메뉴 건너뛰기




Volumn 92, Issue 1, 2014, Pages 116-137

A general protein O-glycosylation system within the Burkholderia cepacia complex is involved in motility and virulence

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL GLYCOPROTEIN; BACTERIAL PROTEIN; O OLIGOSACCHARYLTRANSFERASE PGLL; UNCLASSIFIED DRUG; GLYCOPROTEIN; O ANTIGEN; TRANSFERASE; TRISACCHARIDE;

EID: 84897111790     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12540     Document Type: Article
Times cited : (50)

References (92)
  • 2
    • 84870861469 scopus 로고    scopus 로고
    • An extended spectrum of target proteins and modification sites in the general O-linked protein glycosylation system in Neisseria gonorrhoeae
    • Anonsen, J.H., Vik, Å., Egge-Jacobsen, W., and Koomey, M. (2012) An extended spectrum of target proteins and modification sites in the general O-linked protein glycosylation system in Neisseria gonorrhoeae. J Proteome Res 11: 5781-5793.
    • (2012) J Proteome Res , vol.11 , pp. 5781-5793
    • Anonsen, J.H.1    Vik, A.2    Egge-Jacobsen, W.3    Koomey, M.4
  • 3
    • 84863798364 scopus 로고    scopus 로고
    • Characterization of protein glycosylation in Francisella tularensis subsp. holarctica: identification of a novel glycosylated lipoprotein required for virulence
    • Balonova, L., Mann, B.F., Cerveny, L., Alley, W.R., Chovancova, E., Forslund, A.-L., etal. (2012) Characterization of protein glycosylation in Francisella tularensis subsp. holarctica: identification of a novel glycosylated lipoprotein required for virulence. Mol Cell Proteomics 11: M111.015016.
    • (2012) Mol Cell Proteomics , vol.11
    • Balonova, L.1    Mann, B.F.2    Cerveny, L.3    Alley, W.R.4    Chovancova, E.5    Forslund, A.-L.6
  • 4
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema, P.J., Raijmakers, R., Lemeer, S., Mohammed, S., and Heck, A.J.R. (2009) Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat Protocols 4: 484-494.
    • (2009) Nat Protocols , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.R.5
  • 5
    • 0000170541 scopus 로고
    • Sour skin, a bacterial rot of onion bulbs
    • Burkholder, W.H. (1950) Sour skin, a bacterial rot of onion bulbs. Phytopathology 40: 115-117.
    • (1950) Phytopathology , vol.40 , pp. 115-117
    • Burkholder, W.H.1
  • 6
    • 34548273058 scopus 로고    scopus 로고
    • The tomato rhizosphere, an environment rich in nitrogen-fixing Burkholderia species with capabilities of interest for agriculture and bioremediation
    • Caballero-Mellado, J., Onofre-Lemus, J., Estrada-de Los Santos, P., and Martínez-Aguilar, L. (2007) The tomato rhizosphere, an environment rich in nitrogen-fixing Burkholderia species with capabilities of interest for agriculture and bioremediation. Appl Environ Microbiol 73: 5308-5319.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 5308-5319
    • Caballero-Mellado, J.1    Onofre-Lemus, J.2    Estrada-de Los Santos, P.3    Martínez-Aguilar, L.4
  • 7
    • 27144454305 scopus 로고    scopus 로고
    • An expression vector containing a rhamnose-inducible promoter provides tightly regulated gene expression in Burkholderia cenocepacia
    • Cardona, S.T., and Valvano, M.A. (2005) An expression vector containing a rhamnose-inducible promoter provides tightly regulated gene expression in Burkholderia cenocepacia. Plasmid 54: 219-228.
    • (2005) Plasmid , vol.54 , pp. 219-228
    • Cardona, S.T.1    Valvano, M.A.2
  • 8
    • 0028988630 scopus 로고
    • pilO, a gene required for glycosylation of Pseudomonas aeruginosa 1244 pilin
    • Castric, P. (1995) pilO, a gene required for glycosylation of Pseudomonas aeruginosa 1244 pilin. Microbiology 141: 1247-1254.
    • (1995) Microbiology , vol.141 , pp. 1247-1254
    • Castric, P.1
  • 9
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A.C., and Cohen, S.N. (1978) Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol 134: 1141-1156.
    • (1978) J Bacteriol , vol.134 , pp. 1141-1156
    • Chang, A.C.1    Cohen, S.N.2
  • 10
    • 0034799341 scopus 로고    scopus 로고
    • Taxonomy and identification of the Burkholderia cepacia complex
    • Coenye, T., Vandamme, P., Govan, J.R.W., and LiPuma, J.J. (2001) Taxonomy and identification of the Burkholderia cepacia complex. J Clin Microbiol 39: 3427-3436.
    • (2001) J Clin Microbiol , vol.39 , pp. 3427-3436
    • Coenye, T.1    Vandamme, P.2    Govan, J.R.W.3    LiPuma, J.J.4
  • 11
    • 15244340417 scopus 로고    scopus 로고
    • Human symbionts use a host-like pathway for surface fucosylation
    • Coyne, M.J., Reinap, B., Lee, M.M., and Comstock, L.E. (2005) Human symbionts use a host-like pathway for surface fucosylation. Science 307: 1778-1781.
