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Volumn 195, Issue 8, 2013, Pages 1680-1688

Ultrastructural analysis of the rugose cell envelope of a member of the pasteurellaceae family

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATIBACTER ACTINOMYCETEMCOMITANS; ANTIBIOTIC RESISTANCE; ARTICLE; ATOMIC FORCE MICROSCOPY; BACTERIAL MEMBRANE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BACTERIUM MUTANT; CELL STRUCTURE; CELL ULTRASTRUCTURE; CONTROLLED STUDY; ELECTRON MICROSCOPY; FREEZE DRYING; FROZEN SECTION; MORAXELLACEAE; NONHUMAN; PASTEURELLACEAE; PRIORITY JOURNAL; RUGOSE CELL ENVELOPE; TISSUE SECTION; TRANSGENIC ORGANISM; ULTRASTRUCTURE ANALYSIS AND ELECTRON MICROSCOPY;

EID: 84876078027     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02149-12     Document Type: Article
Times cited : (17)

References (54)
  • 2
    • 0026071729 scopus 로고
    • Freezesubstitution of gram-negative eubacteria: general cell morphology and envelope profiles
    • Graham LL, Harris R, Villiger W, Beveridge TJ. 1991. Freezesubstitution of gram-negative eubacteria: general cell morphology and envelope profiles. J. Bacteriol. 173:1623-1633.
    • (1991) J. Bacteriol. , vol.173 , pp. 1623-1633
    • Graham, L.L.1    Harris, R.2    Villiger, W.3    Beveridge, T.J.4
  • 4
    • 0014401447 scopus 로고
    • Separation by density gradient centrifugation of two types of membranes from spheroplast membrane of Escherichia coli K-12
    • Miura T, Mizushima S. 1968. Separation by density gradient centrifugation of two types of membranes from spheroplast membrane of Escherichia coli K-12. Biochim. Biophys. Acta 150:159-161.
    • (1968) Biochim. Biophys. Acta , vol.150 , pp. 159-161
    • Miura, T.1    Mizushima, S.2
  • 5
    • 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
  • 6
    • 79959435716 scopus 로고    scopus 로고
    • Assembly of bacterial inner membrane proteins
    • Dalbey RE, Wang P, Kuhn A. 2011. Assembly of bacterial inner membrane proteins. Annu. Rev. Biochem. 80:161-187.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 161-187
    • Dalbey, R.E.1    Wang, P.2    Kuhn, A.3
  • 7
    • 0018587209 scopus 로고
    • The outer membrane of Gram-negative bacteria
    • Nikaido H, Nakae T. 1979. The outer membrane of Gram-negative bacteria. Adv. Microb. Physiol. 20:163-250.
    • (1979) Adv. Microb. Physiol. , vol.20 , pp. 163-250
    • Nikaido, H.1    Nakae, T.2
  • 8
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial outer membrane
    • Bos MP, Robert V, Tommassen J. 2007. Biogenesis of the gram-negative bacterial outer membrane. Annu. Rev. Microbiol. 61:191-214.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 10
    • 66649113467 scopus 로고    scopus 로고
    • Membrane-protein structure: piercing insights
    • Bayley H. 2009. Membrane-protein structure: piercing insights. Nature 459:651-652.
    • (2009) Nature , vol.459 , pp. 651-652
    • Bayley, H.1
  • 11
    • 4444246066 scopus 로고    scopus 로고
    • Identification of an extracellular matrix protein adhesin, EmaA, which mediates the adhesion of Actinobacillus actinomycetemcomitans to collagen
    • Mintz KP. 2004. Identification of an extracellular matrix protein adhesin, EmaA, which mediates the adhesion of Actinobacillus actinomycetemcomitans to collagen. Microbiology 150(Pt 8):2677-2688.
    • (2004) Microbiology , vol.150 , Issue.PT 8 , pp. 2677-2688
    • Mintz, K.P.1
  • 12
    • 0032989015 scopus 로고    scopus 로고
    • Bacterial adhesins: common themes and variations in architecture and assembly
    • Soto GE, Hultgren SJ. 1999. Bacterial adhesins: common themes and variations in architecture and assembly. J. Bacteriol. 181:1059-1071.
