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Volumn 195, Issue 19, 2013, Pages 4425-4435

Comparative proteome analysis of spontaneous outer membrane vesicles and purified outer membranes of neisseria meningitidis

Author keywords

[No Author keywords available]

Indexed keywords

NITROGEN 15; OUTER MEMBRANE PROTEIN; PEPTIDOGLYCAN; PROTEOME;

EID: 84885466975     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00625-13     Document Type: Article
Times cited : (95)

References (64)
  • 1
    • 77749309281 scopus 로고    scopus 로고
    • Virulence and immunomodulatory roles of bacterial outer membrane vesicles
    • Ellis TN, Kuehn MJ. 2010. Virulence and immunomodulatory roles of bacterial outer membrane vesicles. Microbiol. Mol. Biol. Rev. 74:81-94.
    • (2010) Microbiol. Mol. Biol. Rev. , vol.74 , pp. 81-94
    • Ellis, T.N.1    Kuehn, M.J.2
  • 2
    • 77957959533 scopus 로고    scopus 로고
    • Biological functions and biogenesis of secreted bacterial outer membrane vesicles
    • Kulp A, Kuehn MJ. 2010. Biological functions and biogenesis of secreted bacterial outer membrane vesicles. Annu. Rev. Microbiol. 64:163-184.
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 163-184
    • Kulp, A.1    Kuehn, M.J.2
  • 3
    • 84873160157 scopus 로고    scopus 로고
    • The role of bacterial outer membrane vesicles for intra- and interspecies delivery
    • Berleman J, Auer M. 2013. The role of bacterial outer membrane vesicles for intra- and interspecies delivery. Environ. Microbiol. 15:347-354.
    • (2013) Environ. Microbiol. , vol.15 , pp. 347-354
    • Berleman, J.1    Auer, M.2
  • 4
    • 84860588660 scopus 로고    scopus 로고
    • Cell contact-dependent outer membrane exchange in myxobacteria: genetic determinants and mechanism
    • doi:10.1371 /journal.pgen.1002626
    • Pathak DT, Wei X, Bucuvalas A, Haft DH, Gerloff DL, Wall D. 2012. Cell contact-dependent outer membrane exchange in myxobacteria: genetic determinants and mechanism. PLoS Genet. 8:e1002626. doi:10.1371 /journal.pgen.1002626.
    • (2012) PLoS Genet , vol.8
    • Pathak, D.T.1    Wei, X.2    Bucuvalas, A.3    Haft, D.H.4    Gerloff, D.L.5    Wall, D.6
  • 5
    • 10644226878 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells
    • Kesty NC, Mason KM, Reedy M, Miller SE, Kuehn MJ. 2004. Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells. EMBO J. 23:4538-4549.
    • (2004) EMBO J , vol.23 , pp. 4538-4549
    • Kesty, N.C.1    Mason, K.M.2    Reedy, M.3    Miller, S.E.4    Kuehn, M.J.5
  • 6
    • 33846037385 scopus 로고    scopus 로고
    • Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response
    • McBroom AJ, Kuehn MJ. 2007. Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response. Mol. Microbiol. 63:545-558.
    • (2007) Mol. Microbiol. , vol.63 , pp. 545-558
    • McBroom, A.J.1    Kuehn, M.J.2
  • 7
    • 84872823871 scopus 로고    scopus 로고
    • Cysteine depletion causes oxidative stress and triggers outer membrane vesicle release by Neisseria meningitidis; implications for vaccine development
    • doi:10.1371/journal.pone.0054314
    • van de Waterbeemd B, Zomer G, van den Ijssel J, van Keulen L, Eppink MH, van der Ley P, van der Pol LA. 2013. Cysteine depletion causes oxidative stress and triggers outer membrane vesicle release by Neisseria meningitidis; implications for vaccine development. PLoS One 8:e54314. doi:10.1371/journal.pone.0054314.
