-1514.
    • (2013) J Bacteriol , vol.195 , Issue.7 , pp. 1504-1514
    • Davis, M.R.1    Muszynski, A.2    Lollett, I.V.3    Pritchett, C.L.4    Carlson, R.W.5    Goldberg, J.B.6
  • 9
    • 0033582497 scopus 로고    scopus 로고
    • Non-lamellar structure and negative charges of lipopolysaccharides required for efficient folding of outer membrane protein PhoE of Escherichia coli
    • de Cock H., Brandenburg K., Wiese A., Holst O., Seydel U. Non-lamellar structure and negative charges of lipopolysaccharides required for efficient folding of outer membrane protein PhoE of Escherichia coli. J Biol Chem 1999, 274(8):5114-5119.
    • (1999) J Biol Chem , vol.274 , Issue.8 , pp. 5114-5119
    • de Cock, H.1    Brandenburg, K.2    Wiese, A.3    Holst, O.4    Seydel, U.5
  • 11
    • 84899734976 scopus 로고    scopus 로고
    • Preferential packing of acidic glycosidases and proteases into Bacteroides outer membrane vesicles
    • Elhenawy W., Debelyy M.O., Feldman M.F. Preferential packing of acidic glycosidases and proteases into Bacteroides outer membrane vesicles. mBio 2014, 5(2):e00909-e00914.
    • (2014) mBio , vol.5 , Issue.2 , pp. e00909-e00914
    • Elhenawy, W.1    Debelyy, M.O.2    Feldman, M.F.3
  • 12
    • 77749309281 scopus 로고    scopus 로고
    • Virulence and immunomodulatory roles of bacterial outer membrane vesicles
    • Ellis T.N., Kuehn M.J. Virulence and immunomodulatory roles of bacterial outer membrane vesicles. Microbiol Mol Biol Rev 2010, 74(1):81-94.
    • (2010) Microbiol Mol Biol Rev , vol.74 , Issue.1 , pp. 81-94
    • Ellis, T.N.1    Kuehn, M.J.2
  • 13
    • 0035678319 scopus 로고    scopus 로고
    • Salmonella typhimurium outer membrane remodeling: role in resistance to host innate immunity
    • Ernst R.K., Guina T., Miller S.I. Salmonella typhimurium outer membrane remodeling: role in resistance to host innate immunity. Microbes Infect 2001, 3(14-15):1327-1334.
    • (2001) Microbes Infect , vol.3 , Issue.14-15 , pp. 1327-1334
    • Ernst, R.K.1    Guina, T.2    Miller, S.I.3
  • 15
    • 73449141831 scopus 로고    scopus 로고
    • Roles of capsule and lipopolysaccharide O antigen in interactions of human monocyte-derived dendritic cells and Klebsiella pneumoniae
    • Evrard B., Balestrino D., Dosgilbert A., Bouya-Gachancard J.L., Charbonnel N., Forestier C., et al. Roles of capsule and lipopolysaccharide O antigen in interactions of human monocyte-derived dendritic cells and Klebsiella pneumoniae. Infect Immun 2010, 78(1):210-219.
    • (2010) Infect Immun , vol.78 , Issue.1 , pp. 210-219
    • Evrard, B.1    Balestrino, D.2    Dosgilbert, A.3    Bouya-Gachancard, J.L.4    Charbonnel, N.5    Forestier, C.6
  • 16
    • 33645473483 scopus 로고    scopus 로고
    • Outer membrane vesicles from group B Neisseria meningitidis delta gna33 mutant: proteomic and immunological comparison with detergent-derived outer membrane vesicles
    • Ferrari G., Garaguso I., Adu-Bobie J., Doro F., Taddei A.R., Biolchi A., et al. Outer membrane vesicles from group B Neisseria meningitidis delta gna33 mutant: proteomic and immunological comparison with detergent-derived outer membrane vesicles. Proteomics 2006, 6(6):1856-1866.
