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Volumn 7, Issue 9, 2011, Pages

Burkholderia cenocepacia bc2l-c is a super lectin with dual specificity and proinflammatory activity

Author keywords

[No Author keywords available]

Indexed keywords

BC2L C LECTIN; EPITOPE; FUCOSE; HEPTOSE; INTERLEUKIN 8; LECTIN; MANNOSE; UNCLASSIFIED DRUG; AUTACOID; FUCOSE BINDING LECTIN; FUCOSE-BINDING LECTIN; MANNOSE BINDING LECTIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 84859999995     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002238     Document Type: Article
Times cited : (56)

References (49)
  • 1
    • 44249085887 scopus 로고    scopus 로고
    • Burkholderia cepacia complex bacteria: opportunistic pathogens with important natural biology
    • Mahenthiralingam E, Baldwin A, Dowson CG, (2008) Burkholderia cepacia complex bacteria: opportunistic pathogens with important natural biology. J Appl Microbiol 104: 1539-1551.
    • (2008) J Appl Microbiol , vol.104 , pp. 1539-1551
    • Mahenthiralingam, E.1    Baldwin, A.2    Dowson, C.G.3
  • 3
    • 0028943646 scopus 로고
    • Burkholderia cepacia and cystic fibrosis: do natural environments present a potential hazard?
    • Butler SL, Doherty CJ, Hughes JE, Nelson JW, Govan JR, (1995) Burkholderia cepacia and cystic fibrosis: do natural environments present a potential hazard? J Clin Microbiol 33: 1001-1004.
    • (1995) J Clin Microbiol , vol.33 , pp. 1001-1004
    • Butler, S.L.1    Doherty, C.J.2    Hughes, J.E.3    Nelson, J.W.4    Govan, J.R.5
  • 4
    • 0036668118 scopus 로고    scopus 로고
    • Influence of taxonomic status on the in vitro antimicrobial susceptibility of the Burkholderia cepacia complex
    • Nzula S, Vandamme P, Govan JR, (2002) Influence of taxonomic status on the in vitro antimicrobial susceptibility of the Burkholderia cepacia complex. J Antimicrob Chemother 50: 265-269.
    • (2002) J Antimicrob Chemother , vol.50 , pp. 265-269
    • Nzula, S.1    Vandamme, P.2    Govan, J.R.3
  • 5
    • 69949123399 scopus 로고    scopus 로고
    • Interactions of Burkholderia cenocepacia and other Burkholderia cepacia complex bacteria with epithelial and phagocytic cells
    • Saldías MS, Valvano MA, (2009) Interactions of Burkholderia cenocepacia and other Burkholderia cepacia complex bacteria with epithelial and phagocytic cells. Microbiology 155: 2809-2817.
    • (2009) Microbiology , vol.155 , pp. 2809-2817
    • Saldías, M.S.1    Valvano, M.A.2
  • 6
    • 77957726305 scopus 로고    scopus 로고
    • A decade of Burkholderia cenocepacia virulence determinant research
    • Loutet SA, Valvano MA, (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
  • 7
    • 42449095600 scopus 로고    scopus 로고
    • Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia
    • Lameignere E, Malinovska L, Slavikova M, Duchaud E, Mitchell EP, et al. (2008) Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia. Biochem J 411: 307-318.
    • (2008) Biochem J , vol.411 , pp. 307-318
    • Lameignere, E.1    Malinovska, L.2    Slavikova, M.3    Duchaud, E.4    Mitchell, E.P.5
  • 8
    • 1442348321 scopus 로고    scopus 로고
    • Structures of the lectins from Pseudomonas aeruginosa: Insights into molecular basis for host glycan recognition
    • Imberty A, Wimmerova M, Mitchell EP, Gilboa-Garber N, (2004) Structures of the lectins from Pseudomonas aeruginosa: Insights into molecular basis for host glycan recognition. Microb Infect 6: 222-229.
    • (2004) Microb Infect , vol.6 , pp. 222-229
    • Imberty, A.1    Wimmerova, M.2    Mitchell, E.P.3    Gilboa-Garber, N.4
  • 9
    • 65449143628 scopus 로고    scopus 로고
    • Role of LecA and LecB lectins in Pseudomonas aeruginosa induced lung injury and effect of carbohydrates ligands
    • Chemani C, Imberty A, de Bentzman S, Pierre P, Wimmerová M, et al. (2009) Role of LecA and LecB lectins in Pseudomonas aeruginosa induced lung injury and effect of carbohydrates ligands. Infect Immun 77: 2065-2075.
    • (2009) Infect Immun , vol.77 , pp. 2065-2075
    • Chemani, C.1    Imberty, A.2    de Bentzman, S.3    Pierre, P.4    Wimmerová, M.5
  • 10
    • 57649218723 scopus 로고    scopus 로고
