메뉴 건너뛰기




Volumn 2, Issue 5, 1996, Pages 305-312

The isolation and characterization of a porin protein from Bacteroides fragilis

Author keywords

Bacteroides fragilis; Outer membrane; Porin

Indexed keywords

BACTERIAL PROTEIN; COPPER; LIPOSOME; OUTER MEMBRANE PROTEIN; PORIN;

EID: 0030271094     PISSN: 10759964     EISSN: None     Source Type: Journal    
DOI: 10.1006/anae.1996.0039     Document Type: Article
Times cited : (13)

References (53)
  • 1
    • 0002906968 scopus 로고
    • General aspects of anaerobic infections
    • Fingeold S.M. and George W.L. (eds), Academic Press, Inc., San Diego
    • 1. Finegold S.M. (1989) General aspects of anaerobic infections. In Fingeold S.M. and George W.L. (eds), Anaerobic Infections in Humans, pp. 137-153. Academic Press, Inc., San Diego
    • (1989) Anaerobic Infections in Humans , pp. 137-153
    • Finegold, S.M.1
  • 2
    • 0018074492 scopus 로고
    • Outer membranes of gram negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PA01 and use in reconstitution and definition of the permeability barrier
    • 2. Hancock R.E.W. and Nikaido H. (1978) Outer membranes of gram negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PA01 and use in reconstitution and definition of the permeability barrier. J. Bacteriol. 136: 381-390
    • (1978) J. Bacteriol. , vol.136 , pp. 381-390
    • Hancock, R.E.W.1    Nikaido, H.2
  • 3
    • 0019814049 scopus 로고
    • Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the ompF porin
    • 3. Harder K.J., Nikaido H. and Matsuhashi M. (1981) Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the ompF porin. Antimicrob. Agents Chemother. 20: 549-552
    • (1981) Antimicrob. Agents Chemother. , vol.20 , pp. 549-552
    • Harder, K.J.1    Nikaido, H.2    Matsuhashi, M.3
  • 4
    • 0023619948 scopus 로고
    • Loss of OmpC porin in a strain of Salmonella typhimurium causes increased resistance to cephalosporins during therapy
    • 4. Medeiros A.A., O'Brien T.F., Rosenberg E.Y. and Nikaido H. (1987) Loss of OmpC porin in a strain of Salmonella typhimurium causes increased resistance to cephalosporins during therapy. J. Infect. Dis. 156: 751-757
    • (1987) J. Infect. Dis. , vol.156 , pp. 751-757
    • Medeiros, A.A.1    O'Brien, T.F.2    Rosenberg, E.Y.3    Nikaido, H.4
  • 5
    • 0022263488 scopus 로고
    • Role of permeability barriers in resistance to beta-lactam antibiotics
    • 5. Nikaido H. (1985) Role of permeability barriers in resistance to beta-lactam antibiotics. [Review]. Pharmacology & Therapeutics 27: 197-231
    • (1985) Pharmacology & Therapeutics , vol.27 , pp. 197-231
    • Nikaido, H.1
  • 6
    • 0023748575 scopus 로고
    • Bacterial resistance to antibiotics as a function of outer membrane permeability
    • 6. Nikaido H. (1988) Bacterial resistance to antibiotics as a function of outer membrane permeability. [Review]. J. Antimicrob. Chemother. 22 Suppl A: 17-22
    • (1988) J. Antimicrob. Chemother. , vol.22 , Issue.SUPPL. A , pp. 17-22
    • Nikaido, H.1
  • 7
    • 0024467106 scopus 로고
    • Outer membrane barrier as a mechanism of antimicrobial resistance
    • 7. Nikaido H. (1989) Outer membrane barrier as a mechanism of antimicrobial resistance. [Review]. Antimicrob. Agents Chemother. 33: 1831-1836
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1831-1836
    • Nikaido, H.1
  • 8
    • 0020522392 scopus 로고
