메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; MENINGOCOCCUS VACCINE; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN ZNUD; UNCLASSIFIED DRUG; ZINC; BACTERIAL PROTEIN; CATION TRANSPORT PROTEIN; ZNUD PROTEIN, NEISSERIA MENINGITIDIS;

EID: 84939606863     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8996     Document Type: Article
Times cited : (58)

References (52)
  • 1
    • 84863899006 scopus 로고    scopus 로고
    • Nutritional immunity: Transition metals at the pathogen-host interface
    • Hood, M. I. & Skaar, E. P. Nutritional immunity: transition metals at the pathogen-host interface. Nat. Rev. Microbiol. 10, 525-537 (2012).
    • (2012) Nat. Rev. Microbiol , vol.10 , pp. 525-537
    • Hood, M.I.1    Skaar, E.P.2
  • 2
    • 59049102145 scopus 로고    scopus 로고
    • Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex
    • Krieg, S. et al. Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex. Proc. Natl Acad. Sci. USA 106, 1045-1050 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1045-1050
    • Krieg, S.1
  • 3
    • 84857783784 scopus 로고    scopus 로고
    • Structural basis for iron piracy by pathogenic Neisseria
    • Noinaj, N. et al. Structural basis for iron piracy by pathogenic Neisseria. Nature 483, 53-58 (2012).
    • (2012) Nature , vol.483 , pp. 53-58
    • Noinaj, N.1
  • 4
    • 84897918689 scopus 로고    scopus 로고
    • Competition for zinc binding in the host-pathogen interaction Front
    • Cerasi, M., Ammendola, S. & Battistoni, A. Competition for zinc binding in the host-pathogen interaction. Front. Cell Infect. Microbiol. 3, 108 (2013).
    • (2013) Cell Infect. Microbiol , vol.3 , pp. 108
    • Cerasi, M.1    Ammendola, S.2    Battistoni, A.3
  • 5
    • 77949885386 scopus 로고    scopus 로고
    • Nutritional immunity beyond iron: A role for manganese and zinc
    • Kehl-Fie, T. E. & Skaar, E. P. Nutritional immunity beyond iron: a role for manganese and zinc. Curr. Opin. Chem. Biol. 14, 218-224 (2010).
    • (2010) Curr. Opin. Chem. Biol , vol.14 , pp. 218-224
    • Kehl-Fie, T.E.1    Skaar, E.P.2
  • 6
    • 84887281591 scopus 로고    scopus 로고
    • Zinc piracy as a mechanism of Neisseria meningitidis for evasion of nutritional immunity
    • Stork, M. et al. Zinc piracy as a mechanism of Neisseria meningitidis for evasion of nutritional immunity. PLoS Pathog. 9, e1003733 (2013).
    • (2013) PLoS Pathog , vol.9 , pp. e1003733
    • Stork, M.1
  • 7
    • 70350348305 scopus 로고    scopus 로고
    • Metalloproteomes: A bioinformatic approach
    • Andreini, C., Bertini, I. & Rosato, A. Metalloproteomes: a bioinformatic approach. Acc. Chem. Res. 42, 1471-1479 (2009).
    • (2009) Acc. Chem. Res , vol.42 , pp. 1471-1479
    • Andreini, C.1    Bertini, I.2    Rosato, A.3
  • 9
    • 0021236274 scopus 로고
    • Albumin bound and alpha 2-macroglobulin bound zinc concentrations in the sera of healthy adults
    • Foote, J. W. & Delves, H. T. Albumin bound and alpha 2-macroglobulin bound zinc concentrations in the sera of healthy adults. J. Clin. Pathol. 37, 1050-1054 (1984).
    • (1984) J. Clin. Pathol , vol.37 , pp. 1050-1054
    • Foote, J.W.1    Delves, H.T.2
  • 10
    • 0029028318 scopus 로고
    • A novel dialysis procedure measuring free Zn2+ in bovine milk and plasma
    • Zhang, P. & Allen, J. C. A novel dialysis procedure measuring free Zn2+ in bovine milk and plasma. J. Nutr. 125, 1904-1910 (1995).
    • (1995) J. Nutr , vol.125 , pp. 1904-1910
    • Zhang, P.1    Allen, J.C.2
  • 11
    • 0033935895 scopus 로고    scopus 로고
    • Albumin facilitates zinc acquisition by endothelial cells
    • Rowe, D. J. & Bobilya, D. J. Albumin facilitates zinc acquisition by endothelial cells. Proc. Soc. Exp. Biol. Med. 224, 178-186 (2000).