    • (2005) Science , vol.307 , pp. 1778-1781
    • Coyne, M.J.1    Reinap, B.2    Lee, M.M.3    Comstock, L.E.4
  • 12
    • 0024446387 scopus 로고
    • A plasmid which can be transferred between Escherichia coli and Pasteurella haemolytica by electroporation and conjugation
    • Craig, F.F., Coote, J.G., Parton, R., Freer, J.H., and Gilmour, N.J. (1989) A plasmid which can be transferred between Escherichia coli and Pasteurella haemolytica by electroporation and conjugation. J Gen Microbiol 135: 2885-2890.
    • (1989) J Gen Microbiol , vol.135 , pp. 2885-2890
    • Craig, F.F.1    Coote, J.G.2    Parton, R.3    Freer, J.H.4    Gilmour, N.J.5
  • 13
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: a sequence logo generator
    • Crooks, G.E. (2004) WebLogo: a sequence logo generator. Genome Res 14: 1188-1190.
    • (2004) Genome Res , vol.14 , pp. 1188-1190
    • Crooks, G.E.1
  • 14
    • 0029190247 scopus 로고
    • Electrotransformation of Pseudomonas
    • Dennis, J.J., and Sokol, P.A. (1995) Electrotransformation of Pseudomonas. Methods Mol Biol 47: 125-133.
    • (1995) Methods Mol Biol , vol.47 , pp. 125-133
    • Dennis, J.J.1    Sokol, P.A.2
  • 15
    • 0031869639 scopus 로고    scopus 로고
    • Plasposons: modular self-cloning minitransposon derivatives for rapid genetic analysis of gram-negative bacterial genomes
    • Dennis, J.J., and Zylstra, G.J. (1998) Plasposons: modular self-cloning minitransposon derivatives for rapid genetic analysis of gram-negative bacterial genomes. Appl Environ Microbiol 64: 2710-2715.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2710-2715
    • Dennis, J.J.1    Zylstra, G.J.2
  • 17
    • 0030600480 scopus 로고    scopus 로고
    • A set of compatible tac promoter expression vectors
    • Dykxhoorn, D.M., St. Pierre, R., and Linn, T. (1996) A set of compatible tac promoter expression vectors. Gene 177: 133-136.
    • (1996) Gene , vol.177 , pp. 133-136
    • Dykxhoorn, D.M.1    St Pierre, R.2    Linn, T.3
  • 18
    • 80053602806 scopus 로고    scopus 로고
    • O-linked glycosylation of the PilA pilin protein of Francisella tularensis: identification of the endogenous protein-targeting oligosaccharyltransferase and characterization of the native oligosaccharide
    • Egge-Jacobsen, W., Salomonsson, E.N., Aas, F.E., Forslund, A.L., Winther-Larsen, H.C., Maier, J., etal. (2011) O-linked glycosylation of the PilA pilin protein of Francisella tularensis: identification of the endogenous protein-targeting oligosaccharyltransferase and characterization of the native oligosaccharide. J Bacteriol 193: 5487-5497.
    • (2011) J Bacteriol , vol.193 , pp. 5487-5497
    • Egge-Jacobsen, W.1    Salomonsson, E.N.2    Aas, F.E.3    Forslund, A.L.4    Winther-Larsen, H.C.5    Maier, J.6
  • 19
    • 58049214870 scopus 로고    scopus 로고
    • Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation
    • Faridmoayer, A., Fentabil, M.A., Haurat, M.F., Yi, W., Woodward, R., Wang, P.G., and Feldman, M.F. (2008) Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation. J Biol Chem 283: 34596-34604.
    • (2008) J Biol Chem , vol.283 , pp. 34596-34604
    • Faridmoayer, A.1    Fentabil, M.A.2    Haurat, M.F.3    Yi, W.4    Woodward, R.5    Wang, P.G.6    Feldman, M.F.7
  • 20
    • 84880069216 scopus 로고    scopus 로고
    • The exopolysaccharide gene cluster Bcam1330-Bcam1341 is involved in Burkholderia cenocepacia biofilm formation, and its expression is regulated by c-di-GMP and Bcam1349
    • Fazli, M., McCarthy, Y., Givskov, M., Ryan, R.P., and Tolker-Nielsen, T. (2013) The exopolysaccharide gene cluster Bcam1330-Bcam1341 is involved in Burkholderia cenocepacia biofilm formation, and its expression is regulated by c-di-GMP and Bcam1349. Microbiologyopen 2: 105-122.
    • (2013) Microbiologyopen , vol.2 , pp. 105-122
    • Fazli, M.1    McCarthy, Y.2    Givskov, M.3    Ryan, R.P.4    Tolker-Nielsen, T.5
  • 21
    • 20044393802 scopus 로고    scopus 로고
    • Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli
    • Feldman, M.F., Wacker, M., Hernandez, M., Hitchen, P.G., Marolda, C.L., Kowarik, M., etal. (2005) Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli. Proc Natl Acad Sci USA 102: 3016-3021.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3016-3021
    • Feldman, M.F.1    Wacker, M.2    Hernandez, M.3    Hitchen, P.G.4    Marolda, C.L.5    Kowarik, M.6
  • 22
    • 64249095086 scopus 로고    scopus 로고
    • A general O-glycosylation system important to the physiology of a major human intestinal symbiont
    • Fletcher, C.M., Coyne, M.J., Villa, O.F., Chatzidaki-Livanis, M., and Comstock, L.E. (2009) A general O-glycosylation system important to the physiology of a major human intestinal symbiont. Cell 137: 321-331.