    • Inhibition and dispersion of Pseudomonas aeruginosa biofilms by glycopeptide dendrimers targeting the fucose-specific lectin LecB
    • Johansson EM, Crusz SA, Kolomiets E, Buts L, Kadam RU, et al. (2008) Inhibition and dispersion of Pseudomonas aeruginosa biofilms by glycopeptide dendrimers targeting the fucose-specific lectin LecB. Chem Biol 15: 1249-1257.
    • (2008) Chem Biol , vol.15 , pp. 1249-1257
    • Johansson, E.M.1    Crusz, S.A.2    Kolomiets, E.3    Buts, L.4    Kadam, R.U.5
  • 11
    • 70849085834 scopus 로고    scopus 로고
    • Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin
    • Lameignere E, Shiao TC, Roy R, Wimmerova M, Dubreuil F, et al. (2010) Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin. Glycobiology 20: 87-98.
    • (2010) Glycobiology , vol.20 , pp. 87-98
    • Lameignere, E.1    Shiao, T.C.2    Roy, R.3    Wimmerova, M.4    Dubreuil, F.5
  • 12
    • 73449121072 scopus 로고    scopus 로고
    • A TNF-like trimeric lectin domain from Burkholderia cenocepacia with specificity for fucosylated human histo-blood group antigens
    • Sulak O, Cioci G, Delia M, Lahmann M, Varrot A, et al. (2010) A TNF-like trimeric lectin domain from Burkholderia cenocepacia with specificity for fucosylated human histo-blood group antigens. Structure 18: 59-72.
    • (2010) Structure , vol.18 , pp. 59-72
    • Sulak, O.1    Cioci, G.2    Delia, M.3    Lahmann, M.4    Varrot, A.5
  • 13
    • 34347396244 scopus 로고    scopus 로고
    • Engineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference
    • Adam J, Pokorna M, Sabin C, Mitchell EP, Imberty A, et al. (2007) Engineering of PA-IIL lectin from Pseudomonas aeruginosa- Unravelling the role of the specificity loop for sugar preference. BMC Struct Biol 7: 36.
    • (2007) BMC Struct Biol , vol.7 , pp. 36
    • Adam, J.1    Pokorna, M.2    Sabin, C.3    Mitchell, E.P.4    Imberty, A.5
  • 14
    • 58149107409 scopus 로고    scopus 로고
    • Chemical and biological features of Burkholderia cepacia complex lipopolysaccharides
    • De Soyza A, Silipo A, Lanzetta R, Govan JR, Molinaro A, (2008) Chemical and biological features of Burkholderia cepacia complex lipopolysaccharides. Innate Immun 14: 127-144.
    • (2008) Innate Immun , vol.14 , pp. 127-144
    • De Soyza, A.1    Silipo, A.2    Lanzetta, R.3    Govan, J.R.4    Molinaro, A.5
  • 15
    • 64549163217 scopus 로고    scopus 로고
    • Structural elucidation of the novel core oligosaccharide from LPS of Burkholderia cepacia serogroup O4
    • Masoud H, Perry MB, Brisson JR, Uhrin D, Li J, et al. (2009) Structural elucidation of the novel core oligosaccharide from LPS of Burkholderia cepacia serogroup O4. Glycobiology 19: 462-471.
    • (2009) Glycobiology , vol.19 , pp. 462-471
    • Masoud, H.1    Perry, M.B.2    Brisson, J.R.3    Uhrin, D.4    Li, J.5
  • 16
    • 0036895829 scopus 로고    scopus 로고
    • Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients
    • Mitchell E, Houles C, Sudakevitz D, Wimmerova M, Gautier C, et al. (2002) Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients. Nature Struct Biol 9: 918-921.
    • (2002) Nature Struct Biol , vol.9 , pp. 918-921
    • Mitchell, E.1    Houles, C.2    Sudakevitz, D.3    Wimmerova, M.4    Gautier, C.5
  • 17
    • 33745118300 scopus 로고    scopus 로고
    • Unusual entropy-driven affinity of Chromobacterium violaceum lectin CV-IIL toward fucose and mannose
    • Pokorna M, Cioci G, Perret S, Rebuffet E, Kostlanova N, et al. (2006) Unusual entropy-driven affinity of Chromobacterium violaceum lectin CV-IIL toward fucose and mannose. Biochemistry 45: 7501-7510.
    • (2006) Biochemistry , vol.45 , pp. 7501-7510
    • Pokorna, M.1    Cioci, G.2    Perret, S.3    Rebuffet, E.4    Kostlanova, N.5
  • 18
    • 2442614012 scopus 로고    scopus 로고
    • A new Ralstonia solanacearum high affinity mannose-binding lectin RS-IIL structurally resembling the Pseudomonas aeruginosa fucose-specific lectin PA-IIL
    • Sudakevitz D, Kostlanova N, Blatman-Jan G, Mitchell EP, Lerrer B, et al. (2004) A new Ralstonia solanacearum high affinity mannose-binding lectin RS-IIL structurally resembling the Pseudomonas aeruginosa fucose-specific lectin PA-IIL. Mol Microbiol 52: 691-700.