    • (2013) PLoS One , vol.8
    • van de Waterbeemd, B.1    Zomer, G.2    van den Ijssel, J.3    van Keulen, L.4    Eppink, M.H.5    van der Ley, P.6    van der Pol, L.A.7
  • 8
    • 68249144375 scopus 로고    scopus 로고
    • Proteome analysis of outer membrane vesicles from a clinical Acinetobacter baumannii isolate
    • Kwon SO, Gho YS, Lee JC, Kim SI. 2009. Proteome analysis of outer membrane vesicles from a clinical Acinetobacter baumannii isolate. FEMS Microbiol. Lett. 297:150-156.
    • (2009) FEMS Microbiol. Lett. , vol.297 , pp. 150-156
    • Kwon, S.O.1    Gho, Y.S.2    Lee, J.C.3    Kim, S.I.4
  • 11
    • 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, Hoppert M, Sogaard-Andersen L, Hedderich R. 2010. 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. 9:5197-5208.
    • (2010) J. Proteome Res. , vol.9 , pp. 5197-5208
    • Kahnt, J.1    Aguiluz, K.2    Koch, J.3    Treuner-Lange, A.4    Konovalova, A.5    Huntley, S.6    Hoppert, M.7    Sogaard-Andersen, L.8    Hedderich, R.9
  • 12
    • 33644681971 scopus 로고    scopus 로고
    • Biochemical and functional characterization of membrane blebs purified from Neisseria meningitidis serogroup B
    • Post DM, Zhang D, Eastvold JS, Teghanemt A, Gibson BW, Weiss JP. 2005. Biochemical and functional characterization of membrane blebs purified from Neisseria meningitidis serogroup B. J. Biol. Chem. 280: 38383-38394.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38383-38394
    • Post, D.M.1    Zhang, D.2    Eastvold, J.S.3    Teghanemt, A.4    Gibson, B.W.5    Weiss, J.P.6
  • 13
    • 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 AR, Biolchi A, Brunelli B, Giuliani MM, Pizza M, Norais N, Grandi G. 2006. Outer membrane vesicles from group B Neisseria meningitidis delta gna33 mutant: proteomic and immunological comparison with detergent-derived outer membrane vesicles. Proteomics 6:1856-1866.
    • (2006) Proteomics , vol.6 , pp. 1856-1866
    • Ferrari, G.1    Garaguso, I.2    Adu-Bobie, J.3    Doro, F.4    Taddei, A.R.5    Biolchi, A.6    Brunelli, B.7    Giuliani, M.M.8    Pizza, M.9    Norais, N.10    Grandi, G.11
  • 15
    • 0001502602 scopus 로고
    • Extrameningeal meningococcus infection
    • Herrick WW. 1919. Extrameningeal meningococcus infection. Arch. Intern. Med. 23:409-418.
    • (1919) Arch. Intern. Med. , vol.23 , pp. 409-418
    • Herrick, W.W.1
  • 16
    • 0033957876 scopus 로고    scopus 로고
    • Update on meningococcal disease with emphasis on pathogenesis and clinical management
    • table of contents
    • van Deuren M, Brandtzaeg P, van der Meer JW. 2000. Update on meningococcal disease with emphasis on pathogenesis and clinical management. Clin. Microbiol. Rev. 13:144-166, table of contents.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 144-166
    • van Deuren, M.1    Brandtzaeg, P.2    van der Meer, J.W.3
  • 18
    • 0026538006 scopus 로고
    • Meningococcal endotoxin in lethal septic shock plasma studied by gas chromatography, mass-spectrometry, ultracentrifugation, and electron microscopy
    • Brandtzaeg P, Bryn K, Kierulf P, Ovstebo R, Namork E, Aase B, Jantzen E. 1992. Meningococcal endotoxin in lethal septic shock plasma studied by gas chromatography, mass-spectrometry, ultracentrifugation, and electron microscopy. J. Clin. Invest. 89:816-823.
    • (1992) J. Clin. Invest. , vol.89 , pp. 816-823
    • Brandtzaeg, P.1    Bryn, K.2    Kierulf, P.3    Ovstebo, R.4    Namork, E.5    Aase, B.6    Jantzen, E.7
  • 22
    • 77957355947 scopus 로고    scopus 로고
    • A phase 1 study of a group B meningococcal native outer membrane vesicle vaccine made from a strain with deleted lpxL2 and synX and stable expression of opcA
    • Keiser PB, Gibbs BT, Coster TS, Moran EE, Stoddard MB, Labrie JE, III, Schmiel DH, Pinto V, Chen P, Zollinger WD. 2010. A phase 1 study of a group B meningococcal native outer membrane vesicle vaccine made from a strain with deleted lpxL2 and synX and stable expression of opcA. Vaccine 28:6970-6976.