    • (2009) Cell , vol.137 , pp. 321-331
    • Fletcher, C.M.1    Coyne, M.J.2    Villa, O.F.3    Chatzidaki-Livanis, M.4    Comstock, L.E.5
  • 23
    • 79952797070 scopus 로고    scopus 로고
    • Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis
    • Fletcher, C.M., Coyne, M.J., and Comstock, L.E. (2011) Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis. J Biol Chem 286: 3219-3226.
    • (2011) J Biol Chem , vol.286 , pp. 3219-3226
    • Fletcher, C.M.1    Coyne, M.J.2    Comstock, L.E.3
  • 25
    • 84861416540 scopus 로고    scopus 로고
    • Characterization of exogenous bacterial oligosaccharyltransferases in Escherichia coli reveals the potential for O-linked protein glycosylation in Vibrio cholerae and Burkholderia thailandensis
    • Gebhart, C., Ielmini, M.V., Reiz, B., Price, N.L., Aas, F.E., Koomey, M., and Feldman, M.F. (2012) Characterization of exogenous bacterial oligosaccharyltransferases in Escherichia coli reveals the potential for O-linked protein glycosylation in Vibrio cholerae and Burkholderia thailandensis. Glycobiology 22: 962-974.
    • (2012) Glycobiology , vol.22 , pp. 962-974
    • Gebhart, C.1    Ielmini, M.V.2    Reiz, B.3    Price, N.L.4    Aas, F.E.5    Koomey, M.6    Feldman, M.F.7
  • 26
    • 0142030034 scopus 로고    scopus 로고
    • Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene
    • Goon, S., Kelly, J.F., Logan, S.M., Ewing, C.P., and Guerry, P. (2003) Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene. Mol Microbiol 50: 659-671.
    • (2003) Mol Microbiol , vol.50 , pp. 659-671
    • Goon, S.1    Kelly, J.F.2    Logan, S.M.3    Ewing, C.P.4    Guerry, P.5
  • 27
    • 0027266917 scopus 로고
    • Evidence for transmission of Pseudomonas cepacia by social contact in cystic fibrosis
    • Govan, J.R., Brown, P.H., Maddison, J., Doherty, C.J., Nelson, J.W., Dodd, M., etal. (1993) Evidence for transmission of Pseudomonas cepacia by social contact in cystic fibrosis. Lancet 342: 15-19.
    • (1993) Lancet , vol.342 , pp. 15-19
    • Govan, J.R.1    Brown, P.H.2    Maddison, J.3    Doherty, C.J.4    Nelson, J.W.5    Dodd, M.6
  • 28
    • 33645293731 scopus 로고    scopus 로고
    • Changes in flagellin glycosylation affect Campylobacter autoagglutination and virulence
    • Guerry, P., Ewing, C.P., Schirm, M., Lorenzo, M., Kelly, J., Pattarini, D., etal. (2006) Changes in flagellin glycosylation affect Campylobacter autoagglutination and virulence. Mol Microbiol 60: 299-311.
    • (2006) Mol Microbiol , vol.60 , pp. 299-311
    • Guerry, P.1    Ewing, C.P.2    Schirm, M.3    Lorenzo, M.4    Kelly, J.5    Pattarini, D.6
  • 29
    • 34247210823 scopus 로고    scopus 로고
    • Microbial ecology of the cystic fibrosis lung
    • Harrison, F. (2007) Microbial ecology of the cystic fibrosis lung. Microbiology 153: 917-923.
    • (2007) Microbiology , vol.153 , pp. 917-923
    • Harrison, F.1
  • 30
    • 3242663192 scopus 로고    scopus 로고
    • Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili
    • Hegge, F.T., Hitchen, P.G., Aas, F.E., Kristiansen, H., Løvold, C., Egge-Jacobsen, W., etal. (2004) Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili. Proc Natl Acad Sci USA 101: 10798-10803.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10798-10803
    • Hegge, F.T.1    Hitchen, P.G.2    Aas, F.E.3    Kristiansen, H.4    Løvold, C.5    Egge-Jacobsen, W.6
  • 31
    • 0018556564 scopus 로고
    • In vitro packaging of lambda and cosmid DNA
    • Hohn, B. (1979) In vitro packaging of lambda and cosmid DNA. Methods Enzymol 68: 299-309.
    • (1979) Methods Enzymol , vol.68 , pp. 299-309
    • Hohn, B.1
  • 32
    • 79951966895 scopus 로고    scopus 로고
    • Analogies and homologies in lipopolysaccharide and glycoprotein biosynthesis in bacteria
    • Hug, I., and Feldman, M.F. (2011) Analogies and homologies in lipopolysaccharide and glycoprotein biosynthesis in bacteria. Glycobiolog 21: 138-151.
