메뉴 건너뛰기




Volumn 11, Issue 7, 2012, Pages

Characterization of protein glycosylation in Francisella tularensis subsp. holarctica: Identification of a novel glycosylated lipoprotein required for virulence

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DSBA PROTEIN; FTH 0069; GLYCAN; HEXOSE; MONOSACCHARIDE; O ANTIGEN; PILIN; UNCLASSIFIED DRUG;

EID: 84863798364     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.015016     Document Type: Article
Times cited : (31)

References (47)
  • 1
    • 21544481151 scopus 로고    scopus 로고
    • Role of motility and flagellin glycosylation in the pathogenesis of Pseudomonas aeruginosa burn wound infections
    • DOI 10.1128/IAI.73.7.4395-4398.2005
    • Arora, S. K., Neely, A. N., Blair, B., Lory, S., and Ramphal, R. (2005) Role of motility and flagelin glycosylation in the pathogenesis of Pseudomonas aeruginosa burn wound infections. Infect. Immun. 73, 4395-4398 (Pubitemid 40923187)
    • (2005) Infection and Immunity , vol.73 , Issue.7 , pp. 4395-4398
    • Arora, S.K.1    Neely, A.N.2    Blair, B.3    Lory, S.4    Ramphal, R.5
  • 2
    • 3142673556 scopus 로고    scopus 로고
    • The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks
    • Karlyshev, A. V., Everest, P., Linton, D., Cawthraw, S., Newell, D. G., and Wren, B. W. (2004) The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks. Microbiology 150, 1957-1964 (Pubitemid 38923693)
    • (2004) Microbiology , vol.150 , Issue.6 , pp. 1957-1964
    • Karlyshev, A.V.1    Everest, P.2    Linton, D.3    Cawthraw, S.4    Newell, D.G.5    Wren, B.W.6
  • 3
    • 0036127088 scopus 로고    scopus 로고
    • Campylobacter protein glycosylation affects host cell interactions
    • DOI 10.1128/IAI.70.4.2242-2244.2002
    • Szymanski, C. M., Burr, D. H., and Guerry, P. (2002) Campylobacter protein glycosylation affects host cell interactions. Infect. Immun. 70, 2242-2244 (Pubitemid 34242232)
    • (2002) Infection and Immunity , vol.70 , Issue.4 , pp. 2242-2244
    • Szymanski, C.M.1    Burr, D.H.2    Guerry, P.3
  • 4
    • 0142030034 scopus 로고    scopus 로고
    • Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene
    • DOI 10.1046/j.1365-2958.2003.03725.x
    • 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 (Pubitemid 37297142)
    • (2003) Molecular Microbiology , vol.50 , Issue.2 , pp. 659-671
    • Goon, S.1    Kelly, J.F.2    Logan, S.M.3    Ewing, C.P.4    Guerry, P.5
  • 5
    • 0037035408 scopus 로고    scopus 로고
    • The neuA/flmD gene cluster of Helicobacter pylori is involved in flagellar biosynthesis and flagellin glycosylation
    • DOI 10.1016/S0378-1097(02)00638-9, PII S0378109702006389
    • 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 (Pubitemid 34607181)
    • (2002) FEMS Microbiology Letters , vol.210 , Issue.2 , pp. 165-172
    • Josenhans, C.1    Vossebein, L.2    Friedrich, S.3    Suerbaum, S.4
  • 6
    • 0035167082 scopus 로고    scopus 로고
    • Role of flm locus in mesophilic Aeromonas species adherence
    • DOI 10.1128/IAI.69.1.65-74.2001
    • Gryllos, I., Shaw, J. G., Gavín, R., Merino, S., and Tomás, J. M. (2001) Role of flm locus in mesophilic Aeromonas species adherence. Infect. Immun. 69, 65-74 (Pubitemid 32038300)
    • (2001) Infection and Immunity , vol.69 , Issue.1 , pp. 65-74
    • Gryllos, I.1    Shaw, J.G.2    Gavin, R.3    Merino, S.4    Tomas, J.M.5
  • 7
    • 0031914987 scopus 로고    scopus 로고
    • Consequences of the loss of O-linked glycosylation of meningococcal type IV pilin on piliation and pilus-mediated adhesion
    • DOI 10.1046/j.1365-2958.1998.00706.x
    • Marceau, M., Forest, K., Béretti, J. L., Tainer, J., and Nassif, X. (1998) Consequences of the loss of O-linked glycosylation of meningococcal type IV pilin on piliation and pilus-mediated adhesion. Mol. Microbiol. 27, 705-715 (Pubitemid 28081980)