    • (2000) Proc. Soc. Exp. Biol. Med , vol.224 , pp. 178-186
    • Rowe, D.J.1    Bobilya, D.J.2
  • 12
    • 84880839043 scopus 로고    scopus 로고
    • In vitro resistance mechanisms of Neisseria meningitidis against neutrophil extracellular traps
    • Lappann, M. et al. In vitro resistance mechanisms of Neisseria meningitidis against neutrophil extracellular traps. Mol. Microbiol. 89, 433-449 (2013).
    • (2013) Mol. Microbiol , vol.89 , pp. 433-449
    • Lappann, M.1
  • 13
    • 77957684250 scopus 로고    scopus 로고
    • An outer membrane receptor of Neisseria meningitidis involved in zinc acquisition with vaccine potential
    • Stork, M. et al. An outer membrane receptor of Neisseria meningitidis involved in zinc acquisition with vaccine potential. PLoS Pathog. 6, e1000969 (2010).
    • (2010) PLoS Pathog , vol.6 , pp. e1000969
    • Stork, M.1
  • 14
    • 84871096238 scopus 로고    scopus 로고
    • The zinc-responsive regulon of Neisseria meningitidis comprises 17 genes under control of a Zur element
    • Pawlik, M. C. et al. The zinc-responsive regulon of Neisseria meningitidis comprises 17 genes under control of a Zur element. J. Bacteriol. 194, 6594-6603 (2012).
    • (2012) J. Bacteriol , vol.194 , pp. 6594-6603
    • Pawlik, M.C.1
  • 16
    • 79958032046 scopus 로고    scopus 로고
    • Transcriptome analysis of Neisseria meningitidis in human whole blood and mutagenesis studies identify virulence factors involved in blood survival
    • Echenique-Rivera, H. et al. Transcriptome analysis of Neisseria meningitidis in human whole blood and mutagenesis studies identify virulence factors involved in blood survival. PLoS Pathog. 7, e1002027 (2011).
    • (2011) PLoS Pathog , vol.7 , pp. e1002027
    • Echenique-Rivera, H.1
  • 17
    • 0344284618 scopus 로고    scopus 로고
    • Pathogenesis therapy, and prevention of meningococcal sepsis
    • Stephens, D. S. & Zimmer, S. M. Pathogenesis, therapy, and prevention of meningococcal sepsis. Curr. Infect. Dis. Rep. 4, 377-386 (2002).
    • (2002) Curr. Infect. Dis. Rep , vol.4 , pp. 377-386
    • Stephens, D.S.1    Zimmer, S.M.2
  • 18
    • 0020518256 scopus 로고
    • Antigenic similarities between brain components and bacteria causing meningitis. Implications for vaccine development and pathogenesis
    • Finne, J., Leinonen, M. & Makela, P. H. Antigenic similarities between brain components and bacteria causing meningitis. Implications for vaccine development and pathogenesis. Lancet 2, 355-357 (1983).
    • (1983) Lancet , vol.2 , pp. 355-357
    • Finne, J.1    Leinonen, M.2    Makela, P.H.3
  • 19
    • 84877791728 scopus 로고    scopus 로고
    • ZnuD, a potential candidate for a simple and universal Neisseria meningitidis vaccine
    • Hubert, K. et al. ZnuD, a potential candidate for a simple and universal Neisseria meningitidis vaccine. Infect. Immun. 81, 1915-1927 (2013).
    • (2013) Infect. Immun , vol.81 , pp. 1915-1927
    • Hubert, K.1
  • 20
  • 22
    • 46149094595 scopus 로고    scopus 로고
    • New substrates for TonBdependent transport: Do we only see the 'tip of the iceberg'?
    • Schauer, K., Rodionov, D. A. & de Reuse, H. New substrates for TonBdependent transport: do we only see the 'tip of the iceberg'? Trends Biochem. Sci. 33, 330-338 (2008).
    • (2008) Trends Biochem. Sci , vol.33 , pp. 330-338
    • Schauer, K.1    Rodionov, D.A.2    De Reuse, H.3
  • 23
    • 84857948447 scopus 로고    scopus 로고
    • The Neisseria meningitidis ZnuD zinc receptor contributes to interactions with epithelial cells and supports heme utilization when expressed in Escherichia coli
    • Kumar, P., Sannigrahi, S. & Tzeng, Y. L. The Neisseria meningitidis ZnuD zinc receptor contributes to interactions with epithelial cells and supports heme utilization when expressed in Escherichia coli. Infect. Immun. 80, 657-667 (2012).