    • (2011) Glycobiolog , vol.21 , pp. 138-151
    • Hug, I.1    Feldman, M.F.2
  • 33
    • 33645774852 scopus 로고    scopus 로고
    • Modular stop and go extraction tips with stacked disks for parallel and multidimensional peptide fractionation in proteomics
    • Ishihama, Y., Rappsilber, J., and Mann, M. (2006) Modular stop and go extraction tips with stacked disks for parallel and multidimensional peptide fractionation in proteomics. J Proteome Res 5: 988-994.
    • (2006) J Proteome Res , vol.5 , pp. 988-994
    • Ishihama, Y.1    Rappsilber, J.2    Mann, M.3
  • 34
    • 84864072948 scopus 로고    scopus 로고
    • Identification of a general O-linked protein glycosylation system in Acinetobacter baumannii and its role in virulence and biofilm formation
    • Iwashkiw, J.A., Seper, A., Weber, B.S., Scott, N.E., Vinogradov, E., Stratilo, C., etal. (2012) Identification of a general O-linked protein glycosylation system in Acinetobacter baumannii and its role in virulence and biofilm formation. PLoS Pathog 8: e1002758.
    • (2012) PLoS Pathog , vol.8
    • Iwashkiw, J.A.1    Seper, A.2    Weber, B.S.3    Scott, N.E.4    Vinogradov, E.5    Stratilo, C.6
  • 35
    • 84879506906 scopus 로고    scopus 로고
    • Pour some sugar on it: the expanding world of bacterial protein O-linked glycosylation
    • Iwashkiw, J.A., Vozza, N.F., Kinsella, R.L., and Feldman, M.F. (2013) Pour some sugar on it: the expanding world of bacterial protein O-linked glycosylation. Mol Microbiol 89: 14-28.
    • (2013) Mol Microbiol , vol.89 , pp. 14-28
    • Iwashkiw, J.A.1    Vozza, N.F.2    Kinsella, R.L.3    Feldman, M.F.4
  • 36
    • 84878514516 scopus 로고    scopus 로고
    • Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells
    • Jen, F.E.-C., Warren, M.J., Schulz, B.L., Power, P.M., Swords, W.E., Weiser, J.N., etal. (2013) Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells. PLoS Pathog 9: e1003377.
    • (2013) PLoS Pathog , vol.9
    • Jen, F.-C.1    Warren, M.J.2    Schulz, B.L.3    Power, P.M.4    Swords, W.E.5    Weiser, J.N.6
  • 37
    • 79955980572 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae pilin glycan contributes to CR3 activation during challenge of primary cervical epithelial cells
    • Jennings, M.P., Jen, F.E.-C., Roddam, L.F., Apicella, M.A., and Edwards, J.L. (2011) Neisseria gonorrhoeae pilin glycan contributes to CR3 activation during challenge of primary cervical epithelial cells. Cell Microbiol 13: 885-896.
    • (2011) Cell Microbiol , vol.13 , pp. 885-896
    • Jennings, M.P.1    Jen, F.-C.2    Roddam, L.F.3    Apicella, M.A.4    Edwards, J.L.5
  • 38
    • 0037035408 scopus 로고    scopus 로고
    • The neuA/flmD gene cluster of Helicobacter pylori is involved in flagellar biosynthesis and flagellin glycosylation
    • Josenhans, C., Vossebein, L., Friedrich, S., and Suerbaum, S. (2002) The neuA/flmD gene cluster of Helicobacter pylori is involved in flagellar biosynthesis and flagellin glycosylation. FEMS Microbiol Lett 210: 165-172.
    • (2002) FEMS Microbiol Lett , vol.210 , pp. 165-172
    • Josenhans, C.1    Vossebein, L.2    Friedrich, S.3    Suerbaum, S.4
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, UK
    • Laemmli, UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
  • 40
    • 4544254484 scopus 로고    scopus 로고
    • N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176
    • Larsen, J.C., Szymanski, C., and Guerry, P. (2004) N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176. J Bacteriol 186: 6508-6514.
    • (2004) J Bacteriol , vol.186 , pp. 6508-6514
    • Larsen, J.C.1    Szymanski, C.2    Guerry, P.3
  • 41
    • 84883176518 scopus 로고    scopus 로고
    • A common pathway for O-linked protein-glycosylation and synthesis of capsule in Acinetobacter baumannii
    • Lees-Miller, R.G., Iwashkiw, J.A., Scott, N.E., Seper, A., Vinogradov, E., Schild, S., etal. (2013) A common pathway for O-linked protein-glycosylation and synthesis of capsule in Acinetobacter baumannii. Mol Microbiol 89: 816-830.
    • (2013) Mol Microbiol , vol.89 , pp. 816-830
    • Lees-Miller, R.G.1    Iwashkiw, J.A.2    Scott, N.E.3    Seper, A.4    Vinogradov, E.5    Schild, S.6
  • 42
    • 0036955925 scopus 로고    scopus 로고
    • Construction and evaluation of plasmid vectors optimized for constitutive and regulated gene expression in Burkholderia cepacia complex isolates
    • Lefebre, M.D., and Valvano, M.A. (2002) Construction and evaluation of plasmid vectors optimized for constitutive and regulated gene expression in Burkholderia cepacia complex isolates. Appl Environ Microbiol 68: 5956-5964.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 5956-5964
    • Lefebre, M.D.1    Valvano, M.A.2
  • 44
    • 20244371925 scopus 로고    scopus 로고
    • Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway
    • Linton, D., Dorrell, N., Hitchen, P.G., Amber, S., Karlyshev, A.V., Morris, H.R., etal. (2005) Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway. Mol Microbiol 55: 1695-1703.