    • (1999) J. Bacteriol. , vol.181 , pp. 1059-1071
    • Soto, G.E.1    Hultgren, S.J.2
  • 13
    • 70350449410 scopus 로고    scopus 로고
    • Investigation of the three-dimensional architecture of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans by electron tomography
    • Yu C, Mintz KP, Ruiz T. 2009. Investigation of the three-dimensional architecture of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans by electron tomography. J. Bacteriol. 191:6253-6261.
    • (2009) J. Bacteriol. , vol.191 , pp. 6253-6261
    • Yu, C.1    Mintz, K.P.2    Ruiz, T.3
  • 14
    • 0030925485 scopus 로고    scopus 로고
    • Surface signaling: novel transcription initiation mechanism starting from the cell surface
    • Braun V. 1997. Surface signaling: novel transcription initiation mechanism starting from the cell surface. Arch. Microbiol. 167:325-331.
    • (1997) Arch. Microbiol. , vol.167 , pp. 325-331
    • Braun, V.1
  • 15
    • 38349127277 scopus 로고    scopus 로고
    • Inter-kingdom signaling: communication between bacteria and their hosts
    • Hughes DT, Sperandio V. 2008. Inter-kingdom signaling: communication between bacteria and their hosts. Nat. Rev. Microbiol. 6:111-120.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 111-120
    • Hughes, D.T.1    Sperandio, V.2
  • 16
    • 33750684655 scopus 로고    scopus 로고
    • Bacterial protein toxins and lipids: pore formation or toxin entry into cells
    • Geny B, Popoff MR. 2006. Bacterial protein toxins and lipids: pore formation or toxin entry into cells. Biol. Cell 98:667-678.
    • (2006) Biol. Cell , vol.98 , pp. 667-678
    • Geny, B.1    Popoff, M.R.2
  • 17
    • 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
  • 18
    • 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
  • 21
    • 18144381988 scopus 로고    scopus 로고
    • Antimicrobial actions of the human epididymis 2 (HE2) protein isoforms, HE2α, HE2β1, and HE2β2
    • Yenugu S, Hamil KG, French FS, Hall SH. 2004. Antimicrobial actions of the human epididymis 2 ((HE2) protein isoforms, HE2α, HE2β1, and HE2β2 Biol. Endocrinol. 2:61.
    • (2004) Reprod. Biol. Endocrinol. , vol.2 , pp. 61
    • Yenugu, S.1    Hamil, K.G.2    French, F.S.3    Hall, S.H.4
  • 22
    • 33750465551 scopus 로고    scopus 로고
    • Novel surface structures are associated with the adhesion of Actinobacillus actinomycetemcomitans to collagen
    • Ruiz T, Lenox C, Radermacher M, Mintz KP. 2006. Novel surface structures are associated with the adhesion of Actinobacillus actinomycetemcomitans to collagen. Infect. Immun. 74:6163-6170.
    • (2006) Infect. Immun. , vol.74 , pp. 6163-6170
    • Ruiz, T.1    Lenox, C.2    Radermacher, M.3    Mintz, K.P.4
  • 23
    • 0034669051 scopus 로고    scopus 로고
    • Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins
    • Hoiczyk E, Roggenkamp A, Reichenbecher M, Lupas A, Heesemann J. 2000. Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. EMBO J. 19:5989-5999.
    • (2000) EMBO J. , vol.19 , pp. 5989-5999
    • Hoiczyk, E.1    Roggenkamp, A.2    Reichenbecher, M.3    Lupas, A.4    Heesemann, J.5
  • 25
    • 0027514792 scopus 로고
    • Actinobacillus actinomycetemcomitans and localized juvenile periodontitis. Clinical, microbiologic and histologic studies
    • Christersson LA. 1993. Actinobacillus actinomycetemcomitans and localized juvenile periodontitis. Clinical, microbiologic and histologic studies. Swed. Dent. J. Suppl. 90:1-46.