    • (2012) Infect. Immun , vol.80 , pp. 657-667
    • Kumar, P.1    Sannigrahi, S.2    Tzeng, Y.L.3
  • 24
    • 84874093218 scopus 로고    scopus 로고
    • Use of a molecular decoy to segregate transport from antigenicity in the FrpB iron transporter from Neisseria meningitidis
    • Saleem, M. et al. Use of a molecular decoy to segregate transport from antigenicity in the FrpB iron transporter from Neisseria meningitidis. PLoS ONE 9, e56746 (2013).
    • (2013) PLoS ONE , vol.9 , pp. e56746
    • Saleem, M.1
  • 25
    • 84855724118 scopus 로고    scopus 로고
    • The ironrepressed, AraC-like regulator MpeR activates expression of fetA in Neisseria gonorrhoeae
    • Hollander, A., Mercante, A. D., Shafer, W. M. & Cornelissen, C. N. The ironrepressed, AraC-like regulator MpeR activates expression of fetA in Neisseria gonorrhoeae. Infect. Immun. 79, 4764-4776 (2011).
    • (2011) Infect. Immun , vol.79 , pp. 4764-4776
    • Hollander, A.1    Mercante, A.D.2    Shafer, W.M.3    Cornelissen, C.N.4
  • 26
    • 40449131050 scopus 로고    scopus 로고
    • Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms
    • Xu, Y., Feng, L., Jeffrey, P. D., Shi, Y. & Morel, F. M. Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms. Nature 452, 56-61 (2008).
    • (2008) Nature , vol.452 , pp. 56-61
    • Xu, Y.1    Feng, L.2    Jeffrey, P.D.3    Shi, Y.4    Morel, F.M.5
  • 27
    • 77951944746 scopus 로고    scopus 로고
    • Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium
    • Wernimont, A. K. et al. Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium. Nat. Struct. Mol. Biol. 17, 596-601 (2010).
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 596-601
    • Wernimont, A.K.1
  • 28
    • 33845505955 scopus 로고    scopus 로고
    • Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates proteinprotein interactions
    • Paul, I., Cui, J. & Maynard, E. L. Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates proteinprotein interactions. Proc. Natl Acad. Sci. USA 103, 18475-18480 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 18475-18480
    • Paul, I.1    Cui, J.2    Maynard, E.L.3
  • 29
    • 34447339675 scopus 로고    scopus 로고
    • Mechanics of force propagation in TonB-dependent outer membrane transport
    • Gumbart, J., Wiener, M. C. & Tajkhorshid, E. Mechanics of force propagation in TonB-dependent outer membrane transport. Biophys. J. 93, 496-504 (2007).
    • (2007) Biophys. J. , vol.93 , pp. 496-504
    • Gumbart, J.1    Wiener, M.C.2    Tajkhorshid, E.3
  • 30
    • 84908587091 scopus 로고    scopus 로고
    • Genetic manipulation of Neisseria gonorrhoeae
    • Chapter 4, Unit 4A 2
    • Dillard, J. P. Genetic manipulation of Neisseria gonorrhoeae. Curr. Protoc. Microbiol.. Chapter 4, Unit 4A 2 (2006).
    • (2006) Curr. Protoc. Microbiol
    • Dillard, J.P.1
  • 31
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207-234 (2005).
    • (2005) Protein Expr. Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 32
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 34
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. & Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993).
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 35
    • 84867820827 scopus 로고    scopus 로고
    • LAMBADA and InflateGRO2: Efficient membrane alignment and insertion of membrane proteins for molecular dynamics simulations
    • Schmidt, T. H. & Kandt, C. LAMBADA and InflateGRO2: efficient membrane alignment and insertion of membrane proteins for molecular dynamics simulations. J. Chem. Inf. Model. 52, 2657-2669 (2012).
    • (2012) J. Chem. Inf. Model , vol.52 , pp. 2657-2669
    • Schmidt, T.H.1    Kandt, C.2
  • 36
    • 84875592758 scopus 로고    scopus 로고
    • GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit
    • Pronk, S. et al. GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29, 845-854 (2013).