    • (1998) Molecular Microbiology , vol.27 , Issue.4 , pp. 705-715
    • Marceau, M.1    Forest, K.2    Beretti, J.-L.3    Tainer, J.4    Nassif, X.5
  • 8
    • 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
  • 12
    • 69949155661 scopus 로고    scopus 로고
    • Functional analyses of pilin-like proteins from Francisella tularensis: Complementation of type IV pilus phenotypes in Neisseria gonorrhoeae
    • Salomonsson, E., Forsberg, A., Roos, N., Holz, C., Maier, B., Koomey, M., and Winther-Larsen, H. C. (2009) Functional analyses of pilin-like proteins from Francisella tularensis: Complementation of type IV pilus phenotypes in Neisseria gonorrhoeae. Microbiology 155, 2546-2559
    • (2009) Microbiology , vol.155 , pp. 2546-2559
    • Salomonsson, E.1    Forsberg, A.2    Roos, N.3    Holz, C.4    Maier, B.5    Koomey, M.6    Winther-Larsen, H.C.7
  • 13
    • 77950672706 scopus 로고    scopus 로고
    • Multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism
    • Balonova, L., Hernychova, L., Mann, B. F., Link, M., Bilkova, Z., Novotny, M. V., and Stulik, J. (2010) Multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism. J. Proteome Res. 9, 1995-2005
    • (2010) J. Proteome Res. , vol.9 , pp. 1995-2005
    • Balonova, L.1    Hernychova, L.2    Mann, B.F.3    Link, M.4    Bilkova, Z.5    Novotny, M.V.6    Stulik, J.7
  • 18
    • 34249946537 scopus 로고    scopus 로고
    • Proteomic analysis of antibody response in a case of laboratory-acquired infection with Francisella tularensis subsp. tularensis
    • Janovská, S., Pávková, I., Reichelová, M., Hubáleka, M., Stulík, J., and Macela, A. (2007) Proteomic analysis of antibody response in a case of laboratory-acquired infection with Francisella tularensis subsp. tularensis. Folia Microbiol. 52, 194-198 (Pubitemid 46877932)
    • (2007) Folia Microbiologica , vol.52 , Issue.2 , pp. 194-198
    • Janovska, S.1    Pavkova, I.2    Reichelova, M.3    Hubalek, M.4    Stulik, J.5    Macela, A.6
  • 19
    • 33845979136 scopus 로고    scopus 로고
    • The immunologically distinct O antigens from Francisella tularensis subspecies tularensis and Francisella novicida are both virulence determinants and protective antigens
    • DOI 10.1128/IAI.01241-06
    • Thomas, R. M., Titball, R. W., Oyston, P. C., Griffin, K., Waters, E., Hitchen, P. G., Michell, S. L., Grice, I. D., Wilson, J. C., and Prior, J. L. (2007) The immunologically distinct O antigens from Francisella tularensis subspecies tularensis and Francisella novicida are both virulence determinants and protective antigens. Infect. Immun. 75, 371-378 (Pubitemid 46047913)
    • (2007) Infection and Immunity , vol.75 , Issue.1 , pp. 371-378
    • Thomas, R.M.1    Titball, R.W.2    Oyston, P.C.F.3    Griffin, K.4    Waters, E.5    Hitchen, P.G.6    Michell, S.L.7    Grice, I.D.8    Wilson, J.C.9    Prior, J.L.10
  • 20
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., Priefer, U., and Pühler, A. (1983) A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bacteria. Nat. Biotechnol. 1, 784-791 (Pubitemid 14239484)
    • (1983) Bio/Technology , vol.1 , Issue.9 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 21
    • 0037721461 scopus 로고    scopus 로고
    • A method for allelic replacement in Francisella tularensis
    • DOI 10.1016/S0378-1097(03)00313-6
    • Golovliov, I., Sjöstedt, A., Mokrievich, A., and Pavlov, V. (2003) A method for allelic replacement in Francisella tularensis. FEMS Microbiol. Lett. 222, 273-280 (Pubitemid 36589005)
    • (2003) FEMS Microbiology Letters , vol.222 , Issue.2 , pp. 273-280
    • Golovliov, I.1    Sjostedt, A.2    Mokrievich, A.3    Pavlov, V.4
  • 22
    • 0002447206 scopus 로고
    • Bacterial lipopolysaccharides: Extraction with phenol-water and further applications of the procedure