    • Porin channels in Escherichia coli: Studies with beta-lactams in intact cells
    • 8. Nikaido H., Rosenberg E.Y. and Foulds J. (1983) Porin channels in Escherichia coli: studies with beta-lactams in intact cells. J. Bacteriol. 153: 232-240
    • (1983) J. Bacteriol. , vol.153 , pp. 232-240
    • Nikaido, H.1    Rosenberg, E.Y.2    Foulds, J.3
  • 9
    • 0022263277 scopus 로고
    • Newer mechanisms of resistance to beta-lactam antibiotics in gram negative bacteria
    • 9. Piddock L.J. and Wise R. (1985) Newer mechanisms of resistance to beta-lactam antibiotics in gram negative bacteria. Antimicrob. Agents Chemother. 16: 279-284
    • (1985) Antimicrob. Agents Chemother. , vol.16 , pp. 279-284
    • Piddock, L.J.1    Wise, R.2
  • 10
    • 0021968133 scopus 로고
    • Diffusion of beta-lactam antibiotics through the porin channels of Escherichia coli K-12
    • 10. Yoshimura F. and Nikaido H. (1985) Diffusion of beta-lactam antibiotics through the porin channels of Escherichia coli K-12. Antimicrob. Agents Chemother. 27: 84-92
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 84-92
    • Yoshimura, F.1    Nikaido, H.2
  • 13
    • 0022570517 scopus 로고
    • Beta-lactamases of type culture strains of the Bacteroides fragilis group and of strains that hydrolyse cefoxitin, latamoxef and imipenem
    • 13. Eley A. and Greenwood D. (1986) Beta-lactamases of type culture strains of the Bacteroides fragilis group and of strains that hydrolyse cefoxitin, latamoxef and imipenem. J. Med. Microbiol. 21: 49-57
    • (1986) J. Med. Microbiol. , vol.21 , pp. 49-57
    • Eley, A.1    Greenwood, D.2
  • 15
    • 0019855250 scopus 로고
    • Outer membrane proteins of the Bacteroides fragilis group
    • 15. Diedrich D.L. and Martin A.R. (1981) Outer membrane proteins of the Bacteroides fragilis group. Curr Microbiol. 6: 85-88
    • (1981) Curr Microbiol. , vol.6 , pp. 85-88
    • Diedrich, D.L.1    Martin, A.R.2
  • 17
    • 0021264085 scopus 로고
    • Isolation and characterization of outer membranes of Bacteroides thetaiotaomicron grown on different carbohydrates
    • 17. Kotarski S.F. and Salyers A.A. (1984) Isolation and characterization of outer membranes of Bacteroides thetaiotaomicron grown on different carbohydrates. J. Bacteriol. 158: 102-109
    • (1984) J. Bacteriol. , vol.158 , pp. 102-109
    • Kotarski, S.F.1    Salyers, A.A.2
  • 18
    • 0002431489 scopus 로고
    • Outer membrane
    • Neidhart F.C., Ingraham J.L., Low K.B., Magasanik B., Schaechter M. and Umbarger H.R. (eds), American Society for Microbiology, Washington, DC
    • 18. Nikaido H. and Vaara M. (1987) Outer membrane. In Neidhart F.C., Ingraham J.L., Low K.B., Magasanik B., Schaechter M. and Umbarger H.R. (eds), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. Vol. 1. pp. 7-22. American Society for Microbiology, Washington, DC
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , vol.1 , pp. 7-22
    • Nikaido, H.1    Vaara, M.2
  • 19
    • 0025091804 scopus 로고
    • Structural and functional properties of porin channels in E. Coli outer membranes
    • 19. Rosenbusch J.P. (1990) Structural and functional properties of porin channels in E. coli outer membranes. Experientia 46: 167-173
    • (1990) Experientia , vol.46 , pp. 167-173
    • Rosenbusch, J.P.1
  • 20
    • 0023222342 scopus 로고
    • The role of beta-lactamase and the permeability barrier on the activity of cephalosporins against members of the Bacteroides fragilis group
