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Volumn 24, Issue 2, 2016, Pages 221-231

Structural Insights into Outer Membrane Permeability of Acinetobacter baumannii

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; ARGININE; BENZOIC ACID; FOSFOMYCIN; GLUCOSE; GLUTAMIC ACID; GLUTAMINE; GLYCINE; IMIPENEM; LIPOSOME; MALTOSE; MEROPENEM; PHENYLALANINE; PUTRESCINE; TRYPTOPHAN; OUTER MEMBRANE PROTEIN;

EID: 84955517726     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.12.009     Document Type: Article
Times cited : (42)

References (49)
  • 1
    • 84879918924 scopus 로고    scopus 로고
    • Carbapenem resistance in Acinetobacter baumannii: Laboratory challenges, mechanistic insights and therapeutic strategies
    • I. Abbott, G.M. Cerqueira, S. Bhuiyan, and A.Y. Peleg Carbapenem resistance in Acinetobacter baumannii: laboratory challenges, mechanistic insights and therapeutic strategies Expert Rev. Anti Infect. Ther. 11 2013 395 409
    • (2013) Expert Rev. Anti Infect. Ther. , vol.11 , pp. 395-409
    • Abbott, I.1    Cerqueira, G.M.2    Bhuiyan, S.3    Peleg, A.Y.4
  • 3
    • 0026545214 scopus 로고
    • Investigation of the selectivity of maltoporin channels using mutant LamB proteins: Mutations changing the maltodextrin binding site
    • R. Benz, G. Francis, T. Nakae, and T. Ferenci Investigation of the selectivity of maltoporin channels using mutant LamB proteins: mutations changing the maltodextrin binding site Biochim. Biophys. Acta 1104 1992 299 307
    • (1992) Biochim. Biophys. Acta , vol.1104 , pp. 299-307
    • Benz, R.1    Francis, G.2    Nakae, T.3    Ferenci, T.4
  • 5
    • 79961240781 scopus 로고    scopus 로고
    • Proteomic and functional analyses reveal a unique lifestyle for Acinetobacter baumannii biofilms and a key role for histidine metabolism
    • M.P. Cabral, N.C. Soares, J. Aranda, J.R. Parreira, C. Rumbo, M. Poza, J. Valle, V. Calamia, I. Lasa, and G. Bou Proteomic and functional analyses reveal a unique lifestyle for Acinetobacter baumannii biofilms and a key role for histidine metabolism J. Proteome Res. 10 2011 3399 3417
    • (2011) J. Proteome Res. , vol.10 , pp. 3399-3417
    • Cabral, M.P.1    Soares, N.C.2    Aranda, J.3    Parreira, J.R.4    Rumbo, C.5    Poza, M.6    Valle, J.7    Calamia, V.8    Lasa, I.9    Bou, G.10
  • 8
    • 0036231824 scopus 로고    scopus 로고
    • The benPK operon, proposed to play a role in transport, is part of a regulon for benzoate catabolism in Acinetobacter sp. strain ADP1
    • T.J. Clark, C. Momany, and E.L. Neidle The benPK operon, proposed to play a role in transport, is part of a regulon for benzoate catabolism in Acinetobacter sp. strain ADP1 Microbiology 148 2002 1213 1223
    • (2002) Microbiology , vol.148 , pp. 1213-1223
    • Clark, T.J.1    Momany, C.2    Neidle, E.L.3
  • 9
    • 0041663886 scopus 로고    scopus 로고
    • Molecular origin of the cation selectivity in OmpF porin: Single channel conductances vs. free energy calculation
    • C. Danelon, A. Suenaga, M. Winterhalter, and I. Yamato Molecular origin of the cation selectivity in OmpF porin: single channel conductances vs. free energy calculation Biophys. Chem. 104 2003 591 603
    • (2003) Biophys. Chem. , vol.104 , pp. 591-603
    • Danelon, C.1    Suenaga, A.2    Winterhalter, M.3    Yamato, I.4
  • 10
  • 15
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • L.M. Guzman, D. Belin, M.J. Carson, and J. Beckwith Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter J. Bacteriol. 177 1995 4121 4130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 16