    • (2005) Mol Microbiol , vol.55 , pp. 1695-1703
    • Linton, D.1    Dorrell, N.2    Hitchen, P.G.3    Amber, S.4    Karlyshev, A.V.5    Morris, H.R.6
  • 45
    • 0025116483 scopus 로고
    • Person-to-person transmission of Pseudomonas cepacia between patients with cystic fibrosis
    • LiPuma, J.J., Dasen, S.E., Nielson, D.W., Stern, R.C., and Stull, T.L. (1990) Person-to-person transmission of Pseudomonas cepacia between patients with cystic fibrosis. Lancet 336: 1094-1096.
    • (1990) Lancet , vol.336 , pp. 1094-1096
    • LiPuma, J.J.1    Dasen, S.E.2    Nielson, D.W.3    Stern, R.C.4    Stull, T.L.5
  • 46
    • 77957726305 scopus 로고    scopus 로고
    • A decade of Burkholderia cenocepacia virulence determinant research
    • Loutet, S.A., and Valvano, M.A. (2010) A decade of Burkholderia cenocepacia virulence determinant research. Infect Immun 78: 4088-4100.
    • (2010) Infect Immun , vol.78 , pp. 4088-4100
    • Loutet, S.A.1    Valvano, M.A.2
  • 47
    • 0033950408 scopus 로고    scopus 로고
    • Diagnostically and experimentally useful panel of strains from the Burkholderia cepacia complex
    • Mahenthiralingam, E., Coenye, T., Chung, J.W., Speert, D.P., Govan, J.R., Taylor, P., etal. (2000) Diagnostically and experimentally useful panel of strains from the Burkholderia cepacia complex. J Clin Microbiol 38: 910-913.
    • (2000) J Clin Microbiol , vol.38 , pp. 910-913
    • Mahenthiralingam, E.1    Coenye, T.2    Chung, J.W.3    Speert, D.P.4    Govan, J.R.5    Taylor, P.6
  • 48
    • 13444251656 scopus 로고    scopus 로고
    • The multifarious, multireplicon Burkholderia cepacia complex
    • Mahenthiralingam, E., Urban, T.A., and Goldberg, J.B. (2005) The multifarious, multireplicon Burkholderia cepacia complex. Nat Rev Microbiol 3: 144-156.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 144-156
    • Mahenthiralingam, E.1    Urban, T.A.2    Goldberg, J.B.3
  • 49
    • 34147137522 scopus 로고    scopus 로고
    • Micromethods for the characterization of lipid A-core and O-antigen lipopolysaccharide
    • Marolda, C.L., Lahiry, P., Vinés, E., Saldías, S., and Valvano, M.A. (2006) Micromethods for the characterization of lipid A-core and O-antigen lipopolysaccharide. Methods Mol Biol 347: 237-252.
    • (2006) Methods Mol Biol , vol.347 , pp. 237-252
    • Marolda, C.L.1    Lahiry, P.2    Vinés, E.3    Saldías, S.4    Valvano, M.A.5
  • 50
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama, S.I., Yokota, N., and Tokuda, H. (1997) A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. EMBO J 16: 6947-6955.
    • (1997) EMBO J , vol.16 , pp. 6947-6955
    • Matsuyama, S.I.1    Yokota, N.2    Tokuda, H.3
  • 51
    • 36849069564 scopus 로고    scopus 로고
    • Glycosylation of the OMP85 homolog of Porphyromonas gingivalis and its involvement in biofilm formation
    • Nakao, R., Tashiro, Y., Nomura, N., Kosono, S., Ochiai, K., Yonezawa, H., etal. (2008) Glycosylation of the OMP85 homolog of Porphyromonas gingivalis and its involvement in biofilm formation. Biochem Biophys Res Commun 365: 784-789.
    • (2008) Biochem Biophys Res Commun , vol.365 , pp. 784-789
    • Nakao, R.1    Tashiro, Y.2    Nomura, N.3    Kosono, S.4    Ochiai, K.5    Yonezawa, H.6
  • 52
    • 84868336980 scopus 로고    scopus 로고
    • Expert system for computer-assisted annotation of MS/MS spectra
    • Neuhauser, N., Michalski, A., Cox, J., and Mann, M. (2012) Expert system for computer-assisted annotation of MS/MS spectra. Mol Cell Proteomics 11: 1500-1509.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1500-1509
    • Neuhauser, N.1    Michalski, A.2    Cox, J.3    Mann, M.4
  • 53
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: sweeter than ever
    • Nothaft, H., and Szymanski, C.M. (2010) Protein glycosylation in bacteria: sweeter than ever. Nat Rev Microbiol 8: 765-778.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 54
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in Bacteria
    • Okuda, S., and Tokuda, H. (2011) Lipoprotein sorting in Bacteria. Annu Rev Microbiol 65: 239-259.