    • 20. Malouin F. and Lamothe F. (1987) The role of beta-lactamase and the permeability barrier on the activity of cephalosporins against members of the Bacteroides fragilis group. Can. J. Microbiol. 33: 262-266
    • (1987) Can. J. Microbiol. , vol.33 , pp. 262-266
    • Malouin, F.1    Lamothe, F.2
  • 21
    • 0016216108 scopus 로고
    • Nutritional features of Bacteroides fragilis subsp. Fragilis
    • 21. Varel V.H. and Bryant M.P. (1974) Nutritional features of Bacteroides fragilis subsp. fragilis. Appl. Microbiol. 28: 251-257
    • (1974) Appl. Microbiol. , vol.28 , pp. 251-257
    • Varel, V.H.1    Bryant, M.P.2
  • 22
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4. DNA packaging events
    • 22. Laemmli U.K. and Favre M. (1973) Maturation of the head of bacteriophage T4. DNA packaging events. J. Mol. Biol. 80: 575-599
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 23
    • 0026713164 scopus 로고
    • The isolation and characterisation of a major outer-membrane protein from Bacteroides distasonis
    • 23. Wexler H.M., Getty C. and Fisher G. (1992) The isolation and characterisation of a major outer-membrane protein from Bacteroides distasonis. J. Med. Microbiol. 37: 165-175
    • (1992) J. Med. Microbiol. , vol.37 , pp. 165-175
    • Wexler, H.M.1    Getty, C.2    Fisher, G.3
  • 24
    • 0013852467 scopus 로고
    • Correlation of amino-acid composition with certain characteristics of proteins
    • 24. Hatch F.T. (1965) Correlation of amino-acid composition with certain characteristics of proteins. Nature 206: 777-779
    • (1965) Nature , vol.206 , pp. 777-779
    • Hatch, F.T.1
  • 26
    • 0020597554 scopus 로고
    • Porin channels in Escherichia coli: Studies with liposomes reconstituted from purified proteins
    • 26. Nikaido H., and Rosenberg E.Y. (1983) Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins. J. Bacteriol. 153: 241-252
    • (1983) J. Bacteriol. , vol.153 , pp. 241-252
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 27
    • 0019824138 scopus 로고
    • Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli
    • 27. Nikaido H. and Rosenberg E.Y. (1981) Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli. J. Gen. Physiol. 77: 121-135
    • (1981) J. Gen. Physiol. , vol.77 , pp. 121-135
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 28
    • 0020983948 scopus 로고
    • Proteins forming large channels from bacterial and mitochondrial outer membranes: Porins and phage lambda receptor proteins
    • Fleischer S. and Fleischer B. (eds) Biomembranes, Academic Press, New York
    • 28. Nikaido H. (1983) Proteins forming large channels from bacterial and mitochondrial outer membranes: Porins and phage lambda receptor proteins. In Fleischer S. and Fleischer B. (eds) Methods in Enzymology, Vol 97: Biomembranes, pp 85-100 Academic Press, New York
    • (1983) Methods in Enzymology , vol.97 , pp. 85-100
    • Nikaido, H.1
  • 29
    • 0022447230 scopus 로고
    • Bordetella pertussis major outer membrane porin protein forms small, anion-selective channels in lipid bilayer membranes
    • 29. Armstrong S.K., Parr T.R. Jr., Parker C.D., and Hancock R.E. (1986) Bordetella pertussis major outer membrane porin protein forms small, anion-selective channels in lipid bilayer membranes. J. Bacteriol. 166: 212-216
    • (1986) J. Bacteriol. , vol.166 , pp. 212-216