    • (2013) Bioinformatics , vol.29 , pp. 845-854
    • Pronk, S.1
  • 37
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • Klauda, J. B., Venable, R. M. & Freites, J. A. Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types. J. Phys. Chem. B 114, 7830-7843 (2010).
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7830-7843
    • Klauda, J.B.1    Venable, R.M.2    Freites, J.A.3
  • 38
    • 84865723813 scopus 로고    scopus 로고
    • Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone and side-chain dihedral angles
    • Best, R. B. et al. Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone and side-chain dihedral angles. J. Chem. Theory Comput. 8, 3257-3273 (2012).
    • (2012) J. Chem. Theory Comput , vol.8 , pp. 3257-3273
    • Best, R.B.1
  • 40
    • 84879379897 scopus 로고    scopus 로고
    • QM/MM molecular dynamics simulations of the hydration of Mg (II) and Zn (II) ions
    • Riahi, S., Roux, B. & Rowley, C. N. QM/MM molecular dynamics simulations of the hydration of Mg (II) and Zn (II) ions. Can. J. Chem. 91, 552-558 (2013).
    • (2013) Can. J. Chem , vol.91 , pp. 552-558
    • Riahi, S.1    Roux, B.2    Rowley, C.N.3
  • 41
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N- log(N) method for Ewald sums in large systems
    • Darden, T., York, D. & Pedersen, L. Particle mesh Ewald: An N- log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089-10092 (1993).
    • (1993) J. Chem. Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 42
    • 33645961739 scopus 로고
    • A smooth particle mesh Ewald method
    • Essmann, U. et al. A smooth particle mesh Ewald method. J. Chem. Phys. 103, 8577-8593 (1995).
    • (1995) J. Chem. Phys , vol.103 , pp. 8577-8593
    • Essmann, U.1
  • 43
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • Nose, S. & klein, M. L. Constant pressure molecular dynamics for molecular systems. Mol. Phys. 50, 1055-1076 (1983).
    • (1983) Mol. Phys , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.L.2
  • 44
    • 0019707626 scopus 로고
    • Polymorphic transitions in single-crystals - A new molecular-dynamics method
    • Parrinello, M. & Rahman, A. Polymorphic transitions in single-crystals - a new molecular-dynamics method. J. Appl. Phys. 52, 7182-7190 (1981).
    • (1981) J. Appl. Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 45
    • 84943502952 scopus 로고
    • Molecular dynamics method for simulations in the canonical ensemble
    • Nose, S. Molecular dynamics method for simulations in the canonical ensemble. Mol. Phys. 52, 255-268 (1984).
    • (1984) Mol. Phys , vol.52 , pp. 255-268
    • Nose, S.1
  • 46
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. Canonical dynamics: equilibrium phase-space distributions. Phys. Rev. 31, 1695 (1985).
    • (1985) Phys. Rev , vol.31 , pp. 1695
    • Hoover, W.G.1
  • 47
    • 84939642673 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithm
    • Miyamoto, S. & Kollman, P. A. SETTLE: an analytical version of the SHAKE and RATTLE algorithm. J. Comp. Chem. 13, 1695-1697 (1992).
    • (1992) J. Comp. Chem , vol.13 , pp. 1695-1697
    • Miyamoto, S.1    Kollman, P.A.2
  • 48
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • Hess, B. P-LINCS: a parallel linear constraint solver for molecular simulation. J. Chem. Theory Comput. 4, 116-122 (2008).
    • (2008) J. Chem. Theory Comput , vol.4 , pp. 116-122
    • Hess, B.1
  • 49
    • 79958185452 scopus 로고    scopus 로고
    • MDAnalysis: A toolkit for the analysis of molecular dynamics simulations
    • Michaud-Agrawal, N., Denning, E. J., Woolf, T. B. & Beckstein, O. MDAnalysis: a toolkit for the analysis of molecular dynamics simulations. J. Comp. Chem. 32, 2319-2327 (2011).
    • (2011) J. Comp. Chem , vol.32 , pp. 2319-2327
    • Michaud-Agrawal, N.1    Denning, E.J.2    Woolf, T.B.3    Beckstein, O.4
  • 52
    • 38649130696 scopus 로고    scopus 로고
    • Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli
    • Yatsunyk, L. A. et al. Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli. J. Biol. Inorg. Chem. 13, 271-288 (2008).
    • (2008) J. Biol. Inorg. Chem , vol.13 , pp. 271-288
    • Yatsunyk, L.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.