메뉴 건너뛰기




Volumn 199, Issue 1, 2001, Pages 1-7

Multiple facets of bacterial porins

Author keywords

Adhesin; Bacterium; Immunogene; Outer membrane protein; Porin; Receptor

Indexed keywords

BACTERICIDE; PORIN;

EID: 0035873239     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(01)00127-6     Document Type: Article
Times cited : (198)

References (39)
  • 1
    • 0002431489 scopus 로고    scopus 로고
    • Outer membrane. In: Escherichia coli and Salmonella, Cellular and Molecular Biology
    • Neidhardt, F.C., Ed., ASM Press, Washington, DC.
    • Nikaido, H. (1996) Outer membrane. In: Escherichia coli and Salmonella, Cellular and Molecular Biology (Neidhardt, F.C., Ed.), pp. 29-47. ASM Press, Washington, DC.
    • (1996) , pp. 29-47
    • Nikaido, H.1
  • 2
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: barrels in a nutshell
    • Koebnik, R., Locher, K.P. and Van Gelder, P. (2000) Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol. 37, 239-253.
    • (2000) Mol. Microbiol , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 3
    • 0017155947 scopus 로고
    • Identification of the outer membrane protein of Escherichia coli that produces transmembrane channels in reconstituted vesicle membranes
    • Nakae, T. (1976) Identification of the outer membrane protein of Escherichia coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem. Biophys. Res. Commun. 71, 877-884.
    • (1976) Biochem. Biophys. Res. Commun , vol.71 , pp. 877-884
    • Nakae, T.1
  • 5
    • 0026737314 scopus 로고
    • Protein, Structure of porin refined at 1.8 Aî resolution
    • Weiss, M.S. and Schulz, G.E. (1992) Protein, Structure of porin refined at 1.8 Aî resolution. J. Mol. Biol. 227, 493-509.
    • (1992) J. Mol. Biol. , vol.227 , pp. 493-509
    • Weiss, M.S.1    Schulz, G.E.2
  • 6
    • 0029992419 scopus 로고    scopus 로고
    • From acids to osmZ: multiple factors in£uence synthesis of OmpF and OmpC porins in Escherichia coli
    • Pratt, L.A., Hsing, W., Gibson, K.E. and Silhavy, T.J. (1996) From acids to osmZ: multiple factors in£uence synthesis of OmpF and OmpC porins in Escherichia coli. Mol. Microbiol. 20, 911-917.
    • (1996) Mol. Microbiol , vol.20 , pp. 911-917
    • Pratt, L.A.1    Hsing, W.2    Gibson, K.E.3    Silhavy, T.J.4
  • 7
    • 0344004830 scopus 로고    scopus 로고
    • Identification and characterization of a new porin gene of K. pneumoniae. Its role in L-lactam antibiotic resistance
    • Domenech-Sanchez, A., Hernandez-Alles, S., Martinez-Martinez, L., Benedi, V.J. and Alberti, S. (1999) Identification and characterization of a new porin gene of K. pneumoniae. Its role in L-lactam antibiotic resistance. J. Bacteriol. 181, 2726-2732.
    • (1999) J. Bacteriol , vol.181 , pp. 2726-2732
    • Domenech-Sanchez, A.1    Hernandez-Alles, S.2    Martinez-Martinez, L.3    Benedi, V.J.4    Alberti, S.5
  • 8
    • 0032844440 scopus 로고    scopus 로고
    • The mar regulon: multiple resistance to antibiotics and other toxic chemicals
    • Aleskun, M.N. and Levy, S.B. (1999) The mar regulon: multiple resistance to antibiotics and other toxic chemicals. Trends Microbiol. 7, 410-413.
    • (1999) Trends Microbiol , vol.7 , pp. 410-413
    • Aleskun, M.N.1    Levy, S.B.2
  • 9
    • 0030841732 scopus 로고    scopus 로고
    • Function and modulation of bacterial porins: insights from electrophysiology
    • Delcour, A.H. (1997) Function and modulation of bacterial porins: insights from electrophysiology. FEMS Microbiol. Lett. 151, 115-123.
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 115-123
    • Delcour, A.H.1
  • 10
    • 0023698816 scopus 로고
    • Mutations that alter the pore function of the OmpF porin of Escherichia coli K-12
    • Benson, S.A., Occi, J.L.L. and Sampson, B.A. (1988) Mutations that alter the pore function of the OmpF porin of Escherichia coli K-12. J. Mol. Biol. 203, 961-970.
    • (1988) J. Mol. Biol , vol.203 , pp. 961-970
    • Benson, S.A.1    Occi, J.L.L.2    Sampson, B.A.3