    • (1993) Swed. Dent. J. Suppl. , vol.90 , pp. 1-46
    • Christersson, L.A.1
  • 27
    • 0020526731 scopus 로고
    • Infections due to Actinobacillus actinomycetemcomitans: a report of 3 cases
    • Mauff AC, Miller S, Kuhnle V, Carmichael M. 1983. Infections due to Actinobacillus actinomycetemcomitans: a report of 3 cases. S. Afr. Med. J. 63:580-581.
    • (1983) S. Afr. Med. J. , vol.63 , pp. 580-581
    • Mauff, A.C.1    Miller, S.2    Kuhnle, V.3    Carmichael, M.4
  • 28
    • 0018356427 scopus 로고
    • Vertebral osteomyelitis due to Actinobacillus actinomycetemcomitans
    • Muhle I, Rau J, Ruskin J. 1979. Vertebral osteomyelitis due to Actinobacillus actinomycetemcomitans. JAMA 241:1824-1825.
    • (1979) JAMA , vol.241 , pp. 1824-1825
    • Muhle, I.1    Rau, J.2    Ruskin, J.3
  • 29
    • 50249144596 scopus 로고    scopus 로고
    • Membrane morphology and leukotoxin secretion are associated with a novel membrane protein of Aggregatibacter actinomycetemcomitans
    • Gallant CV, Sedic M, Chicoine EA, Ruiz T, Mintz KP. 2008. Membrane morphology and leukotoxin secretion are associated with a novel membrane protein of Aggregatibacter actinomycetemcomitans. J. Bacteriol. 190: 5972-5980.
    • (2008) J. Bacteriol. , vol.190 , pp. 5972-5980
    • Gallant, C.V.1    Sedic, M.2    Chicoine, E.A.3    Ruiz, T.4    Mintz, K.P.5
  • 30
    • 84857030774 scopus 로고    scopus 로고
    • Correlation of the amino-acid sequence and the 3D structure of the functional domain of EmaA from Aggregatibacter actinomycetemcomitans
    • Azari F, Radermacher M, Mintz KP, Ruiz T. 2012. Correlation of the amino-acid sequence and the 3D structure of the functional domain of EmaA from Aggregatibacter actinomycetemcomitans. J. Struct. Biol. 177: 439-446.
    • (2012) J. Struct. Biol. , vol.177 , pp. 439-446
    • Azari, F.1    Radermacher, M.2    Mintz, K.P.3    Ruiz, T.4
  • 31
    • 42549117252 scopus 로고    scopus 로고
    • Functional mapping of an oligomeric autotransporter adhesin of Aggregatibacter actinomycetemcomitans
    • Yu C, Ruiz T, Lenox C, Mintz KP. 2008. Functional mapping of an oligomeric autotransporter adhesin of Aggregatibacter actinomycetemcomitans. J. Bacteriol. 190:3098-3109.
    • (2008) J. Bacteriol. , vol.190 , pp. 3098-3109
    • Yu, C.1    Ruiz, T.2    Lenox, C.3    Mintz, K.P.4
  • 32
    • 0028101001 scopus 로고
    • Adhesion of Actinobacillus actinomycetemcomitans to a human oral cell line
    • Mintz KP, Fives-Taylor PM. 1994. Adhesion of Actinobacillus actinomycetemcomitans to a human oral cell line. Infect. Immun. 62:3672-3678.
    • (1994) Infect. Immun. , vol.62 , pp. 3672-3678
    • Mintz, K.P.1    Fives-Taylor, P.M.2
  • 33
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer JR, Mastronarde DN, McIntosh JR. 1996. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116:71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 34
    • 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, Ladjadj M, Leith A. 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    Ladjadj, M.6    Leith, A.7
  • 35
    • 84985231782 scopus 로고
    • Threedimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M, Wagenknecht T, Verschoor A, Frank J. 1987. Threedimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 146(Pt 2):113-136.