    • Armstrong, S.K.1    Parr T.R., Jr.2    Parker, C.D.3    Hancock, R.E.4
  • 30
    • 0026331087 scopus 로고
    • Pore-forming ability of major outer membrane proteins from Wolinella recta ATCC 33238
    • 30. Kennell W.L., Egli C., Hancock R.E.W. and Holt S.C. (1992) Pore-forming ability of major outer membrane proteins from Wolinella recta ATCC 33238. Infect. Immun. 60: 380-384
    • (1992) Infect. Immun. , vol.60 , pp. 380-384
    • Kennell, W.L.1    Egli, C.2    Hancock, R.E.W.3    Holt, S.C.4
  • 31
    • 0022466549 scopus 로고
    • Lipopolysaccharide-free Escherichia coli OmpF and Pseudomonas aeruginosa protein P porins are functionally active in lipid bilayer membranes
    • 31. Parr T.R., Jr., Poole K., Crockford G.W. and Hancock R.E. (1986) Lipopolysaccharide-free Escherichia coli OmpF and Pseudomonas aeruginosa protein P porins are functionally active in lipid bilayer membranes. J. Bacteriol. 165: 523-526
    • (1986) J. Bacteriol. , vol.165 , pp. 523-526
    • Parr T.R., Jr.1    Poole, K.2    Crockford, G.W.3    Hancock, R.E.4
  • 32
    • 0019214630 scopus 로고
    • Determination of ion permeability through the channels made of porins from the outer membrane of Salmonella typhimurium in lipid bilayer membranes
    • 32. Jenz R., Ishu J. and Nakae T. (1980) Determination of ion permeability through the channels made of porins from the outer membrane of Salmonella typhimurium in lipid bilayer membranes. Journal of Membrane Biology 56: 19-29
    • (1980) Journal of Membrane Biology , vol.56 , pp. 19-29
    • Jenz, R.1    Ishu, J.2    Nakae, T.3
  • 33
    • 0023627552 scopus 로고
    • Imipenem resistance in Pseudomonas aeruginosa is due to diminished expression of outer membrane proteins
    • 33. Buscher K., Cullman W., Dick W., Wendt S. and Opferkuch W. (1987). Imipenem resistance in Pseudomonas aeruginosa is due to diminished expression of outer membrane proteins. J. Infect. Dis 156: 681-684
    • (1987) J. Infect. Dis , vol.156 , pp. 681-684
    • Buscher, K.1    Cullman, W.2    Dick, W.3    Wendt, S.4    Opferkuch, W.5
  • 34
    • 0023117286 scopus 로고
    • Identification of porins in outer membrane of Proteus, Morganella, and Providencia spp. And their role in outer membrane permeation of beta-lactams
    • 34. Mitsuyama J., Hiruma R., Yamaguchi A. and Sawai T. (1987) Identification of porins in outer membrane of Proteus, Morganella, and Providencia spp. and their role in outer membrane permeation of beta-lactams. Antimicrob. Agents Chemother. 31: 379-384
    • (1987) Antimicrob. Agents Chemother. , vol.31 , pp. 379-384
    • Mitsuyama, J.1    Hiruma, R.2    Yamaguchi, A.3    Sawai, T.4
  • 36
    • 0020465880 scopus 로고
    • Outer membrane permeation of beta-lactam antibiotics in Escherichia coli, Proteus mirabilis, and Enterobacter cloacae
    • 36. Sawai T., Hiruma R., Kawana N., Kaneko M., Taniyasu F. and Inami A. (1982) Outer membrane permeation of beta-lactam antibiotics in Escherichia coli, Proteus mirabilis, and Enterobacter cloacae. Antimicrob. Agents Chemother. 22: 585-592
    • (1982) Antimicrob. Agents Chemother. , vol.22 , pp. 585-592
    • Sawai, T.1    Hiruma, R.2    Kawana, N.3    Kaneko, M.4    Taniyasu, F.5    Inami, A.6
  • 37
    • 0024341335 scopus 로고
    • Decreased outer membrane permeability in imipenem-resistant mutants of Pseudomonas aeruginosa