    • (2010) Vaccine , vol.28 , pp. 6970-6976
    • Keiser, P.B.1    Gibbs, B.T.2    Coster, T.S.3    Moran, E.E.4    Stoddard, M.B.5    Labrie, J.E.6    Schmiel, D.H.7    Pinto, V.8    Chen, P.9    Zollinger, W.D.10
  • 23
    • 84875923227 scopus 로고    scopus 로고
    • Quantitative proteomics reveals distinct differences in the protein content of outer membrane vesicle vaccines
    • 15 February 2013, posting date. (Epub ahead of print.) doi:10.1021/pr301208g
    • van de Waterbeemd B, Mommen GP, Pennings JL, Eppink MH, Wijffels R, van der Pol LA, de Jong AP. 15 February 2013, posting date. Quantitative proteomics reveals distinct differences in the protein content of outer membrane vesicle vaccines. J. Proteome Res. (Epub ahead of print.) doi:10.1021/pr301208g.
    • (2013) J. Proteome Res.
    • van de Waterbeemd, B.1    Mommen, G.P.2    Pennings, J.L.3    Eppink, M.H.4    Wijffels, R.5    van der Pol, L.A.6    de Jong, A.P.7
  • 24
    • 0029077758 scopus 로고
    • Investigations into the molecular basis of meningococcal toxicity for human endothelial and epithelial cells: the synergistic effect of LPS and pili
    • Dunn KL, Virji M, Moxon ER. 1995. Investigations into the molecular basis of meningococcal toxicity for human endothelial and epithelial cells: the synergistic effect of LPS and pili. Microb. Pathog. 18:81-96.
    • (1995) Microb. Pathog. , vol.18 , pp. 81-96
    • Dunn, K.L.1    Virji, M.2    Moxon, E.R.3
  • 25
    • 0031851907 scopus 로고    scopus 로고
    • Necessity of molecular techniques to distinguish between Neisseria meningitidis strains isolated from patients with meningococcal disease and from their healthy contacts
    • Vogel U, Morelli G, Zurth K, Claus H, Kriener E, Achtman M, Frosch M. 1998. Necessity of molecular techniques to distinguish between Neisseria meningitidis strains isolated from patients with meningococcal disease and from their healthy contacts. J. Clin. Microbiol. 36:2465-2470.
    • (1998) J. Clin. Microbiol. , vol.36 , pp. 2465-2470
    • Vogel, U.1    Morelli, G.2    Zurth, K.3    Claus, H.4    Kriener, E.5    Achtman, M.6    Frosch, M.7
  • 27
    • 33750723428 scopus 로고    scopus 로고
    • Meningococcal biofilm formation: structure, development and phenotypes in a standardized continuous flow system
    • Lappann M, Haagensen JA, Claus H, Vogel U, Molin S. 2006. Meningococcal biofilm formation: structure, development and phenotypes in a standardized continuous flow system. Mol. Microbiol. 62:1292-1309.
    • (2006) Mol. Microbiol. , vol.62 , pp. 1292-1309
    • Lappann, M.1    Haagensen, J.A.2    Claus, H.3    Vogel, U.4    Molin, S.5
  • 29
    • 0017475522 scopus 로고
    • The surface of Neisseria gonorrhoeae: isolation of the major components of the outer membrane
    • Heckels JE. 1977. The surface of Neisseria gonorrhoeae: isolation of the major components of the outer membrane. J. Gen. Microbiol. 99:333- 341.
    • (1977) J. Gen. Microbiol. , vol.99 , pp. 333-341
    • Heckels, J.E.1
  • 30
    • 0018853713 scopus 로고
    • Chemical analysis of major outer membrane proteins of Neisseria meningitidis: comparison of serotypes 2 and 11
    • Tsai CM, Frasch CE. 1980. Chemical analysis of major outer membrane proteins of Neisseria meningitidis: comparison of serotypes 2 and 11. J. Bacteriol. 141:169-176.