    • (1987) J. Microsc. , vol.146 , Issue.PT 2 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 37
    • 77952581453 scopus 로고    scopus 로고
    • Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions
    • Pintilie GD, Zhang J, Goddard TD, Chiu W, Gossard DC. 2010. Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions. J. Struct. Biol. 170:427-438.
    • (2010) J. Struct. Biol. , vol.170 , pp. 427-438
    • Pintilie, G.D.1    Zhang, J.2    Goddard, T.D.3    Chiu, W.4    Gossard, D.C.5
  • 39
    • 0036157198 scopus 로고    scopus 로고
    • Outer membrane-like vesicles secreted by Actinobacillus actinomycetemcomitans are enriched in leukotoxin
    • Kato S, Kowashi Y, Demuth DR. 2002. Outer membrane-like vesicles secreted by Actinobacillus actinomycetemcomitans are enriched in leukotoxin. Microb. Pathog. 32:1-13.
    • (2002) Microb. Pathog. , vol.32 , pp. 1-13
    • Kato, S.1    Kowashi, Y.2    Demuth, D.R.3
  • 40
    • 0030016553 scopus 로고    scopus 로고
    • Influence of pili, fibrils, and capsule on in vitro adherence by Haemophilus influenzae type b
    • St Geme JW, III, Cutter D. 1996. Influence of pili, fibrils, and capsule on in vitro adherence by Haemophilus influenzae type b. Mol. Microbiol. 21:21-31.
    • (1996) Mol. Microbiol. , vol.21 , pp. 21-31
    • St Geme, J.W.1    Cutter, D.2
  • 41
    • 0026318173 scopus 로고
    • Zones of membrane adhesion in the cryofixed envelope of Escherichia coli
    • Bayer ME. 1991. Zones of membrane adhesion in the cryofixed envelope of Escherichia coli. J. Struct. Biol. 107:268-280.
    • (1991) J. Struct. Biol. , vol.107 , pp. 268-280
    • Bayer, M.E.1
  • 42
    • 0029781799 scopus 로고    scopus 로고
    • Periplasm, periplasmic spaces, and their relation to bacterial wall structure: novel secretion of selected periplasmic proteins from Pseudomonas aeruginosa
    • Beveridge TJ, Kadurugamuwa JL. 1996. Periplasm, periplasmic spaces, and their relation to bacterial wall structure: novel secretion of selected periplasmic proteins from Pseudomonas aeruginosa. Microb. Drug Resist. 2:1-8.
    • (1996) Microb. Drug Resist. , vol.2 , pp. 1-8
    • Beveridge, T.J.1    Kadurugamuwa, J.L.2
  • 43
    • 0026479698 scopus 로고
    • Freeze-substitution studies of bacteria
    • Graham LL. 1992. Freeze-substitution studies of bacteria. Electron. Microsc. Rev. 5:77-103.
    • (1992) Electron. Microsc. Rev. , vol.5 , pp. 77-103
    • Graham, L.L.1
  • 44
    • 0025314999 scopus 로고
    • The 'Bayer bridges' confronted with results from improved electron microscopy methods
    • Kellenberger E. 1990. The 'Bayer bridge's confronted with results from improved electron microscopy methods. Mol. Microbiol. 4:697-705.
    • (1990) Mol. Microbiol. , vol.4 , pp. 697-705
    • Kellenberger, E.1
  • 45
    • 0032839616 scopus 로고    scopus 로고
    • Structures of gram-negative cell walls and their derived membrane vesicles
    • Beveridge TJ. 1999. Structures of gram-negative cell walls and their derived membrane vesicles. J. Bacteriol. 181:4725-4733.
    • (1999) J. Bacteriol. , vol.181 , pp. 4725-4733
    • Beveridge, T.J.1
  • 46
    • 0141994975 scopus 로고    scopus 로고
    • Cryotransmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa
    • Matias VR, Al-Amoudi A, Dubochet J, Beveridge TJ. 2003. Cryotransmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa. J. Bacteriol. 185:6112-6118.