    • (2006) Proteomics , vol.6 , Issue.6 , pp. 1856-1866
    • Ferrari, G.1    Garaguso, I.2    Adu-Bobie, J.3    Doro, F.4    Taddei, A.R.5    Biolchi, A.6
  • 17
    • 33745232494 scopus 로고    scopus 로고
    • The ionic interaction of Klebsiella pneumoniae K2 capsule and core lipopolysaccharide
    • Fresno S., Jimenez N., Izquierdo L., Merino S., Corsaro M.M., De Castro C., et al. The ionic interaction of Klebsiella pneumoniae K2 capsule and core lipopolysaccharide. Microbiology 2006, 152(Pt 6):1807-1818.
    • (2006) Microbiology , vol.152 , pp. 1807-1818
    • Fresno, S.1    Jimenez, N.2    Izquierdo, L.3    Merino, S.4    Corsaro, M.M.5    De Castro, C.6
  • 18
    • 23044448465 scopus 로고    scopus 로고
    • The role of galacturonic acid in outer membrane stability in Klebsiella pneumoniae
    • Frirdich E., Bouwman C., Vinogradov E., Whitfield C. The role of galacturonic acid in outer membrane stability in Klebsiella pneumoniae. J Biol Chem 2005, 280(30):27604-27612.
    • (2005) J Biol Chem , vol.280 , Issue.30 , pp. 27604-27612
    • Frirdich, E.1    Bouwman, C.2    Vinogradov, E.3    Whitfield, C.4
  • 19
    • 0031692318 scopus 로고    scopus 로고
    • Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model
    • Garduno R.A., Garduno E., Hoffman P.S. Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model. Infect Immun 1998, 66(10):4602-4610.
    • (1998) Infect Immun , vol.66 , Issue.10 , pp. 4602-4610
    • Garduno, R.A.1    Garduno, E.2    Hoffman, P.S.3
  • 20
    • 79961239912 scopus 로고    scopus 로고
    • Small RNAs endow a transcriptional activator with essential repressor functions for single-tier control of a global stress regulon
    • Gogol E.B., Rhodius V.A., Papenfort K., Vogel J., Gross C.A. Small RNAs endow a transcriptional activator with essential repressor functions for single-tier control of a global stress regulon. Proc Natl Acad Sci U S A 2011, 108(31):12875-12880.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.31 , pp. 12875-12880
    • Gogol, E.B.1    Rhodius, V.A.2    Papenfort, K.3    Vogel, J.4    Gross, C.A.5
  • 21
    • 0037072819 scopus 로고    scopus 로고
    • Pore formation and function of phosphoporin PhoE of Escherichia coli are determined by the core sugar moiety of lipopolysaccharide
    • Hagge S.O., de Cock H., Gutsmann T., Beckers F., Seydel U., Wiese A. Pore formation and function of phosphoporin PhoE of Escherichia coli are determined by the core sugar moiety of lipopolysaccharide. J Biol Chem 2002, 277(37):34247-34253.
    • (2002) J Biol Chem , vol.277 , Issue.37 , pp. 34247-34253
    • Hagge, S.O.1    de Cock, H.2    Gutsmann, T.3    Beckers, F.4    Seydel, U.5    Wiese, A.6
  • 22
    • 0032946335 scopus 로고    scopus 로고
    • Klebsiella pneumoniae lipopolysaccharide O typing: revision of prototype strains and O-group distribution among clinical isolates from different sources and countries
    • Hansen D.S., Mestre F., Alberti S., Hernandez-Alles S., Alvarez D., Domenech-Sanchez A., et al. Klebsiella pneumoniae lipopolysaccharide O typing: revision of prototype strains and O-group distribution among clinical isolates from different sources and countries. J Clin Microbiol 1999, 37(1):56-62.
    • (1999) J Clin Microbiol , vol.37 , Issue.1 , pp. 56-62
    • Hansen, D.S.1    Mestre, F.2    Alberti, S.3    Hernandez-Alles, S.4    Alvarez, D.5    Domenech-Sanchez, A.6
  • 23
    • 84921419290 scopus 로고    scopus 로고
    • Prokaryotic membrane vesicles: new insights on biogenesis and biological roles
    • Haurat M.F., Elhenawy W., Feldman M.F. Prokaryotic membrane vesicles: new insights on biogenesis and biological roles. Biol Chem 2014, 396:95-109.