  • 11
    • 0027152155 scopus 로고
    • Specific regions of Escherichia coli OmpF protein involved in antigenic and colicin receptor sites and in stable trimerization
    • Fourel, D., Mizushima, S., Bernadac, A. and Pages, J.-M. (1993) Specific regions of Escherichia coli OmpF protein involved in antigenic and colicin receptor sites and in stable trimerization. J. Bacteriol. 175, 2754-2757.
    • (1993) J. Bacteriol , vol.175 , pp. 2754-2757
    • Fourel, D.1    Mizushima, S.2    Bernadac, A.3    Pages, J.-M.4
  • 13
    • 0033978873 scopus 로고    scopus 로고
    • Substitutions in the eyelet region disrupt cefepime di¡usion through the Escherichia coli OmpF channel
    • Simonet, V., Mallea, M. and Pages, J.-M. (2000) Substitutions in the eyelet region disrupt cefepime di¡usion through the Escherichia coli OmpF channel. Antimicrob. Agents Chemother. 44, 311-315.
    • (2000) Antimicrob. Agents Chemother , vol.44 , pp. 311-315
    • Simonet, V.1    Mallea, M.2    Pages, J.-M.3
  • 14
    • 0030839791 scopus 로고    scopus 로고
    • Complex inhibition of OmpF and OmpC bacterial porins by polyamines
    • Iyer, R. and Delcour, A.H. (1997) Complex inhibition of OmpF and OmpC bacterial porins by polyamines. J. Biol. Chem. 272, 18595-18601.
    • (1997) J. Biol. Chem , vol.272 , pp. 18595-18601
    • Iyer, R.1    Delcour, A.H.2
  • 15
    • 0025140705 scopus 로고
    • Signal transduction and gene regulation through the phosphorylation of two regulatory components: the molecular basis for the osmotic regulation of the porin genes
    • Mizuno, T. and Mizushima, S. (1990) Signal transduction and gene regulation through the phosphorylation of two regulatory components: the molecular basis for the osmotic regulation of the porin genes. Mol. Microbiol. 4, 1077-1082.
    • (1990) Mol. Microbiol , vol.4 , pp. 1077-1082
    • Mizuno, T.1    Mizushima, S.2
  • 16
    • 0033539905 scopus 로고    scopus 로고
    • In vivo modification of porin activity conferring antibiotic resistance to Enterobacter aerogenes
    • Chevalier, J., Pages, J.-M. and Mallea, M. (1999) in vivo modification of porin activity conferring antibiotic resistance to Enterobacter aerogenes. Biochem. Biophys. Res. Commun. 266, 248-251.
    • (1999) Biochem. Biophys. Res. Commun , vol.266 , pp. 248-251
    • Chevalier, J.1    Pages, J.-M.2    Mallea, M.3
  • 17
    • 0031753295 scopus 로고    scopus 로고
    • Gonococcal resistance to L-lactams and tetracycline involves mutation in loop 3 of the porin encoded at the penB locus
    • Gill, M.J., Simjee, S., Al-Hattawi, K., Robertson, B.D., Easmon, C.S.F. and Ison, C.A. (1998) Gonococcal resistance to L-lactams and tetracycline involves mutation in loop 3 of the porin encoded at the penB locus. Antimicrob. Agents Chemother. 42, 2799-2803.
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 2799-2803
    • Gill, M.J.1    Simjee, S.2    Al-Hattawi, K.3    Robertson, B.D.4    Easmon, C.S.F.5    Ison, C.A.6
  • 19
    • 0033522876 scopus 로고    scopus 로고
    • Porins OmpC and PhoE of Escherichia coli as specific cell-surface targets of human lactoferrin
    • Sallmann, F.R., Baveye-Descamps, S., Pattus, F., Salmon, V., Branza, N., Spik, G. and Legrand, D. (1999) Porins OmpC and PhoE of Escherichia coli as specific cell-surface targets of human lactoferrin. J. Bacteriol. 274, 16107-16114.
    • (1999) J. Bacteriol , vol.274 , pp. 16107-16114
    • Sallmann, F.R.1    Baveye-Descamps, S.2    Pattus, F.3    Salmon, V.4    Branza, N.5    Spik, G.6    Legrand, D.7
  • 21
    • 0031848916 scopus 로고    scopus 로고
    • Activation of the complement classical pathway (C1q binding) by mesophilic Aeromonas hydrophila outer membrane protein
    • Merino, S., Nogueras, M.M., Aguilar, A., Rubires, X., Alberti, S., Benedi, V.J. and Tomas, J.M. (1998) Activation of the complement classical pathway (C1q binding) by mesophilic Aeromonas hydrophila outer membrane protein. Infect. Immun. 66, 3825-3831.