    • (2011) Annu Rev Microbiol , vol.65 , pp. 239-259
    • Okuda, S.1    Tokuda, H.2
  • 55
    • 34548336772 scopus 로고    scopus 로고
    • Higher-energy C-trap dissociation for peptide modification analysis
    • Olsen, J.V., Macek, B., Lange, O., Makarov, A., Horning, S., and Mann, M. (2007) Higher-energy C-trap dissociation for peptide modification analysis. Nat Methods 4: 709-712.
    • (2007) Nat Methods , vol.4 , pp. 709-712
    • Olsen, J.V.1    Macek, B.2    Lange, O.3    Makarov, A.4    Horning, S.5    Mann, M.6
  • 56
    • 14544282391 scopus 로고    scopus 로고
    • Reconstitution of O-specific lipopolysaccharide expression in Burkholderia cenocepacia strain J2315, which is associated with transmissible infections in patients with cystic fibrosis
    • Ortega, X., Hunt, T.A., Loutet, S., Vinion-Dubiel, A.D., Datta, A., Choudhury, B., etal. (2005) Reconstitution of O-specific lipopolysaccharide expression in Burkholderia cenocepacia strain J2315, which is associated with transmissible infections in patients with cystic fibrosis. J Bacteriol 187: 1324-1333.
    • (2005) J Bacteriol , vol.187 , pp. 1324-1333
    • Ortega, X.1    Hunt, T.A.2    Loutet, S.3    Vinion-Dubiel, A.D.4    Datta, A.5    Choudhury, B.6
  • 57
    • 69249111807 scopus 로고    scopus 로고
    • Biosynthesis and structure of the Burkholderia cenocepacia K56-2 lipopolysaccharide core oligosaccharide: truncation of the core oligosaccharide leads to increased binding and sensitivity to polymixin B
    • Ortega, X., Silipo, A., Saldías, M.S., Bates, C.C., Molinaro, A., and Valvano, M.A. (2009) Biosynthesis and structure of the Burkholderia cenocepacia K56-2 lipopolysaccharide core oligosaccharide: truncation of the core oligosaccharide leads to increased binding and sensitivity to polymixin B. J Biol Chem 284: 21738-21751.
    • (2009) J Biol Chem , vol.284 , pp. 21738-21751
    • Ortega, X.1    Silipo, A.2    Saldías, M.S.3    Bates, C.C.4    Molinaro, A.5    Valvano, M.A.6
  • 58
    • 21344459511 scopus 로고    scopus 로고
    • Biotechnological potential within the genus Burkholderia
    • O'Sullivan, L.A., and Mahenthiralingam, E. (2005) Biotechnological potential within the genus Burkholderia. Lett Appl Microbiol 41: 8-11.
    • (2005) Lett Appl Microbiol , vol.41 , pp. 8-11
    • O'Sullivan, L.A.1    Mahenthiralingam, E.2
  • 59
    • 80055084408 scopus 로고    scopus 로고
    • Characterization and scope of S-layer protein O-glycosylation in Tannerella forsythia
    • Posch, G., Pabst, M., Brecker, L., Altmann, F., Messner, P., and Schäffer, C. (2011) Characterization and scope of S-layer protein O-glycosylation in Tannerella forsythia. J Biol Chem 286: 38714-38724.
    • (2011) J Biol Chem , vol.286 , pp. 38714-38724
    • Posch, G.1    Pabst, M.2    Brecker, L.3    Altmann, F.4    Messner, P.5    Schäffer, C.6
  • 62
    • 33746351043 scopus 로고    scopus 로고
    • Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli
    • Power, P.M., Seib, K.L., and Jennings, M.P. (2006) Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli. Biochem Biophys Res Commun 347: 904-908.
    • (2006) Biochem Biophys Res Commun , vol.347 , pp. 904-908
    • Power, P.M.1    Seib, K.L.2    Jennings, M.P.3
  • 63
    • 78049441523 scopus 로고    scopus 로고
    • 50 values from the method of Miller and Tainter, 1944
    • 50 values from the method of Miller and Tainter, 1944. J Ayub Med Coll Abbottabad 21: 184-185.
    • (2009) J Ayub Med Coll Abbottabad , vol.21 , pp. 184-185
    • Randhawa, M.A.1
  • 64
    • 49049120373 scopus 로고    scopus 로고
    • Affinity-capture tandem mass spectrometric characterization of polyprenyl-linked oligosaccharides: tool to study protein N-glycosylation pathways
    • Reid, C.W., Stupak, J., Chen, M.M., Imperiali, B., Li, J., and Szymanski, C.M. (2008) Affinity-capture tandem mass spectrometric characterization of polyprenyl-linked oligosaccharides: tool to study protein N-glycosylation pathways. Anal Chem 80: 5468-5475.
    • (2008) Anal Chem , vol.80 , pp. 5468-5475
    • Reid, C.W.1    Stupak, J.2    Chen, M.M.3    Imperiali, B.4    Li, J.5    Szymanski, C.M.6
  • 65
    • 0038028636 scopus 로고    scopus 로고
    • Identification and molecular analysis of cable pilus biosynthesis genes in Burkholderia cepacia
    • Sajjan, U.S., Xie, H., Lefebre, M.D., Valvano, M.A., and Forstner, J.F. (2003) Identification and molecular analysis of cable pilus biosynthesis genes in Burkholderia cepacia. Microbiology 149: 961-971.