    • (2003) J. Bacteriol. , vol.185 , pp. 6112-6118
    • Matias, V.R.1    Al-Amoudi, A.2    Dubochet, J.3    Beveridge, T.J.4
  • 47
    • 84855294892 scopus 로고    scopus 로고
    • Outer membrane lipoprotein Lpp is Gram-negative bacterial cell surface receptor for cationic antimicrobial peptides
    • Chang TW, Lin YM, Wang CF, Liao YD. 2012. Outer membrane lipoprotein Lpp is Gram-negative bacterial cell surface receptor for cationic antimicrobial peptides. J. Biol. Chem. 287:418-428.
    • (2012) J. Biol. Chem. , vol.287 , pp. 418-428
    • Chang, T.W.1    Lin, Y.M.2    Wang, C.F.3    Liao, Y.D.4
  • 48
    • 67449108344 scopus 로고    scopus 로고
    • Aggregatibacter actinomycetemcomitans LtxC is required for leukotoxin activity and initial interaction between toxin and host cells
    • Balashova NV, Shah C, Patel JK, Megalla S, Kachlany SC. 2009. Aggregatibacter actinomycetemcomitans LtxC is required for leukotoxin activity and initial interaction between toxin and host cells. Gene 443:42-47.
    • (2009) Gene , vol.443 , pp. 42-47
    • Balashova, N.V.1    Shah, C.2    Patel, J.K.3    Megalla, S.4    Kachlany, S.C.5
  • 49
    • 0024423256 scopus 로고
    • Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene, Delineation of unique features and comparison to homologous toxins
    • Lally ET, Golub EE, Kieba IR, Taichman NS, Rosenbloom J, Rosenbloom JC, Gibson CW, Demuth DR. 1989. Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene. Delineation of unique features and comparison to homologous toxins. J. Biol. Chem. 264:15451-15456.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15451-15456
    • Lally, E.T.1    Golub, E.E.2    Kieba, I.R.3    Taichman, N.S.4    Rosenbloom, J.5    Rosenbloom, J.C.6    Gibson, C.W.7    Demuth, D.R.8
  • 50
    • 33746561249 scopus 로고    scopus 로고
    • Special delivery: vesicle trafficking in prokaryotes
    • Mashburn-Warren LM, Whiteley M. 2006. Special delivery: vesicle trafficking in prokaryotes. Mol. Microbiol. 61:839-846.
    • (2006) Mol. Microbiol. , vol.61 , pp. 839-846
    • Mashburn-Warren, L.M.1    Whiteley, M.2
  • 51
    • 0019795018 scopus 로고
    • Outer-membrane vesicles released by normally growing Escherichia coli contain very little lipoprotein
    • Wensink J, Witholt B. 1981. Outer-membrane vesicles released by normally growing Escherichia coli contain very little lipoprotein. Eur. J. Biochem. 116:331-335.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 331-335
    • Wensink, J.1    Witholt, B.2
  • 53
    • 84863838790 scopus 로고    scopus 로고
    • Membrane vesicle release in bacteria, eukaryotes, and archaea: a conserved yet underappreciated aspect of microbial life
    • Deatherage BL, Cookson BT. 2012. Membrane vesicle release in bacteria, eukaryotes, and archaea: a conserved yet underappreciated aspect of microbial life. Infect. Immun. 80:1948-1957.
    • (2012) Infect. Immun. , vol.80 , pp. 1948-1957
    • Deatherage, B.L.1    Cookson, B.T.2
  • 54
    • 0023219963 scopus 로고
    • Association of thioredoxin with the inner membrane and adhesion sites in Escherichia coli
    • Bayer ME, Bayer MH, Lunn CA, Pigiet V. 1987. Association of thioredoxin with the inner membrane and adhesion sites in Escherichia coli. J. Bacteriol. 169:2659-2666.
    • (1987) J. Bacteriol. , vol.169 , pp. 2659-2666
    • Bayer, M.E.1    Bayer, M.H.2    Lunn, C.A.3    Pigiet, V.4


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