    • (2014) Biol Chem , vol.396 , pp. 95-109
    • Haurat, M.F.1    Elhenawy, W.2    Feldman, M.F.3
  • 25
    • 77950679975 scopus 로고    scopus 로고
    • Localization of proteins in the cell wall of Mycobacterium avium subsp. paratuberculosis K10 by proteomic analysis
    • He Z., De Buck J. Localization of proteins in the cell wall of Mycobacterium avium subsp. paratuberculosis K10 by proteomic analysis. Proteome Sci 2010, 8:21.
    • (2010) Proteome Sci , vol.8 , pp. 21
    • He, Z.1    De Buck, J.2
  • 26
    • 0034724910 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli secretes active heat-labile enterotoxin via outer membrane vesicles
    • Horstman A.L., Kuehn M.J. Enterotoxigenic Escherichia coli secretes active heat-labile enterotoxin via outer membrane vesicles. J Biol Chem 2000, 275(17):12489-12496.
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 12489-12496
    • Horstman, A.L.1    Kuehn, M.J.2
  • 27
    • 84863273999 scopus 로고    scopus 로고
    • Lipopolysaccharide O1 antigen contributes to the virulence in Klebsiella pneumoniae causing pyogenic liver abscess
    • Hsieh P.F., Lin T.L., Yang F.L., Wu M.C., Pan Y.J., Wu S.H., et al. Lipopolysaccharide O1 antigen contributes to the virulence in Klebsiella pneumoniae causing pyogenic liver abscess. PLoS One 2012, 7(3):e33155.
    • (2012) PLoS One , vol.7 , Issue.3 , pp. e33155
    • Hsieh, P.F.1    Lin, T.L.2    Yang, F.L.3    Wu, M.C.4    Pan, Y.J.5    Wu, S.H.6
  • 28
    • 84892547223 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni
    • Jang K.S., Sweredoski M.J., Graham R.L., Hess S., Clemons W.M. Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni. J Proteomics 2014, 98:90-98.
    • (2014) J Proteomics , vol.98 , pp. 90-98
    • Jang, K.S.1    Sweredoski, M.J.2    Graham, R.L.3    Hess, S.4    Clemons, W.M.5
  • 29
    • 0029009438 scopus 로고
    • Virulence factors are released from Pseudomonas aeruginosa in association with membrane vesicles during normal growth and exposure to gentamicin: a novel mechanism of enzyme secretion
    • Kadurugamuwa J.L., Beveridge T.J. Virulence factors are released from Pseudomonas aeruginosa in association with membrane vesicles during normal growth and exposure to gentamicin: a novel mechanism of enzyme secretion. J Bacteriol 1995, 177(14):3998-4008.
    • (1995) J Bacteriol , vol.177 , Issue.14 , pp. 3998-4008
    • Kadurugamuwa, J.L.1    Beveridge, T.J.2
  • 30
    • 0027313566 scopus 로고
    • Surface action of gentamicin on Pseudomonas aeruginosa
    • Kadurugamuwa J.L., Clarke A.J., Beveridge T.J. Surface action of gentamicin on Pseudomonas aeruginosa. J Bacteriol 1993, 175(18):5798-5805.
    • (1993) J Bacteriol , vol.175 , Issue.18 , pp. 5798-5805
    • Kadurugamuwa, J.L.1    Clarke, A.J.2    Beveridge, T.J.3
  • 31
    • 77957351822 scopus 로고    scopus 로고
    • Profiling the outer membrane proteome during growth and development of the social bacterium Myxococcus xanthus by selective biotinylation and analyses of outer membrane vesicles
    • Kahnt J., Aguiluz K., Koch J., Treuner-Lange A., Konovalova A., Huntley S., et al. Profiling the outer membrane proteome during growth and development of the social bacterium Myxococcus xanthus by selective biotinylation and analyses of outer membrane vesicles. J Proteome Res 2010, 9(10):5197-5208.
    • (2010) J Proteome Res , vol.9 , Issue.10 , pp. 5197-5208
    • Kahnt, J.1    Aguiluz, K.2    Koch, J.3    Treuner-Lange, A.4    Konovalova, A.5    Huntley, S.6
  • 32
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 2002, 74(20):5383-5392.