    • (2003) Microbiology , vol.149 , pp. 961-971
    • Sajjan, U.S.1    Xie, H.2    Lefebre, M.D.3    Valvano, M.A.4    Forstner, J.F.5
  • 66
    • 84877069353 scopus 로고    scopus 로고
    • Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates
    • Schulz, B.L., Jen, F.E.-C., Power, P.M., Jones, C.E., Fox, K.L., Ku, S.C., etal. (2013) Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates. PLoS ONE 8: e62768.
    • (2013) PLoS ONE , vol.8
    • Schulz, B.L.1    Jen, F.-C.2    Power, P.M.3    Jones, C.E.4    Fox, K.L.5    Ku, S.C.6
  • 68
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni
    • M000031-MMCP201
    • Scott, N.E., Parker, B.L., Connolly, A.M., Paulech, J., Edwards, A.V.G., Crossett, B., etal. (2011b) Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Mol Cell Proteomics 10: M000031-MCP201.
    • (2011) Mol Cell Proteomics , vol.10
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.G.5    Crossett, B.6
  • 69
    • 84865479016 scopus 로고    scopus 로고
    • Modification of the Campylobacter jejuni N-linked glycan by EptC protein-mediated addition of phosphoethanolamine
    • Scott, N.E., Nothaft, H., Edwards, A., and Labbate, M. (2012) Modification of the Campylobacter jejuni N-linked glycan by EptC protein-mediated addition of phosphoethanolamine. J Biol Chem 287: 29384-29396.
    • (2012) J Biol Chem , vol.287 , pp. 29384-29396
    • Scott, N.E.1    Nothaft, H.2    Edwards, A.3    Labbate, M.4
  • 70
    • 40749107023 scopus 로고    scopus 로고
    • Development of Galleria mellonella as an alternative infection model for the Burkholderia cepacia complex
    • Seed, K.D., and Dennis, J.J. (2008) Development of Galleria mellonella as an alternative infection model for the Burkholderia cepacia complex. Infect Immun 76: 1267-1275.
    • (2008) Infect Immun , vol.76 , pp. 1267-1275
    • Seed, K.D.1    Dennis, J.J.2
  • 72
    • 0028840449 scopus 로고
    • Meningococcal pilin: a glycoprotein substituted with digctosyl 2,4-diacetamido-2,4,6-trideoxyhexose
    • Stimson, E., Virji, M., Makepeace, K., Dell, A., Morris, H.R., Payne, G., etal. (1995) Meningococcal pilin: a glycoprotein substituted with digctosyl 2, 4-diacetamido-2, 4, 6-trideoxyhexose. Mol Microbiol 17: 1201-1214.
    • (1995) Mol Microbiol , vol.17 , pp. 1201-1214
    • Stimson, E.1    Virji, M.2    Makepeace, K.3    Dell, A.4    Morris, H.R.5    Payne, G.6
  • 73
    • 0028233079 scopus 로고
    • Identification and characterization of a chromosomal virulence gene, vacJ, required for intercellular spreading of Shigella flexneri
    • Suzuki, T., Murai, T., Fukuda, I., Tobe, T., Yoshikawa, M., and Sasakawa, C. (1994) Identification and characterization of a chromosomal virulence gene, vacJ, required for intercellular spreading of Shigella flexneri. Mol Microbiol 11: 31-41.
    • (1994) Mol Microbiol , vol.11 , pp. 31-41
    • Suzuki, T.1    Murai, T.2    Fukuda, I.3    Tobe, T.4    Yoshikawa, M.5    Sasakawa, C.6
  • 74
    • 76849086087 scopus 로고    scopus 로고
    • Defects in flagellin glycosylation affect the virulence of Pseudomonas syringae pv. tabaci 6605
    • Taguchi, F., Yamamoto, M., Ohnishi-Kameyama, M., Iwaki, M., Yoshida, M., Ishii, T., etal. (2010) Defects in flagellin glycosylation affect the virulence of Pseudomonas syringae pv. tabaci 6605. Microbiology 156: 72-80.
    • (2010) Microbiology , vol.156 , pp. 72-80
    • Taguchi, F.1    Yamamoto, M.2    Ohnishi-Kameyama, M.3    Iwaki, M.4    Yoshida, M.5    Ishii, T.6
  • 75
    • 0032515174 scopus 로고    scopus 로고
    • Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins
    • Tajima, T., Yokota, N., Matsuyama, S., and Tokuda, H. (1998) Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins. FEBS Lett 439: 51-54.
    • (1998) FEBS Lett , vol.439 , pp. 51-54
    • Tajima, T.1    Yokota, N.2    Matsuyama, S.3    Tokuda, H.4
  • 76
    • 0242575011 scopus 로고    scopus 로고
    • Flagellin glycosylation island in Pseudomonas syringae pv. glycinea and its role in host specificity
    • Takeuchi, K., Taguchi, F., Inagaki, Y., Toyoda, K., Shiraishi, T., and Ichinose, Y. (2003) Flagellin glycosylation island in Pseudomonas syringae pv. glycinea and its role in host specificity. J Bacteriol 185: 6658-6665.