    • Westphal, O., and Jann, K. (1965) Bacterial lipopolysaccharides: Extraction with phenol-water and further applications of the procedure. Methods Carbohydr. Chem. 5, 83-91
    • (1965) Methods Carbohydr. Chem. , vol.5 , pp. 83-91
    • Westphal, O.1    Jann, K.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (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
    • Laemmli, U.K.1
  • 24
    • 60149092781 scopus 로고    scopus 로고
    • ProteinQuant Suite: A bundle of automated software tools for label-free quantitative proteomics
    • Mann, B., Madera, M., Sheng, Q., Tang, H., Mechref, Y., and Novotny, M. V. (2008) ProteinQuant Suite: A bundle of automated software tools for label-free quantitative proteomics. Rapid. Commun. Mass Spectrom 22, 3823-3834
    • (2008) Rapid. Commun. Mass Spectrom , vol.22 , pp. 3823-3834
    • Mann, B.1    Madera, M.2    Sheng, Q.3    Tang, H.4    Mechref, Y.5    Novotny, M.V.6
  • 25
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 27
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar, R. C. (2004) MUSCLE: A multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5, 113
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 28
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall, T. A. (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
  • 30
    • 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
  • 31
    • 33750970274 scopus 로고    scopus 로고
    • Comparative proteome analysis of fractions enriched for membrane-associated proteins from Francisella tularensis subsp. tularensis and F. tularensis subsp. holarctica strains
    • DOI 10.1021/pr0601887
    • Pavkova, I., Reichelova, M., Larsson, P., Hubalek, M., Vackova, J., Forsberg, A., Stulik, J. (2006) Comparative proteome analysis of fractions enriched for membrane-associated proteins from Francisella tularensis subsp. tularensis and F. tularensis subsp. holarctica strains. J. Proteome Res. 5, 3125-3134 (Pubitemid 44749229)
    • (2006) Journal of Proteome Research , vol.5 , Issue.11 , pp. 3125-3134
    • Pavkova, I.1    Reichelova, M.2    Larsson, P.3    Hubalek, M.4    Vackova, J.5    Forsberg, A.6    Stulik, J.7
  • 33
    • 0142061580 scopus 로고    scopus 로고
    • Characterization of the O antigen gene cluster and structural analysis of the O antigen of Francisella tularensis subsp. tularensis
    • DOI 10.1099/jmm.0.05184-0
    • Prior, J. L., Prior, R. G., Hitchen, P. G., Diaper, H., Griffin, K. F., Morris, H. R., Dell, A., and Titball, R. W. (2003) Characterization of the O antigen gene cluster and structural analysis of the O antigen of Francisella tularensis subsp. tularensis. J. Med. Microbiol. 52, 845-851 (Pubitemid 37297312)
    • (2003) Journal of Medical Microbiology , vol.52 , Issue.10 , pp. 845-851
    • Prior, J.L.1    Prior, R.G.2    Hitchen, P.G.3    Diaper, H.4    Griffin, K.F.5    Morris, H.R.6    Dell, A.7    Titball, R.W.8
  • 34
    • 0034685684 scopus 로고    scopus 로고
    • Analysis of post-translational modification of mycobacterial proteins using a cassette expression system
    • DOI 10.1016/S0014-5793(00)01553-2, PII S0014579300015532
    • Herrmann, J. L., Delahay, R., Gallagher, A., Robertson, B., and Young, D. (2000) Analysis of post-translational modification of mycobacterial proteins using a cassette expression system. FEBS Lett. 473, 358-362 (Pubitemid 30249154)
    • (2000) FEBS Letters , vol.473 , Issue.3 , pp. 358-362
    • Herrmann, J.L.1    Delahay, R.2    Gallagher, A.3    Robertson, B.4    Young, D.5
  • 36
    • 70350029185 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the surface-associated 42 kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni
    • Scott, N. E., Bogema, D. R., Connolly, A. M., Falconer, L., Djordjevic, S. P., and Cordwell, S. J. (2009) Mass spectrometric characterization of the surface-associated 42 kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni. J. Proteome Res. 8, 4654-4664