    • (2004) Mol Microbiol , vol.52 , pp. 691-700
    • Sudakevitz, D.1    Kostlanova, N.2    Blatman-Jan, G.3    Mitchell, E.P.4    Lerrer, B.5
  • 19
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • Ideo H, Seko A, Ishizuka I, Yamashita K, (2003) The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity. Glycobiology 13: 713-723.
    • (2003) Glycobiology , vol.13 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 20
    • 34249095527 scopus 로고    scopus 로고
    • Phylogenetic and specificity studies of two-domain GNA-related lectins: generation of multispecificity through domain duplication and divergent evolution
    • Van Damme EJ, Nakamura-Tsuruta S, Smith DF, Ongenaert M, Winter HC, et al. (2007) Phylogenetic and specificity studies of two-domain GNA-related lectins: generation of multispecificity through domain duplication and divergent evolution. Biochem J 404: 51-61.
    • (2007) Biochem J , vol.404 , pp. 51-61
    • Van Damme, E.J.1    Nakamura-Tsuruta, S.2    Smith, D.F.3    Ongenaert, M.4    Winter, H.C.5
  • 21
    • 19044365015 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation
    • Tielker D, Hacker S, Loris R, Strathmann M, Wingender J, et al. (2005) Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation. Microbiology 151: 1313-1323.
    • (2005) Microbiology , vol.151 , pp. 1313-1323
    • Tielker, D.1    Hacker, S.2    Loris, R.3    Strathmann, M.4    Wingender, J.5
  • 22
    • 79951634140 scopus 로고    scopus 로고
    • Glycosylation is required for outer membrane localization of the lectin LecB in Pseudomonas aeruginosa
    • J Bacteriol in press, doi:
    • Bartels KM, Funken H, Knapp A, Brocker M, Bott M, et al. (2011) Glycosylation is required for outer membrane localization of the lectin LecB in Pseudomonas aeruginosa. J Bacteriol in press doi:10.1128/JB.01507-01510.
    • (2011)
    • Bartels, K.M.1    Funken, H.2    Knapp, A.3    Brocker, M.4    Bott, M.5
  • 25
  • 26
    • 36949021096 scopus 로고    scopus 로고
    • Burkholderia cenocepacia ET12 strain activates TNFR1 signalling in cystic fibrosis airway epithelial cells
    • Sajjan US, Hershenson MB, Forstner JF, LiPuma JJ, (2008) Burkholderia cenocepacia ET12 strain activates TNFR1 signalling in cystic fibrosis airway epithelial cells. Cell Microbiol 10: 188-201.
    • (2008) Cell Microbiol , vol.10 , pp. 188-201
    • Sajjan, U.S.1    Hershenson, M.B.2    Forstner, J.F.3    LiPuma, J.J.4
  • 27
    • 80053572292 scopus 로고    scopus 로고
    • Crystal and molecular structure of methyl L-glycero-α-D-manno-heptopyranoside, and synthesis of 1->7 linked L-glycero-α-D-manno-heptobiose and its methyl-α-glycoside
    • Carbohydr. Res. in press, (DOI: 10.1016/j.carres.2011.05.033)
    • Artner D, Stanetty C, Mereiter C, Zamyatina A, Kosma P, (2011) Crystal and molecular structure of methyl L-glycero-α-D-manno-heptopyranoside, and synthesis of 1->7 linked L-glycero-α-D-manno-heptobiose and its methyl-α-glycoside. Carbohydr. Res. in press (DOI: 10.1016/j.carres.2011.05.033).
    • (2011)
    • Artner, D.1    Stanetty, C.2    Mereiter, C.3    Zamyatina, A.4    Kosma, P.5
  • 28
    • 0032770418 scopus 로고    scopus 로고
    • Synthesis of Pseudomonas aeruginosa lipopolysaccharide core antigens containing 7-O-carbamoyl-L-glycero-D-manno-heptopyranosyl residues
    • Reiter A, Zamyatina A, Schindl H, Hofinger A, Kosma P, (1999) Synthesis of Pseudomonas aeruginosa lipopolysaccharide core antigens containing 7-O-carbamoyl-L-glycero-D-manno-heptopyranosyl residues. Carbohydr Res 317: 39-52.
    • (1999) Carbohydr Res , vol.317 , pp. 39-52
    • Reiter, A.1    Zamyatina, A.2    Schindl, H.3    Hofinger, A.4    Kosma, P.5
  • 29
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T, Williston S, Brandts JF, Lin LN, (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179: 131-137.
    • (1989) Anal Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 33
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an Automated Program for Molecular Replacement
    • Vagin A, Teplyakov A, (1997) MOLREP: an Automated Program for Molecular Replacement. J Appl Crystallogr 30: 1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 35