    • (1998) Infect. Immun. , vol.66 , pp. 3825-3831
    • Merino, S.1    Nogueras, M.M.2    Aguilar, A.3    Rubires, X.4    Alberti, S.5    Benedi, V.J.6    Tomas, J.M.7
  • 22
    • 0031907391 scopus 로고    scopus 로고
    • A major outer membrane protein of Rahnella aquatilis functions as a porin and root adhesin
    • Achouak, W., Pages, J.M., De Mot, R., Molle, G. and Heulin, T. (1998) A major outer membrane protein of Rahnella aquatilis functions as a porin and root adhesin. J. Bacteriol. 180, 900-913.
    • (1998) J. Bacteriol , vol.180 , pp. 900-913
    • Achouak, W.1    Pages, J.M.2    De Mot, R.3    Molle, G.4    Heulin, T.5
  • 23
    • 0025880246 scopus 로고
    • Purification of a rootadhesive outer membrane protein of root-colonizing Pseudomonas £uorescens
    • De Mot, R. and Van der leyden, J. (1991) Purification of a rootadhesive outer membrane protein of root-colonizing Pseudomonas £uorescens. FEMS Microbiol. Lett. 81, 323-328.
    • (1991) FEMS Microbiol. Lett , vol.81 , pp. 323-328
    • De Mot, R.1    Van der leyden, J.2
  • 24
    • 0033916611 scopus 로고    scopus 로고
    • Genes expressed in Pseudomonas putida during colonization of a plant-pathogenic fungus
    • Lee, S.W. and Cooksey, D.A. (2000) Genes expressed in Pseudomonas putida during colonization of a plant-pathogenic fungus. Appl. Environ. Microbiol. 66, 2764-2772.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 2764-2772
    • Lee, S.W.1    Cooksey, D.A.2
  • 25
    • 0024399678 scopus 로고
    • Characterization of porin and ompR mutants of a virulent strain of Salmonella typhimurium: ompR mutants are attenuated in vivo
    • Dorman, C.J., Chatfield, S., Higgins, C.F., Hayward, C. and Dougan, G. (1989) Characterization of porin and ompR mutants of a virulent strain of Salmonella typhimurium: ompR mutants are attenuated in vivo. Infect. Immun. 57, 26-2140.
    • (1989) Infect. Immun , vol.57 , pp. 26-2140
    • Dorman, C.J.1    Chatfield, S.2    Higgins, C.F.3    Hayward, C.4    Dougan, G.5
  • 26
    • 0027261249 scopus 로고
    • OmpC is involved in invasion of epithelial cells by Shigella £exneri
    • Bernardini, M.L., Sanna, M.G., Fontaine, A. and Sansonetti, P. (1993) OmpC is involved in invasion of epithelial cells by Shigella £exneri. Infect. Immun. 61, 3625-3635.
    • (1993) Infect. Immun. , vol.61 , pp. 3625-3635
    • Bernardini, M.L.1    Sanna, M.G.2    Fontaine, A.3    Sansonetti, P.4
  • 27
    • 0032788485 scopus 로고    scopus 로고
    • Identification and characterization of a cytotoxic porin-lipopolysaccharide complex produced by Campylobacter jejuni
    • Bacon, D.J., Johnson, W.M. and Rodgers, F.G. (1999) Identification and characterization of a cytotoxic porin-lipopolysaccharide complex produced by Campylobacter jejuni. J. Med. Microbiol. 48, 1-10.
    • (1999) J. Med. Microbiol , vol.48 , pp. 1-10
    • Bacon, D.J.1    Johnson, W.M.2    Rodgers, F.G.3
  • 28
    • 0026531202 scopus 로고
    • In vivo binding of Campylobacter jejuni/coli outer membrane preparations to INT 407 cell membranes.
    • Moser, I., Schro« der, W.F.K.J. and Hellmann, E. (1992) In vivo binding of Campylobacter jejuni/coli outer membrane preparations to INT 407 cell membranes. Med. Microbiol. Immunol. 180, 289-303.
    • (1992) Med. Microbiol. Immunol , vol.180 , pp. 289-303
    • Moser, I.1    Schroder, W.F.K.J.2    Hellmann, E.3
  • 29
    • 0033982811 scopus 로고    scopus 로고
    • Molecular cloning and transcriptional regulation of ompT, a ToxR-repressed gene in Vibrio cholerae
    • Li, C.C., Crawford, J.A., Di Rita, V.J. and Kaper, J.B. (2000) Molecular cloning and transcriptional regulation of ompT, a ToxR-repressed gene in Vibrio cholerae. Mol. Microbiol. 35, 189-203.
    • (2000) Mol. Microbiol , vol.35 , pp. 189-203
    • Li, C.C.1    Crawford, J.A.2    Di Rita, V.J.3    Kaper, J.B.4
  • 30
    • 0034730163 scopus 로고    scopus 로고
    • Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor expression, and intestinal colonization