    • (2002) Anal Chem , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 33
    • 77957959533 scopus 로고    scopus 로고
    • Biological functions and biogenesis of secreted bacterial outer membrane vesicles
    • Kulp A., Kuehn M.J. Biological functions and biogenesis of secreted bacterial outer membrane vesicles. Annu Rev Microbiol 2010, 64:163-184.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 163-184
    • Kulp, A.1    Kuehn, M.J.2
  • 34
    • 68249144375 scopus 로고    scopus 로고
    • Proteome analysis of outer membrane vesicles from a clinical Acinetobacter baumannii isolate
    • Kwon S.O., Gho Y.S., Lee J.C., Kim S.I. Proteome analysis of outer membrane vesicles from a clinical Acinetobacter baumannii isolate. FEMS Microbiol Lett 2009, 297(2):150-156.
    • (2009) FEMS Microbiol Lett , vol.297 , Issue.2 , pp. 150-156
    • Kwon, S.O.1    Gho, Y.S.2    Lee, J.C.3    Kim, S.I.4
  • 35
    • 84885466975 scopus 로고    scopus 로고
    • Comparative proteome analysis of spontaneous outer membrane vesicles and purified outer membranes of Neisseria meningitidis
    • Lappann M., Otto A., Becher D., Vogel U. Comparative proteome analysis of spontaneous outer membrane vesicles and purified outer membranes of Neisseria meningitidis. J Bacteriol 2013, 195(19):4425-4435.
    • (2013) J Bacteriol , vol.195 , Issue.19 , pp. 4425-4435
    • Lappann, M.1    Otto, A.2    Becher, D.3    Vogel, U.4
  • 36
    • 57249108238 scopus 로고    scopus 로고
    • Proteomics in gram-negative bacterial outer membrane vesicles
    • Lee E.Y., Choi D.S., Kim K.P., Gho Y.S. Proteomics in gram-negative bacterial outer membrane vesicles. Mass Spectrom Rev 2008, 27(6):535-555.
    • (2008) Mass Spectrom Rev , vol.27 , Issue.6 , pp. 535-555
    • Lee, E.Y.1    Choi, D.S.2    Kim, K.P.3    Gho, Y.S.4
  • 37
    • 34748828756 scopus 로고    scopus 로고
    • Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli
    • Lee E.Y., Bang J.Y., Park G.W., Choi D.S., Kang J.S., Kim H.J., et al. Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli. Proteomics 2007, 7(17):3143-3153.
    • (2007) Proteomics , vol.7 , Issue.17 , pp. 3143-3153
    • Lee, E.Y.1    Bang, J.Y.2    Park, G.W.3    Choi, D.S.4    Kang, J.S.5    Kim, H.J.6
  • 38
    • 84860434231 scopus 로고    scopus 로고
    • Klebsiella pneumoniae secretes outer membrane vesicles that induce the innate immune response
    • Lee J.C., Lee E.J., Lee J.H., Jun S.H., Choi C.W., Kim S.I., et al. Klebsiella pneumoniae secretes outer membrane vesicles that induce the innate immune response. FEMS Microbiol Lett 2012, 331(1):17-24.
    • (2012) FEMS Microbiol Lett , vol.331 , Issue.1 , pp. 17-24
    • Lee, J.C.1    Lee, E.J.2    Lee, J.H.3    Jun, S.H.4    Choi, C.W.5    Kim, S.I.6
  • 40
    • 84892779367 scopus 로고    scopus 로고
    • Heat shock transcription factor sigma32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli
    • Lim B., Miyazaki R., Neher S., Siegele D.A., Ito K., Walter P., et al. Heat shock transcription factor sigma32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli. PLoS Biol 2013, 11(12):e1001735.
    • (2013) PLoS Biol , vol.11 , Issue.12 , pp. e1001735
    • Lim, B.1    Miyazaki, R.2    Neher, S.3    Siegele, D.A.4    Ito, K.5    Walter, P.6
  • 41
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25(4):402-408.
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 42
    • 33846037385 scopus 로고    scopus 로고
    • Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response
    • McBroom A.J., Kuehn M.J. Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response. Mol Microbiol 2007, 63(2):545-558.
    • (2007) Mol Microbiol , vol.63 , Issue.2 , pp. 545-558
    • McBroom, A.J.1    Kuehn, M.J.2
  • 43
    • 84874729284 scopus 로고    scopus 로고
    • Lipopolysaccharide-deficient Acinetobacter baumannii shows altered signaling through host Toll-like receptors and increased susceptibility to the host antimicrobial peptide LL-37
    • Moffatt J.H., Harper M., Mansell A., Crane B., Fitzsimons T.C., Nation R.L., et al. Lipopolysaccharide-deficient Acinetobacter baumannii shows altered signaling through host Toll-like receptors and increased susceptibility to the host antimicrobial peptide LL-37. Infect Immun 2013, 81(3):684-689.