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 37
    • 0000243829 scopus 로고
    • Procheck - a Program to Check the Stereochemical Quality of Protein Structures
    • Laskowski RA, Macarthur MW, Moss DS, Thornton JM, (1993) Procheck- a Program to Check the Stereochemical Quality of Protein Structures. J Appl Crystallogr 26: 283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 0037681028 scopus 로고    scopus 로고
    • Structure, conformation and dynamics of bioactive oligosaccharides: theoretical approaches and experimental validations
    • Imberty A, Pérez S, (2000) Structure, conformation and dynamics of bioactive oligosaccharides: theoretical approaches and experimental validations. Chem Rev 100: 4567-4588.
    • (2000) Chem Rev , vol.100 , pp. 4567-4588
    • Imberty, A.1    Pérez, S.2
  • 39
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI, (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Cryst 36: 860-864.
    • (2003) J Appl Cryst , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 40
    • 0034849689 scopus 로고    scopus 로고
    • MASSHA - a graphics system for rigid-body modelling of macromolecular complexes against solution scattering data
    • Konarev PV, Petoukhov MV, Svergun DI, (2001) MASSHA- a graphics system for rigid-body modelling of macromolecular complexes against solution scattering data. J Appl Cryst 34: 527-532.
    • (2001) J Appl Cryst , vol.34 , pp. 527-532
    • Konarev, P.V.1    Petoukhov, M.V.2    Svergun, D.I.3
  • 41
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W, (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128: 82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 42
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N, (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142: 334-347.
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 43
    • 40649123787 scopus 로고    scopus 로고
    • Computational resources for cryo-electron tomography in Bsoft
    • Heymann JB, Cardone G, Winkler DC, Steven AC, (2008) Computational resources for cryo-electron tomography in Bsoft. J Struct Biol 161: 232-242.
    • (2008) J Struct Biol , vol.161 , pp. 232-242
    • Heymann, J.B.1    Cardone, G.2    Winkler, D.C.3    Steven, A.C.4
  • 45
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, Radermacher M, Penczek P, Zhu J, Li Y, et al. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116: 190-199.
    • (1996) J Struct Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5
  • 46
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh TR, Gao H, Baxter WT, Asturias FJ, Boisset N, et al. (2008) SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nature protocols 3: 1941-1974.
    • (2008) Nature Protocols , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5
  • 47
    • 11044237547 scopus 로고    scopus 로고
    • Wzx proteins involved in biosynthesis of O antigen function in association with the first sugar of the O-specific lipopolysaccharide subunit
    • Marolda CL, Vicarioli J, Valvano MA, (2004) Wzx proteins involved in biosynthesis of O antigen function in association with the first sugar of the O-specific lipopolysaccharide subunit. Microbiology 150: 4095-4105.
    • (2004) Microbiology , vol.150 , pp. 4095-4105
    • Marolda, C.L.1    Vicarioli, J.2    Valvano, M.A.3
  • 48
    • 42949164547 scopus 로고    scopus 로고
    • A novel sensor kinase-response regulator hybrid controls biofilm formation and type VI secretion system activity in Burkholderia cenocepacia
    • Aubert DF, Flannagan RS, Valvano MA, (2008) A novel sensor kinase-response regulator hybrid controls biofilm formation and type VI secretion system activity in Burkholderia cenocepacia. Infect Immun 76: 1979-1991.
    • (2008) Infect Immun , vol.76 , pp. 1979-1991
    • Aubert, D.F.1    Flannagan, R.S.2    Valvano, M.A.3
  • 49
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski DH, Helinski DR, (1979) Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc Natl Acad Sci U S A 76: 1648-1652.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2


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