    • (1980) J. Bacteriol. , vol.141 , pp. 169-176
    • Tsai, C.M.1    Frasch, C.E.2
  • 31
    • 0346122950 scopus 로고    scopus 로고
    • A correlation algorithm for the automated quantitative analysis of shotgun proteomics data
    • MacCoss MJ, Wu CC, Liu H, Sadygov R, Yates JR, III. 2003. A correlation algorithm for the automated quantitative analysis of shotgun proteomics data. Anal. Chem. 75:6912-6921.
    • (2003) Anal. Chem. , vol.75 , pp. 6912-6921
    • MacCoss, M.J.1    Wu, C.C.2    Liu, H.3    Sadygov, R.4    Yates III, J.R.5
  • 32
    • 44649164495 scopus 로고    scopus 로고
    • Monitoring of changes in the membrane proteome during stationary phase adaptation of Bacillus subtilis using in vivo labeling techniques
    • Dreisbach A, Otto A, Becher D, Hammer E, Teumer A, Gouw JW, Hecker M, Volker U. 2008. Monitoring of changes in the membrane proteome during stationary phase adaptation of Bacillus subtilis using in vivo labeling techniques. Proteomics 8:2062-2076.
    • (2008) Proteomics , vol.8 , pp. 2062-2076
    • Dreisbach, A.1    Otto, A.2    Becher, D.3    Hammer, E.4    Teumer, A.5    Gouw, J.W.6    Hecker, M.7    Volker, U.8
  • 36
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41:95-98.
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 37
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • Park SK, Venable JD, Xu T, Yates JR, III. 2008. A quantitative analysis software tool for mass spectrometry-based proteomics. Nat. Methods 5:319-322.
    • (2008) Nat. Methods , vol.5 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates III, J.R.4
  • 40
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3 0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu NY, Wagner JR, Laird MR, Melli G, Rey S, Lo R, Dao P, Sahinalp SC, Ester M, Foster LJ, Brinkman FS. 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    Dao, P.7    Sahinalp, S.C.8    Ester, M.9    Foster, L.J.10    Brinkman, F.S.11
  • 42
    • 0038487289 scopus 로고    scopus 로고
    • Antigenic diversity of meningococcal enterobactin receptor FetA, a vaccine component
    • Thompson EA, Feavers IM, Maiden MC. 2003. Antigenic diversity of meningococcal enterobactin receptor FetA, a vaccine component. Microbiology 149:1849-1858.
    • (2003) Microbiology , vol.149 , pp. 1849-1858
    • Thompson, E.A.1    Feavers, I.M.2    Maiden, M.C.3
  • 43
    • 0345714773 scopus 로고    scopus 로고
    • Conformational epitopes recognized by protective anti-neisserial surface protein A antibodies
    • Hou VC, Moe GR, Raad Z, Wuorimaa T, Granoff DM. 2003. Conformational epitopes recognized by protective anti-neisserial surface protein A antibodies. Infect. Immun. 71:6844-6849.
    • (2003) Infect. Immun. , vol.71 , pp. 6844-6849
    • Hou, V.C.1    Moe, G.R.2    Raad, Z.3    Wuorimaa, T.4    Granoff, D.M.5
  • 44
    • 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 JN, Skipp PJ, Humphries HE, Christodoulides M, O'Connor CD, Heckels JE. 2007. Proteomic analysis of outer membranes and vesicles from wild-type serogroup B Neisseria meningitidis and a lipopolysaccharide-deficient mutant. Infect. Immun. 75:1364-1372.
    • (2007) Infect. Immun. , vol.75 , 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
  • 45
    • 0017224869 scopus 로고
    • The serological classification of Neisseria gonorrhoeae I. Isolation of the outer membrane complex responsible for serotypic specificity
    • Johnston KH, Holmes KK, Gotschlich EC. 1976. The serological classification of Neisseria gonorrhoeae. I. Isolation of the outer membrane complex responsible for serotypic specificity. J. Exp. Med. 143:741-758.