    • 0031879743 scopus 로고    scopus 로고
    • Resistance mechanisms in Pseudomonas aeruginosa and other nonfermentative gram-negative bacteria
    • R.E. Hancock Resistance mechanisms in Pseudomonas aeruginosa and other nonfermentative gram-negative bacteria Clin. Infect. Dis. 27 Suppl 1 1998 S93 S99
    • (1998) Clin. Infect. Dis. , vol.27 , pp. S93-S99
    • Hancock, R.E.1
  • 17
    • 0019190802 scopus 로고
    • Protein-D1 - A glucose-inducible, pore-forming protein from the outer-membrane of Pseudomonas aeruginosa
    • R.E.W. Hancock, and A.M. Carey Protein-D1 - a glucose-inducible, pore-forming protein from the outer-membrane of Pseudomonas aeruginosa FEMS Microbiol. Lett. 8 1980 105 109
    • (1980) FEMS Microbiol. Lett. , vol.8 , pp. 105-109
    • Hancock, R.E.W.1    Carey, A.M.2
  • 18
    • 0026536545 scopus 로고
    • Overexpression in Escherichia coli and functional analysis of a novel PPi-selective porin, oprO, from Pseudomonas aeruginosa
    • R.E. Hancock, C. Egli, R. Benz, and R.J. Siehnel Overexpression in Escherichia coli and functional analysis of a novel PPi-selective porin, oprO, from Pseudomonas aeruginosa J. Bacteriol. 174 1992 471 476
    • (1992) J. Bacteriol. , vol.174 , pp. 471-476
    • Hancock, R.E.1    Egli, C.2    Benz, R.3    Siehnel, R.J.4
  • 19
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • L. Holm, and P. Rosenström Dali server: conservation mapping in 3D Nucleic Acids Res. 38 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 21
    • 48449099381 scopus 로고    scopus 로고
    • PBEQ-Solver for online visualization of electrostatic potential of biomolecules
    • S. Jo, M. Vargyas, J. Vasko-Szedlar, B. Roux, and W. Im PBEQ-Solver for online visualization of electrostatic potential of biomolecules Nucleic Acids Res. 36 2008 W270 W275
    • (2008) Nucleic Acids Res. , vol.36 , pp. W270-W275
    • Jo, S.1    Vargyas, M.2    Vasko-Szedlar, J.3    Roux, B.4    Im, W.5
  • 23
    • 78149432908 scopus 로고    scopus 로고
    • Structural and dynamical properties of the porins OmpF and OmpC: Insights from molecular simulations
    • A. Kumar, E. Hajjar, P. Ruggerone, and M. Ceccarelli Structural and dynamical properties of the porins OmpF and OmpC: insights from molecular simulations J. Phys. Condens. Matter 22 2010 454125
    • (2010) J. Phys. Condens. Matter , vol.22 , pp. 454125
    • Kumar, A.1    Hajjar, E.2    Ruggerone, P.3    Ceccarelli, M.4
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R. Laskowski, M. MacArthur, D. Moss, and J. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26 1993 283 291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 25
    • 70449124604 scopus 로고    scopus 로고
    • Antibacterial-resistant Pseudomonas aeruginosa: Clinical impact and complex regulation of chromosomally encoded resistance mechanisms
    • P.D. Lister, D.J. Wolter, and N.D. Hanson Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms Clin. Microbiol. Rev. 22 2009 582 610
    • (2009) Clin. Microbiol. Rev. , vol.22 , pp. 582-610
    • Lister, P.D.1    Wolter, D.J.2    Hanson, N.D.3
  • 27
    • 0020636951 scopus 로고
    • Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria
    • B. Lugtenberg, and L. Vanalphen Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria Biochim. Biophys. Acta 737 1983 51 115
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 51-115
    • Lugtenberg, B.1    Vanalphen, L.2
  • 30
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • M. Montal, and P. Mueller Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties Proc. Natl. Acad. Sci. USA 69 1972 3561 3566