    • 37. Trias J., Dufresne J., Levesque R.C. and Nikaido H. (1989) Decreased outer membrane permeability in imipenem-resistant mutants of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 33: 1202-1206
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1202-1206
    • Trias, J.1    Dufresne, J.2    Levesque, R.C.3    Nikaido, H.4
  • 38
    • 0023639252 scopus 로고
    • Penetration of beta-lactams through Pseudomonas aeruginosa porin channels
    • 38. Godfrey A.J. and Bryan L.E. (1987) Penetration of beta-lactams through Pseudomonas aeruginosa porin channels. Antimicrob. Agents Chemother. 31: 1216-1221
    • (1987) Antimicrob. Agents Chemother. , vol.31 , pp. 1216-1221
    • Godfrey, A.J.1    Bryan, L.E.2
  • 39
    • 0020438088 scopus 로고
    • Activity of cefoperazone and two beta-lactamase inhibitors, sulbactam and clavulanic acid, against Bacteroides spp. Correlated with beta-lactamase production
    • 39. Crosby M.A. and Gump D.W. (1982) Activity of cefoperazone and two beta-lactamase inhibitors, sulbactam and clavulanic acid, against Bacteroides spp. correlated with beta-lactamase production. Antimicrob. Agents Chemother. 22: 398-405
    • (1982) Antimicrob. Agents Chemother. , vol.22 , pp. 398-405
    • Crosby, M.A.1    Gump, D.W.2
  • 40
    • 0018378617 scopus 로고
    • Factors contributing to resistance to beta-lactam antibiotics in Bacteroides fragilis
    • 40. Olsson B., Dornsbusch K. and Nord C.E. (1979) Factors contributing to resistance to beta-lactam antibiotics in Bacteroides fragilis. Antimicrob. Agents Chemother 15: 263-268
    • (1979) Antimicrob. Agents Chemother , vol.15 , pp. 263-268
    • Olsson, B.1    Dornsbusch, K.2    Nord, C.E.3
  • 41
    • 0028025336 scopus 로고
    • Porins and specific diffusion channels in bacterial outer membranes
    • 41. Nikaido H. (1994) Porins and specific diffusion channels in bacterial outer membranes. J. Biol. Chem. 269: 3905-3908
    • (1994) J. Biol. Chem. , vol.269 , pp. 3905-3908
    • Nikaido, H.1
  • 42
    • 0018180634 scopus 로고
    • A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis
    • 42. Lane L.C. (1978) A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis. Anal. Biochem. 86: 655-664
    • (1978) Anal. Biochem. , vol.86 , pp. 655-664
    • Lane, L.C.1
  • 43
    • 0018613990 scopus 로고
    • Outer membrane of Pseudomonas aeruginosa: Heat-and 2-Mercaptoethanol-modifiable proteins
    • 43. Hancock R.E.W. and Carey A.M. (1979) Outer membrane of Pseudomonas aeruginosa: Heat-and 2-Mercaptoethanol-modifiable proteins. J. Bacteriol. 140: 902-910
    • (1979) J. Bacteriol. , vol.140 , pp. 902-910
    • Hancock, R.E.W.1    Carey, A.M.2
  • 44
    • 0018357034 scopus 로고
    • Identification of the protein producing transmembrane diffusion pores in the outer membrane of Pseudomonas aeroginosa PA01
    • 44. Hancock R.E.W., Decad G.M. and Nikaido H. (1979) Identification of the protein producing transmembrane diffusion pores in the outer membrane of Pseudomonas aeroginosa PA01. Biochim. Biophys. Acta 554: 323-331
    • (1979) Biochim. Biophys. Acta , vol.554 , pp. 323-331
    • Hancock, R.E.W.1    Decad, G.M.2    Nikaido, H.3
  • 45
    • 0024603176 scopus 로고
    • Characterization of the porins of Campylobacter jejuni and Campylobacter coli and implications for antibiotic susceptibility
    • 45. Page W.J., Huyer G., Huyer M. and Worobec E.A. (1989) Characterization of the porins of Campylobacter jejuni and Campylobacter coli and implications for antibiotic susceptibility. Antimicrob. Agents Chemother. 33: 297-303