    • (1976) J. Exp. Med. , vol.143 , pp. 741-758
    • Johnston, K.H.1    Holmes, K.K.2    Gotschlich, E.C.3
  • 46
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium Isolation and characterization of cytoplasmic and outer membrane
    • Osborn MJ, Gander JE, Parisi E, Carson J. 1972. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J. Biol. Chem. 247: 3962-3972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 47
    • 0016169850 scopus 로고
    • An outer membrane protein of Neisseria meningitidis group B responsible for serotype specificity
    • Frasch CE, Gotschlich EC. 1974. An outer membrane protein of Neisseria meningitidis group B responsible for serotype specificity. J. Exp. Med. 140:87-104.
    • (1974) J. Exp. Med. , vol.140 , pp. 87-104
    • Frasch, C.E.1    Gotschlich, E.C.2
  • 49
    • 84875923227 scopus 로고    scopus 로고
    • Quantitative proteomics reveals distinct differences in the protein content of outer membrane vesicle vaccines
    • 15 February 2013, posting date. (Epub ahead of print.) doi:10.1021/pr301208g
    • van de Waterbeemd B, Mommen GP, Pennings JL, Eppink MH, Wijffels RH, van der Pol LA, de Jong AP. 15 February 2013, posting date. Quantitative proteomics reveals distinct differences in the protein content of outer membrane vesicle vaccines. J. Proteome Res. (Epub ahead of print.) doi:10.1021/pr301208g.
    • (2013) J. Proteome Res.
    • van de Waterbeemd, B.1    Mommen, G.P.2    Pennings, J.L.3    Eppink, M.H.4    Wijffels, R.H.5    van der Pol, L.A.6    de Jong, A.P.7
  • 50
    • 57249108238 scopus 로고    scopus 로고
    • Proteomics in gram-negative bacterial outer membrane vesicles
    • Lee EY, Choi DS, Kim KP, Gho YS. 2008. Proteomics in gram-negative bacterial outer membrane vesicles. Mass Spectrom. Rev. 27:535-555.
    • (2008) Mass Spectrom. Rev. , vol.27 , pp. 535-555
    • Lee, E.Y.1    Choi, D.S.2    Kim, K.P.3    Gho, Y.S.4
  • 51
    • 0024563822 scopus 로고
    • Export and intercellular transfer of DNA via membrane blebs of Neisseria gonorrhoeae
    • Dorward DW, Garon CF, Judd RC. 1989. Export and intercellular transfer of DNA via membrane blebs of Neisseria gonorrhoeae. J. Bacteriol. 171:2499-2505.
    • (1989) J. Bacteriol. , vol.171 , pp. 2499-2505
    • Dorward, D.W.1    Garon, C.F.2    Judd, R.C.3
  • 52
    • 84874815934 scopus 로고    scopus 로고
    • A new type of outer membrane vesicles produced by the Gram-negative bacterium Shewanella vesiculosa M7T: implications for DNA content
    • Pérez-Cruz C, Carrion O, Delgado L, Martinez G, Lopez-Iglesias C, Mercade E. 2013. A new type of outer membrane vesicles produced by the Gram-negative bacterium Shewanella vesiculosa M7T: implications for DNA content. Appl. Environ. Microbiol. 79:1874-1881.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 1874-1881
    • Pérez-Cruz, C.1    Carrion, O.2    Delgado, L.3    Martinez, G.4    Lopez-Iglesias, C.5    Mercade, E.6
  • 54
    • 33745875356 scopus 로고    scopus 로고
    • Self-associating autotransporters SAATs: functional and structural similarities
    • Klemm P, Vejborg RM, Sherlock O. 2006. Self-associating autotransporters, SAATs: functional and structural similarities. Int. J. Med. Microbiol. 296:187-195.
    • (2006) Int. J. Med. Microbiol. , vol.296 , pp. 187-195
    • Klemm, P.1    Vejborg, R.M.2    Sherlock, O.3
  • 56
    • 84872413906 scopus 로고    scopus 로고
    • Involvement of three meningococcal surface-exposed proteins, the heparin-binding protein NhbA, the alpha-peptide of IgA protease and the autotransporter protease NalP, in initiation of biofilm formation
    • Arenas J, Nijland R, Rodriguez FJ, Bosma TN, Tommassen J. 2013. Involvement of three meningococcal surface-exposed proteins, the heparin-binding protein NhbA, the alpha-peptide of IgA protease and the autotransporter protease NalP, in initiation of biofilm formation. Mol. Microbiol. 87:254-268.