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 31
    • 33846113922 scopus 로고    scopus 로고
    • An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane
    • T.F. Moraes, M. Bains, R.E. Hancock, and N.C. Strynadka An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane Nat. Struct. Mol. Biol. 14 2007 85 87
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 85-87
    • Moraes, T.F.1    Bains, M.2    Hancock, R.E.3    Strynadka, N.C.4
  • 32
    • 48449084095 scopus 로고    scopus 로고
    • RAPIDO: A web server for the alignment of protein structures in the presence of conformational changes
    • R. Mosca, and T.R. Schneider RAPIDO: a web server for the alignment of protein structures in the presence of conformational changes Nucleic Acids Res. 36 2008 W42 W46
    • (2008) Nucleic Acids Res. , vol.36 , pp. W42-W46
    • Mosca, R.1    Schneider, T.R.2
  • 34
    • 16244406203 scopus 로고    scopus 로고
    • Acquisition of resistance to carbapenems in multidrug-resistant clinical strains of Acinetobacter baumannii: Natural insertional inactivation of a gene encoding a member of a novel family of beta-barrel outer membrane proteins
    • M.A. Mussi, A.S. Limansky, and A.M. Viale Acquisition of resistance to carbapenems in multidrug-resistant clinical strains of Acinetobacter baumannii: natural insertional inactivation of a gene encoding a member of a novel family of beta-barrel outer membrane proteins Antimicrob. Agents Chemother. 49 2005 1432 1440
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 1432-1440
    • Mussi, M.A.1    Limansky, A.S.2    Viale, A.M.3
  • 35
    • 0037162486 scopus 로고    scopus 로고
    • Designed to penetrate: Time-resolved interaction of single antibiotic molecules with bacterial pores
    • E.M. Nestorovich, C. Danelon, M. Winterhalter, and S.M. Bezrukov Designed to penetrate: time-resolved interaction of single antibiotic molecules with bacterial pores Proc. Natl. Acad. Sci. USA 99 2002 9789 9794
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9789-9794
    • Nestorovich, E.M.1    Danelon, C.2    Winterhalter, M.3    Bezrukov, S.M.4
  • 36
    • 0020597554 scopus 로고
    • Porin channels in Escherichia coli: Studies with liposomes reconstituted from purified proteins
    • H. Nikaido, and E.Y. Rosenberg Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins J. Bacteriol. 153 1983 241 252
    • (1983) J. Bacteriol. , vol.153 , pp. 241-252
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 37
    • 56349139534 scopus 로고    scopus 로고
    • The porin and the permeating antibiotic: A selective diffusion barrier in Gram-negative bacteria
    • J.M. Pages, C.E. James, and M. Winterhalter The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria Nat. Rev. Microbiol. 6 2008 893 903
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 893-903
    • Pages, J.M.1    James, C.E.2    Winterhalter, M.3
  • 38
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • X. Robert, and P. Gouet Deciphering key features in protein structures with the new ENDscript server Nucleic Acids Res. 42 2014 W320 W324
    • (2014) Nucleic Acids Res. , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2
  • 39
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • G.E. Schulz The structure of bacterial outer membrane proteins Biochim. Biophys. Acta 1565 2002 308 317
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 40
    • 0345346392 scopus 로고    scopus 로고
    • Genetic analysis of a chromosomal region containing vanA and vanB, genes required for conversion of either ferulate or vanillate to protocatechuate in Acinetobacter