    • (2009) J. Proteome Res. , vol.8 , pp. 4654-4664
    • Scott, N.E.1    Bogema, D.R.2    Connolly, A.M.3    Falconer, L.4    Djordjevic, S.P.5    Cordwell, S.J.6
  • 39
    • 54049154653 scopus 로고    scopus 로고
    • Evasion of complement-mediated lysis and complement C3 deposition are regulated by Francisella tularensis lipopolysaccharide O antigen
    • Clay, C. D., Soni, S., Gunn, J. S., and Schlesinger, L. S. (2008) Evasion of complement-mediated lysis and complement C3 deposition are regulated by Francisella tularensis lipopolysaccharide O antigen. J. Immunol. 181, 5568-5578
    • (2008) J. Immunol. , vol.181 , pp. 5568-5578
    • Clay, C.D.1    Soni, S.2    Gunn, J.S.3    Schlesinger, L.S.4
  • 40
    • 0036431682 scopus 로고    scopus 로고
    • Glycosylation of Pseudomonas aeruginosa 1244 pilin: Glycan substrate specificity
    • DOI 10.1046/j.1365-2958.2002.03171.x
    • DiGiandomenico, A., Matewish, M. J., Bisaillon, A., Stehle, J. R., Lam, J. S., and Castric, P. (2002) Glycosylation of Pseudomonas aeruginosa 1244 pilin: Glycan substrate specificity. Mol. Microbiol. 46, 519-530 (Pubitemid 35340961)
    • (2002) Molecular Microbiology , vol.46 , Issue.2 , pp. 519-530
    • DiGiandomenico, A.1    Matewish, M.J.2    Bisaillon, A.3    Stehle, J.R.4    Lam, J.S.5    Castric, P.6
  • 41
    • 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. Glycobiology 21, 138-151
    • (2011) Glycobiology , vol.21 , pp. 138-151
    • Hug, I.1    Feldman, M.F.2
  • 42
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • DOI 10.1046/j.1365-2958.1999.01415.x
    • Szymanski, C. M., Yao, R., Ewing, C. P., Trust, T. J., and Guerry, P. (1999) Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol. Microbiol. 32, 1022-1030 (Pubitemid 29255768)
    • (1999) Molecular Microbiology , vol.32 , Issue.5 , pp. 1022-1030
    • Szymanski, C.M.1    Ruijin, Y.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 43
    • 0036173114 scopus 로고    scopus 로고
    • Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni
    • DOI 10.1046/j.1365-2958.2002.02762.x
    • Linton, D., Allan, E., Karlyshev, A. V., Cronshaw, A. D., and Wren, B. W. (2002) Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. Mol. Microbiol. 43, 497-508 (Pubitemid 34146738)
    • (2002) Molecular Microbiology , vol.43 , Issue.2 , pp. 497-508
    • Linton, D.1    Allan, E.2    Karlyshev, A.V.3    Cronshaw, A.D.4    Wren, B.W.5
  • 45
    • 0035860764 scopus 로고    scopus 로고
    • Identification of the carbohydrate moieities and glycosylation motifs in Campylobacter jejuni flagellin
    • Thibault, P., Logan, S. M., Kelly, J. F., Brisson, J. R., Ewing, C. P., Trust, T. J., and Guerry, P. (2001) Identification of the carbohydrate moieities and glycosylation motifs in Campylobacter jejuni flagellin. J. Biol. Chem. 276, 34862-34870
    • (2001) J. Biol. Chem. , vol.276 , pp. 34862-34870
    • Thibault, P.1    Logan, S.M.2    Kelly, J.F.3    Brisson, J.R.4    Ewing, C.P.5    Trust, T.J.6    Guerry, P.7
  • 46
    • 1942540030 scopus 로고    scopus 로고
    • Structural and Genetic Characterization of Glycosylation of Type a Flagellin in Pseudomonas aeruginosa
    • DOI 10.1128/JB.186.9.2523-2531.2004
    • Schirm, M., Arora, S. K., Verma, A., Vinogradov, E., Thibault, P., Ramphal, R., and Logan, S. M. (2004) Structural and genetic characterization of flycosylation of type a flagellin in Pseudomonas aeruginosa. J. Bacteriol 186, 2523-2531 (Pubitemid 38525904)
    • (2004) Journal of Bacteriology , vol.186 , Issue.9 , pp. 2523-2531
    • Schirm, M.1    Arora, S.K.2    Verma, A.3    Vinogradov, E.4    Thibault, P.5    Ramphal, R.6    Logan, S.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.