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 297-303
    • Page, W.J.1    Huyer, G.2    Huyer, M.3    Worobec, E.A.4
  • 47
    • 0024401938 scopus 로고
    • Pseudomonas aeruginosa outer membrane protein F: Structural role and relationship to the Escherichia coli OmpA protein
    • 47. Woodruff W.A. and Hancock R.E. (1989) Pseudomonas aeruginosa outer membrane protein F: structural role and relationship to the Escherichia coli OmpA protein. J. Bacteriol. 171: 3304-3309
    • (1989) J. Bacteriol. , vol.171 , pp. 3304-3309
    • Woodruff, W.A.1    Hancock, R.E.2
  • 48
    • 0028321391 scopus 로고
    • OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms
    • 48. Sugawara E. and Nikaido H. (1994) OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms. J. Biol. Chem. 269: 17981-17987
    • (1994) J. Biol. Chem. , vol.269 , pp. 17981-17987
    • Sugawara, E.1    Nikaido, H.2
  • 49
    • 0024827009 scopus 로고
    • Purification and partial characterization of a major outer membrane protein of Fusobacterium nucleatum
    • 49. Bakken V., Aaro S. and Jensen H.B. (1989) Purification and partial characterization of a major outer membrane protein of Fusobacterium nucleatum. J. Gen. Microbiol. 135: 3253-3262
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 3253-3262
    • Bakken, V.1    Aaro, S.2    Jensen, H.B.3
  • 50
    • 0028822012 scopus 로고
    • The Fusobacterium nucleatum major outer-membrane protein (FomA) forms trimeric, water-filled channels in lipid bilayer membranes
    • 50. Kleivdal H., Benz R. and Jensen H.B. (1995) The Fusobacterium nucleatum major outer-membrane protein (FomA) forms trimeric, water-filled channels in lipid bilayer membranes. Eur. J. Biochem. 233: 310-316
    • (1995) Eur. J. Biochem. , vol.233 , pp. 310-316
    • Kleivdal, H.1    Benz, R.2    Jensen, H.B.3
  • 51
    • 0027373922 scopus 로고
    • Complete sequence of omp1, the structural gene encoding the 40-kDa outer membrane protein of Fusobacterium nucleatum strain Fev1
    • 51. Bolstad A.I. and Jensen H.B. (1993) Complete sequence of omp1, the structural gene encoding the 40-kDa outer membrane protein of Fusobacterium nucleatum strain Fev1. Gene 132: 107-112
    • (1993) Gene , vol.132 , pp. 107-112
    • Bolstad, A.I.1    Jensen, H.B.2
  • 52
    • 0028225962 scopus 로고
    • Sequence variability of the 40-kDa outer membrane proteins of Fusobacterium nucleatum strains a model for the topology of the proteins
    • 52. Bolstad A.I., Tommassen, J. and Jensen H.B. (1994) Sequence variability of the 40-kDa outer membrane proteins of Fusobacterium nucleatum strains a model for the topology of the proteins. Mol. Gen. Gen. 244: 104-110.
    • (1994) Mol. Gen. Gen. , vol.244 , pp. 104-110
    • Bolstad, A.I.1    Tommassen, J.2    Jensen, H.B.3
  • 53
    • 0025812765 scopus 로고
    • Interplay of cell wall barrier and beta-lactamase activity determines high resistance to beta-lactam antibiotics in Mycobacterium chelonae
    • 53. Jarlier V., Gutmann L. and Nikaido H. (1991) Interplay of cell wall barrier and beta-lactamase activity determines high resistance to beta-lactam antibiotics in Mycobacterium chelonae. Antimicrob. Agents Chemother. 35: 1937-1939
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1937-1939
    • Jarlier, V.1    Gutmann, L.2    Nikaido, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.