    • (2013) Infect Immun , vol.81 , Issue.3 , pp. 684-689
    • Moffatt, J.H.1    Harper, M.2    Mansell, A.3    Crane, B.4    Fitzsimons, T.C.5    Nation, R.L.6
  • 44
    • 84895760980 scopus 로고    scopus 로고
    • Influence of O polysaccharides on biofilm development and outer membrane vesicle biogenesis in Pseudomonas aeruginosa PAO1
    • Murphy K., Park A.J., Hao Y., Brewer D., Lam J.S., Khursigara C.M. Influence of O polysaccharides on biofilm development and outer membrane vesicle biogenesis in Pseudomonas aeruginosa PAO1. J Bacteriol 2014, 196(7):1306-1317.
    • (2014) J Bacteriol , vol.196 , Issue.7 , pp. 1306-1317
    • Murphy, K.1    Park, A.J.2    Hao, Y.3    Brewer, D.4    Lam, J.S.5    Khursigara, C.M.6
  • 45
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I., Keller A., Kolker E., Aebersold R. A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 2003, 75(17):4646-4658.
    • (2003) Anal Chem , vol.75 , Issue.17 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 46
    • 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 2003, 67(4):593-656.
    • (2003) Microbiol Mol Biol Rev , vol.67 , Issue.4 , pp. 593-656
    • Nikaido, H.1
  • 47
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H., Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev 1985, 49(1):1-32.
    • (1985) Microbiol Rev , vol.49 , Issue.1 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 48
    • 62749195559 scopus 로고    scopus 로고
    • The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria
    • Nordmann P., Cuzon G., Naas T. The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria. Lancet Infect Dis 2009, 9(4):228-236.
    • (2009) Lancet Infect Dis , vol.9 , Issue.4 , pp. 228-236
    • Nordmann, P.1    Cuzon, G.2    Naas, T.3
  • 49
    • 33646712560 scopus 로고    scopus 로고
    • Interleukin-6 induction by Helicobacter pylori in human macrophages is dependent on phagocytosis
    • Odenbreit S., Linder S., Gebert-Vogl B., Rieder G., Moran A.P., Haas R. Interleukin-6 induction by Helicobacter pylori in human macrophages is dependent on phagocytosis. Helicobacter 2006, 11(3):196-207.
    • (2006) Helicobacter , vol.11 , Issue.3 , pp. 196-207
    • Odenbreit, S.1    Linder, S.2    Gebert-Vogl, B.3    Rieder, G.4    Moran, A.P.5    Haas, R.6
  • 50
    • 0037399254 scopus 로고    scopus 로고
    • Expression of heterologous O-antigen in Yersinia pestis KIM does not affect virulence by the intravenous route
    • Oyston P.C., Prior J.L., Kiljunen S., Skurnik M., Hill J., Titball R.W. Expression of heterologous O-antigen in Yersinia pestis KIM does not affect virulence by the intravenous route. J Med Microbiol 2003, 52(Pt 4):289-294.
    • (2003) J Med Microbiol , vol.52 , pp. 289-294
    • Oyston, P.C.1    Prior, J.L.2    Kiljunen, S.3    Skurnik, M.4    Hill, J.5    Titball, R.W.6
  • 51
    • 79952418804 scopus 로고    scopus 로고
    • Proteomic characterization and functional analysis of outer membrane vesicles of Francisella novicida suggests possible role in virulence and use as a vaccine
    • Pierson T., Matrakas D., Taylor Y.U., Manyam G., Morozov V.N., Zhou W., et al. Proteomic characterization and functional analysis of outer membrane vesicles of Francisella novicida suggests possible role in virulence and use as a vaccine. J Proteome Res 2010, 10(3):954-967.