    • (2013) Mol. Microbiol. , vol.87 , pp. 254-268
    • Arenas, J.1    Nijland, R.2    Rodriguez, F.J.3    Bosma, T.N.4    Tommassen, J.5
  • 57
    • 36549065290 scopus 로고    scopus 로고
    • A functional two-partner secretion system contributes to adhesion of Neisseria meningitidis to epithelial cells
    • Schmitt C, Turner D, Boesl M, Abele M, Frosch M, Kurzai O. 2007. A functional two-partner secretion system contributes to adhesion of Neisseria meningitidis to epithelial cells. J. Bacteriol. 189:7968-7976.
    • (2007) J. Bacteriol. , vol.189 , pp. 7968-7976
    • Schmitt, C.1    Turner, D.2    Boesl, M.3    Abele, M.4    Frosch, M.5    Kurzai, O.6
  • 58
    • 82155166266 scopus 로고    scopus 로고
    • Meningococcal surface fibril (Msf) binds to activated vitronectin and inhibits the terminal complement pathway to increase serum resistance
    • Griffiths NJ, Hill DJ, Borodina E, Sessions RB, Devos NI, Feron CM, Poolman JT, Virji M. 2011. Meningococcal surface fibril (Msf) binds to activated vitronectin and inhibits the terminal complement pathway to increase serum resistance. Mol. Microbiol. 82:1129-1149.
    • (2011) Mol. Microbiol. , vol.82 , pp. 1129-1149
    • Griffiths, N.J.1    Hill, D.J.2    Borodina, E.3    Sessions, R.B.4    Devos, N.I.5    Feron, C.M.6    Poolman, J.T.7    Virji, M.8
  • 59
    • 77957652922 scopus 로고    scopus 로고
    • The meningococcal vaccine candidate neisserial surface protein A (NspA) binds to factorHand enhances meningococcal resistance to complement
    • doi:10.1371/journal.ppat.1001027
    • Lewis LA, Ngampasutadol J, Wallace R, Reid JE, Vogel U, Ram S. 2010. The meningococcal vaccine candidate neisserial surface protein A (NspA) binds to factorHand enhances meningococcal resistance to complement. PLoS Pathog. 6:e1001027. doi:10.1371/journal.ppat.1001027.
    • (2010) PLoS Pathog , vol.6
    • Lewis, L.A.1    Ngampasutadol, J.2    Wallace, R.3    Reid, J.E.4    Vogel, U.5    Ram, S.6
  • 61
    • 33747360999 scopus 로고    scopus 로고
    • Ecological advantages of autolysis during the development and dispersal of Pseudoalteromonas tunicata biofilms
    • Mai-Prochnow A, Webb JS, Ferrari BC, Kjelleberg S. 2006. Ecological advantages of autolysis during the development and dispersal of Pseudoalteromonas tunicata biofilms. Appl. Environ. Microbiol. 72: 5414 -5420.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5414-5420
    • Mai-Prochnow, A.1    Webb, J.S.2    Ferrari, B.C.3    Kjelleberg, S.4
  • 63
    • 1442325407 scopus 로고    scopus 로고
    • Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
    • Grizot S, Buchanan SK. 2004. Structure of the OmpA-like domain of RmpM from Neisseria meningitidis. Mol. Microbiol. 51:1027-1037.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1027-1037
    • Grizot, S.1    Buchanan, S.K.2
  • 64
    • 14844366129 scopus 로고    scopus 로고
    • Analysis of outer membrane protein complexes and heat-modifiable proteins in Neisseria strains using two-dimensional diagonal electrophoresis
    • Sánchez S, Arenas J, Abel A, Criado MT, Ferreiros CM. 2005. Analysis of outer membrane protein complexes and heat-modifiable proteins in Neisseria strains using two-dimensional diagonal electrophoresis. J. Proteome Res. 4:91-95.
    • (2005) J. Proteome Res. , vol.4 , pp. 91-95
    • Sánchez, S.1    Arenas, J.2    Abel, A.3    Criado, M.T.4    Ferreiros, C.M.5


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