    • Provenzano, D. and Klose, K.E. (2000) Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor expression, and intestinal colonization. Proc. Natl. Acad. Sci. USA 97, 10220-10224
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10220-10224
    • Provenzano, D.1    Klose, K.E.2
  • 31
    • 0025743536 scopus 로고
    • Bacterial entry and intracellular processing of Neisseria gonorrhoeae in epithelial cells : immuno-morphological evidence for alterations in the major outer membrane protein
    • Weel, J.F.L., Hopman, C.T.P. and van Putten, J.P.M. (1991) Bacterial entry and intracellular processing of Neisseria gonorrhoeae in epithelial cells : immuno-morphological evidence for alterations in the major outer membrane protein. J. Exp. Med. 174, 705-715.
    • (1991) J. Exp. Med , vol.174 , pp. 705-715
    • Weel, J.F.L.1    Hopman, C.T.P.2    van Putten, J.P.M.3
  • 32
    • 0344142375 scopus 로고    scopus 로고
    • Neisserial porin (PorB) causes rapid calcium in£ux in target cells and induces apoptosis by the activation of cysteine proteases
    • Mu« ller, A., Gu«nther, D., Du« x, F., Naumann, M.MeyerT.F. and Rudel, T. (1999) Neisserial porin (PorB) causes rapid calcium in£ux in target cells and induces apoptosis by the activation of cysteine proteases. EMBO J. 18, 339-352.
    • (1999) EMBO J. , vol.18 , pp. 339-352
    • Muller, A.1    Gunther, D.2    Dux, F.3    Naumann, F.4    Meyer, T.F.5    Rudel, T.6
  • 33
    • 0033306182 scopus 로고    scopus 로고
    • The porin OmpC of Salmonella typhimurium mediates adherence to macrophages
    • Negm, R.S. and Pistole, T.G. (1999) The porin OmpC of Salmonella typhimurium mediates adherence to macrophages. Can. J. Microbiol. 45, 658-669.
    • (1999) Can. J. Microbiol , vol.45 , pp. 658-669
    • Negm, R.S.1    Pistole, T.G.2
  • 34
    • 0033037917 scopus 로고    scopus 로고
    • Porins and lipopolysaccharide (LPS) from Salmonella typhimurium induce leucocyte transmigration through human endothelial cells in vitro
    • Galdiero, M., Folgore, A., Molitierno, M. and Greco, R. (1999) Porins and lipopolysaccharide (LPS) from Salmonella typhimurium induce leucocyte transmigration through human endothelial cells in vitro. Clin. Exp. Immunol. 116, 453-461.
    • (1999) Clin. Exp. Immunol , vol.116 , pp. 453-461
    • Galdiero, M.1    Folgore, A.2    Molitierno, M.3    Greco, R.4
  • 36
    • 0029860724 scopus 로고    scopus 로고
    • High mutation frequencies among Escherichia coli and Salmonella pathogens
    • LeClerc, J.E., Li, B., Payne, W.L. and Cebula, T.A. (1996) High mutation frequencies among Escherichia coli and Salmonella pathogens. Science 274, 1208-1211.
    • (1996) Science , vol.274 , pp. 1208-1211
    • LeClerc, J.E.1    Li, B.2    Payne, W.L.3    Cebula, T.A.4
  • 37
    • 0034063606 scopus 로고    scopus 로고
    • Sequence variation in the porA gene of a clone of Neisseria meningitidis during epidemic spread
    • Jelfs, J., Munro, R., Wedege, E. and Caugant, D.A. (2000) Sequence variation in the porA gene of a clone of Neisseria meningitidis during epidemic spread. Clin. Diagn. Lab. Immunol. 3, 390-395.
    • (2000) Clin. Diagn. Lab. Immunol , vol.3 , pp. 390-395
    • Jelfs, J.1    Munro, R.2    Wedege, E.3    Caugant, D.A.4
  • 38
    • 0031697119 scopus 로고    scopus 로고
    • Characterization of a phage specific to hemorrhagic Escherichia coli O157:H7 and disclosure of variations in host outer membrane protein OmpC
    • Yu, S.L., Ding, H.C., Seah, J.N., Wu, K.M., Chang, Y.C., Chang, K.S.S., Tam, M.F. and Syu, W.J. (1998) Characterization of a phage specific to hemorrhagic Escherichia coli O157:H7 and disclosure of variations in host outer membrane protein OmpC. J. Biomed. Sci. 5, 370-382.
    • (1998) J. Biomed. Sci , vol.5 , pp. 370-382
    • Yu, S.L.1    Ding, H.C.2    Seah, J.N.3    Wu, K.M.4    Chang, Y.C.5    Chang, K.S.S.6    Tam, M.F.7    Syu, W.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.