    • (2010) J Proteome Res , vol.10 , Issue.3 , pp. 954-967
    • Pierson, T.1    Matrakas, D.2    Taylor, Y.U.3    Manyam, G.4    Morozov, V.N.5    Zhou, W.6
  • 52
    • 79952418804 scopus 로고    scopus 로고
    • Proteomic characterization and functional analysis of outer membrane vesicles of Francisella novicida suggests possible role in virulence and use as a vaccine
    • Pierson T., Matrakas D., Taylor Y.U., Manyam G., Morozov V.N., Zhou W., et al. Proteomic characterization and functional analysis of outer membrane vesicles of Francisella novicida suggests possible role in virulence and use as a vaccine. J Proteome Res 2011, 10(3):954-967.
    • (2011) J Proteome Res , vol.10 , Issue.3 , pp. 954-967
    • Pierson, T.1    Matrakas, D.2    Taylor, Y.U.3    Manyam, G.4    Morozov, V.N.5    Zhou, W.6
  • 53
    • 0031792165 scopus 로고    scopus 로고
    • Klebsiella spp. as nosocomial pathogens: epidemiology, taxonomy, typing methods, and pathogenicity factors
    • Podschun R., Ullmann U. Klebsiella spp. as nosocomial pathogens: epidemiology, taxonomy, typing methods, and pathogenicity factors. Clin Microbiol Rev 1998, 11(4):589-603.
    • (1998) Clin Microbiol Rev , vol.11 , Issue.4 , pp. 589-603
    • Podschun, R.1    Ullmann, U.2
  • 54
    • 77956637819 scopus 로고    scopus 로고
    • Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours via substrate limitation of PqsH
    • Schertzer J.W., Brown S.A., Whiteley M. Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours via substrate limitation of PqsH. Mol Microbiol 2010, 77(6):1527-1538.
    • (2010) Mol Microbiol , vol.77 , Issue.6 , pp. 1527-1538
    • Schertzer, J.W.1    Brown, S.A.2    Whiteley, M.3
  • 55
    • 84877316643 scopus 로고    scopus 로고
    • Envelope control of outer membrane vesicle production in Gram-negative bacteria
    • Schwechheimer C., Sullivan C.J., Kuehn M.J. Envelope control of outer membrane vesicle production in Gram-negative bacteria. Biochemistry 2013, 52(18):3031-3040.
    • (2013) Biochemistry , vol.52 , Issue.18 , pp. 3031-3040
    • Schwechheimer, C.1    Sullivan, C.J.2    Kuehn, M.J.3
  • 56
    • 1342302539 scopus 로고    scopus 로고
    • The Klebsiella pneumoniae O antigen contributes to bacteremia and lethality during murine pneumonia
    • Shankar-Sinha S., Valencia G.A., Janes B.K., Rosenberg J.K., Whitfield C., Bender R.A., et al. The Klebsiella pneumoniae O antigen contributes to bacteremia and lethality during murine pneumonia. Infect Immun 2004, 72(3):1423-1430.
    • (2004) Infect Immun , vol.72 , Issue.3 , pp. 1423-1430
    • Shankar-Sinha, S.1    Valencia, G.A.2    Janes, B.K.3    Rosenberg, J.K.4    Whitfield, C.5    Bender, R.A.6
  • 57
    • 51649090185 scopus 로고    scopus 로고
    • A new Vibrio cholerae sRNA modulates colonization and affects release of outer membrane vesicles
    • Song T., Mika F., Lindmark B., Liu Z., Schild S., Bishop A., et al. A new Vibrio cholerae sRNA modulates colonization and affects release of outer membrane vesicles. Mol Microbiol 2008, 70(1):100-111.
    • (2008) Mol Microbiol , vol.70 , Issue.1 , pp. 100-111
    • Song, T.1    Mika, F.2    Lindmark, B.3    Liu, Z.4    Schild, S.5    Bishop, A.6
  • 58
    • 0018150270 scopus 로고
    • Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins
    • Sonntag I., Schwarz H., Hirota Y., Henning U. Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J Bacteriol 1978, 136(1):280-285.
    • (1978) J Bacteriol , vol.136 , Issue.1 , pp. 280-285
    • Sonntag, I.1    Schwarz, H.2    Hirota, Y.3    Henning, U.4
  • 59
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess C., Beil A., Ehrmann M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 1999, 97(3):339-347.