    • A. Segura, P.V. Bunz, D.A. D'Argenio, and L.N. Ornston Genetic analysis of a chromosomal region containing vanA and vanB, genes required for conversion of either ferulate or vanillate to protocatechuate in Acinetobacter J. Bacteriol. 181 1999 3494 3504
    • (1999) J. Bacteriol. , vol.181 , pp. 3494-3504
    • Segura, A.1    Bunz, P.V.2    D'Argenio, D.A.3    Ornston, L.N.4
  • 41
    • 84872043562 scopus 로고    scopus 로고
    • Loss of the OprD homologue protein in Acinetobacter baumannii: Impact on carbapenem susceptibility
    • Y. Smani, and J. Pachon Loss of the OprD homologue protein in Acinetobacter baumannii: impact on carbapenem susceptibility Antimicrob. Agents Chemother. 57 2013 677
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 677
    • Smani, Y.1    Pachon, J.2
  • 42
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • 376
    • O.S. Smart, J.G. Neduvelil, X. Wang, B.A. Wallace, and M.S. Sansom HOLE: a program for the analysis of the pore dimensions of ion channel structural models J. Mol. Graph. 14 1996 354 360 376
    • (1996) J. Mol. Graph. , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5
  • 43
    • 0037229359 scopus 로고    scopus 로고
    • Genes for chlorogenate and hydroxycinnamate catabolism (hca) are linked to functionally related genes in the dca-pca-qui-pob-hca chromosomal cluster of Acinetobacter sp. strain ADP1
    • M.A. Smith, V.B. Weaver, D.M. Young, and L.N. Ornston Genes for chlorogenate and hydroxycinnamate catabolism (hca) are linked to functionally related genes in the dca-pca-qui-pob-hca chromosomal cluster of Acinetobacter sp. strain ADP1 Appl. Environ. Microbiol. 69 2003 524 532
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 524-532
    • Smith, M.A.1    Weaver, V.B.2    Young, D.M.3    Ornston, L.N.4
  • 44
    • 84866342585 scopus 로고    scopus 로고
    • OmpA is the principal nonspecific slow porin of Acinetobacter baumannii
    • E. Sugawara, and H. Nikaido OmpA is the principal nonspecific slow porin of Acinetobacter baumannii J. Bacteriol. 194 2012 4089 4096
    • (2012) J. Bacteriol. , vol.194 , pp. 4089-4096
    • Sugawara, E.1    Nikaido, H.2
  • 45
    • 33644903806 scopus 로고    scopus 로고
    • Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa
    • S. Tamber, M.M. Ochs, and R.E. Hancock Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa J. Bacteriol. 188 2006 45 54
    • (2006) J. Bacteriol. , vol.188 , pp. 45-54
    • Tamber, S.1    Ochs, M.M.2    Hancock, R.E.3
  • 48
    • 34447556772 scopus 로고    scopus 로고
    • Porins, efflux pumps and multidrug resistance in Acinetobacter baumannii
    • J. Vila, S. Marti, and J. Sanchez-Cespedes Porins, efflux pumps and multidrug resistance in Acinetobacter baumannii J. Antimicrob. Chemother. 59 2007 1210 1215
    • (2007) J. Antimicrob. Chemother. , vol.59 , pp. 1210-1215
    • Vila, J.1    Marti, S.2    Sanchez-Cespedes, J.3
  • 49
    • 84934892567 scopus 로고    scopus 로고
    • Small-molecule transport by CarO, an abundant eight-stranded beta-barrel outer membrane protein from Acinetobacter baumannii
    • M. Zahn, T. D'Agostino, E. Eren, A. Basle, M. Ceccarelli, and B. van den Berg Small-molecule transport by CarO, an abundant eight-stranded beta-barrel outer membrane protein from Acinetobacter baumannii J. Mol. Biol. 427 2015 2329 2339
    • (2015) J. Mol. Biol. , vol.427 , pp. 2329-2339
    • Zahn, M.1    D'Agostino, T.2    Eren, E.3    Basle, A.4    Ceccarelli, M.5    Van Den Berg, B.6


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