    • (2003) J Bacteriol , vol.185 , pp. 6658-6665
    • Takeuchi, K.1    Taguchi, F.2    Inagaki, Y.3    Toyoda, K.4    Shiraishi, T.5    Ichinose, Y.6
  • 77
    • 84892383703 scopus 로고    scopus 로고
    • Common duckweed (Lemna minor) is a versatile high-throughput infection model for the Burkholderia cepacia complex and other pathogenic bacteria
    • Thomson, E.L.S., and Dennis, J.J. (2013) Common duckweed (Lemna minor) is a versatile high-throughput infection model for the Burkholderia cepacia complex and other pathogenic bacteria. PLoS ONE 8: e80102.
    • (2013) PLoS ONE , vol.8
    • Thomson, E.L.S.1    Dennis, J.J.2
  • 78
    • 0036130609 scopus 로고    scopus 로고
    • Role of flagella in host cell invasion by Burkholderia cepacia
    • Tomich, M., Herfst, C.A., Golden, J.W., and Mohr, C.D. (2002) Role of flagella in host cell invasion by Burkholderia cepacia. Infect Immun 70: 1799-1806.
    • (2002) Infect Immun , vol.70 , pp. 1799-1806
    • Tomich, M.1    Herfst, C.A.2    Golden, J.W.3    Mohr, C.D.4
  • 79
    • 0020055346 scopus 로고
    • A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels
    • Tsai, C.M., and Frasch, C.E. (1982) A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Anal Biochem 119: 115-119.
    • (1982) Anal Biochem , vol.119 , pp. 115-119
    • Tsai, C.M.1    Frasch, C.E.2
  • 81
    • 69049120321 scopus 로고    scopus 로고
    • Identification of specific and universal virulence factors in Burkholderia cenocepacia strains by using multiple infection hosts
    • Uehlinger, S., Schwager, S., Bernier, S.P., Riedel, K., Nguyen, D.T., Sokol, P.A., etal. (2009) Identification of specific and universal virulence factors in Burkholderia cenocepacia strains by using multiple infection hosts. Infect Immun 77: 4102-4110.
    • (2009) Infect Immun , vol.77 , pp. 4102-4110
    • Uehlinger, S.1    Schwager, S.2    Bernier, S.P.3    Riedel, K.4    Nguyen, D.T.5    Sokol, P.A.6
  • 82
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • UniProt Consortium
    • UniProt Consortium (2012) Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res 40: D71-D75.
    • (2012) Nucleic Acids Res , vol.40
  • 83
  • 84
    • 84997831539 scopus 로고    scopus 로고
    • Draft genome sequences of Burkholderia cenocepacia ET12 lineage strains K56-2 and BC7
    • e00841-e00813
    • Varga, J.J., Losada, L., Zelazny, A.M., Kim, M., McCorrison, J., Brinkac, L., etal. (2013) Draft genome sequences of Burkholderia cenocepacia ET12 lineage strains K56-2 and BC7. Genome Announc 1.pii: e00841-13.
    • (2013) Genome Announc , vol.1
    • Varga, J.J.1    Losada, L.2    Zelazny, A.M.3    Kim, M.4    McCorrison, J.5    Brinkac, L.6
  • 86
    • 0011928107 scopus 로고    scopus 로고
    • N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli
    • Wacker, M., Linton, D., Hitchen, P.G., Nita-Lazar, M., Haslam, S.M., North, S.J., etal. (2002) N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli. Science 298: 1790-1793.
    • (2002) Science , vol.298 , pp. 1790-1793
    • Wacker, M.1    Linton, D.2    Hitchen, P.G.3    Nita-Lazar, M.4    Haslam, S.M.5    North, S.J.6
  • 87
  • 88
    • 0028501914 scopus 로고
    • Non-globular domains in protein sequences: automated segmentation using complexity measures
    • Wootton, J.C. (1994) Non-globular domains in protein sequences: automated segmentation using complexity measures. Comput Chem 18: 269-285.
    • (1994) Comput Chem , vol.18 , pp. 269-285
    • Wootton, J.C.1
  • 89
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi, T., Masuda, K., Narita, S., Matsuyama, S., and Tokuda, H. (2000) A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat Cell Biol 2: 212-218.
    • (2000) Nat Cell Biol , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 90
    • 0037044765 scopus 로고    scopus 로고
    • Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni
    • Young, N.M., Brisson, J.-R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., etal. (2002) Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J Biol Chem 277: 42530-42539.
    • (2002) J Biol Chem , vol.277 , pp. 42530-42539
    • Young, N.M.1    Brisson, J.-R.2    Kelly, J.3    Watson, D.C.4    Tessier, L.5    Lanthier, P.H.6
  • 91
    • 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., etal. (2010) PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26: 1608-1615.
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6
  • 92
    • 78149423445 scopus 로고    scopus 로고
    • Duckweed (Lemna minor) as a model plant system for the study of human microbial pathogenesis
    • Zhang, Y., Hu, Y., Yang, B., Ma, F., Lu, P., Li, L., etal. (2010) Duckweed (Lemna minor) as a model plant system for the study of human microbial pathogenesis. PLoS ONE 5: e13527.
    • (2010) PLoS ONE , vol.5
    • Zhang, Y.1    Hu, Y.2    Yang, B.3    Ma, F.4    Lu, P.5    Li, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.