    • (1999) Cell , vol.97 , Issue.3 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 60
    • 72449173045 scopus 로고    scopus 로고
    • Outer membrane machinery and alginate synthesis regulators control membrane vesicle production in Pseudomonas aeruginosa
    • Tashiro Y., Sakai R., Toyofuku M., Sawada I., Nakajima-Kambe T., Uchiyama H., et al. Outer membrane machinery and alginate synthesis regulators control membrane vesicle production in Pseudomonas aeruginosa. J Bacteriol 2009, 191(24):7509-7519.
    • (2009) J Bacteriol , vol.191 , Issue.24 , pp. 7509-7519
    • Tashiro, Y.1    Sakai, R.2    Toyofuku, M.3    Sawada, I.4    Nakajima-Kambe, T.5    Uchiyama, H.6
  • 61
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • Tatusov R.L., Koonin E.V., Lipman D.J. A genomic perspective on protein families. Science 1997, 278(5338):631-637.
    • (1997) Science , vol.278 , Issue.5338 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 62
    • 33747170862 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of Shigella flexneri 2a membrane proteins
    • Wei C., Yang J., Zhu J., Zhang X., Leng W., Wang J., et al. Comprehensive proteomic analysis of Shigella flexneri 2a membrane proteins. J Proteome Res 2006, 5(8):1860-1865.
    • (2006) J Proteome Res , vol.5 , Issue.8 , pp. 1860-1865
    • Wei, C.1    Yang, J.2    Zhu, J.3    Zhang, X.4    Leng, W.5    Wang, J.6
  • 63
    • 33847764692 scopus 로고    scopus 로고
    • Proteomic analysis of outer membranes and vesicles from wild-type serogroup B Neisseria meningitidis and a lipopolysaccharide-deficient mutant
    • Williams J.N., Skipp P.J., Humphries H.E., Christodoulides M., O'Connor C.D., Heckels J.E. Proteomic analysis of outer membranes and vesicles from wild-type serogroup B Neisseria meningitidis and a lipopolysaccharide-deficient mutant. Infect Immun 2007, 75(3):1364-1372.
    • (2007) Infect Immun , vol.75 , Issue.3 , pp. 1364-1372
    • Williams, J.N.1    Skipp, P.J.2    Humphries, H.E.3    Christodoulides, M.4    O'Connor, C.D.5    Heckels, J.E.6
  • 64
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski J.R., Zougman A., Nagaraj N., Mann M. Universal sample preparation method for proteome analysis. Nat Methods 2009, 6(5):359-362.
    • (2009) Nat Methods , vol.6 , Issue.5 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 65
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu N.Y., Wagner J.R., Laird M.R., Melli G., Rey S., Lo R., et al. PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 2010, 26(13):1608-1615.
    • (2010) Bioinformatics , vol.26 , Issue.13 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6
  • 66
    • 84874980854 scopus 로고    scopus 로고
    • Surface-associated GroEL facilitates the adhesion of Escherichia coli to macrophages through lectin-like oxidized low-density lipoprotein receptor-1
    • Zhu H., Lee C., Zhang D., Wu W., Wang L., Fang X., et al. Surface-associated GroEL facilitates the adhesion of Escherichia coli to macrophages through lectin-like oxidized low-density lipoprotein receptor-1. Microbes Infect 2013, 15(3):172-180.
    • (2013) Microbes Infect , vol.15 , Issue.3 , pp. 172-180
    • Zhu, H.1    Lee, C.2    Zhang, D.3    Wu, W.4    Wang, L.5    Fang, X.6
  • 67
    • 84899747821 scopus 로고    scopus 로고
    • Quantitative proteomics of the Neisseria gonorrhoeae cell envelope and membrane vesicles for the discovery of potential therapeutic targets
    • Zielke R.A., Wierzbicki I.H., Weber J.V., Gafken P.R., Sikora A.E. Quantitative proteomics of the Neisseria gonorrhoeae cell envelope and membrane vesicles for the discovery of potential therapeutic targets. Mol Cell Proteomics 2014, 13(5):1299-1317.
    • (2014) Mol Cell Proteomics , vol.13 , Issue.5 , pp. 1299-1317
    • Zielke, R.A.1    Wierzbicki, I.H.2    Weber, J.V.3    Gafken, P.R.4    Sikora, A.E.5


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