메뉴 건너뛰기




Volumn 14, Issue 3, 1997, Pages 113-123

A novel family of channel-forming, autotransporting, bacterial virulence factors

Author keywords

Autotransporter domain; Channel; Gram negative bacteria; Outer membrane; Phylogenetic tree; Protein transport; Virulence factor; barrel

Indexed keywords

ADHESIN; CARRIER PROTEIN; CYTOTOXIN; PROTEINASE; VIRULENCE FACTOR;

EID: 0030688998     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.3109/09687689709048171     Document Type: Article
Times cited : (105)

References (52)
  • 2
    • 0026553672 scopus 로고
    • PROSITE - A dictionary of sites and patterns in proteins
    • Bairoch, A. (1992) PROSITE - A dictionary of sites and patterns in proteins. Nucleic Acids Research, 20(Suppl.), S2013-S2018.
    • (1992) Nucleic Acids Research , vol.20 , Issue.SUPPL.
    • Bairoch, A.1
  • 3
    • 0029166295 scopus 로고
    • SepA, the major extracellular protein of Shigella flexneri: Autonomous secretion and involvement in tissue invasion
    • Bejelloun-Touimi, Z., Sansonetti, P. J. and Parsot, C. (1995) SepA, the major extracellular protein of Shigella flexneri: autonomous secretion and involvement in tissue invasion. Molecular Microbiology, 17, 123-135.
    • (1995) Molecular Microbiology , vol.17 , pp. 123-135
    • Bejelloun-Touimi, Z.1    Sansonetti, P.J.2    Parsot, C.3
  • 4
    • 0026742008 scopus 로고
    • AIDA-1, the adhesin involved in diffuse adherence of the diarrhoeagenic Escherichia coli strain 2787 (O126:H27), is synthesized via a precursor molecule
    • Benz, I. and Schmidt, M. A. (1992) AIDA-1, the adhesin involved in diffuse adherence of the diarrhoeagenic Escherichia coli strain 2787 (O126:H27), is synthesized via a precursor molecule. Molecular Microbiology, 6, 1539-1546.
    • (1992) Molecular Microbiology , vol.6 , pp. 1539-1546
    • Benz, I.1    Schmidt, M.A.2
  • 6
    • 0017868338 scopus 로고
    • Empirical prediction of protein conformation
    • Chou, P. Y. and Fasman, G. D. (1978) Empirical prediction of protein conformation. Annual Review of Biochemistry, 47, 251-276.
    • (1978) Annual Review of Biochemistry , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0028308711 scopus 로고
    • Divergence of genetic sequences for the vacuolating cytotoxin among Helicobacter pylori strains
    • Cover, T. L., Tummuru, M. K. R., Cao, P., Thompson, S. A. and Blaser, M. J. (1994) Divergence of genetic sequences for the vacuolating cytotoxin among Helicobacter pylori strains. Journal of Biological Chemistry, 269, 10566-10573.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 10566-10573
    • Cover, T.L.1    Tummuru, M.K.R.2    Cao, P.3    Thompson, S.A.4    Blaser, M.J.5
  • 10
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of Gram-negative bacteria
    • Dinh, T., Paulsen, I. T. and Saier, M. H. Jr (1994) A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of Gram-negative bacteria. Journal of Bacteriology, 176, 3825-3831.
    • (1994) Journal of Bacteriology , vol.176 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier Jr., M.H.3
  • 13
    • 0021152462 scopus 로고
    • Three dimensional structure of membrane and surface proteins
    • Eisenberg, D. (1984) Three dimensional structure of membrane and surface proteins. Annual Review of Biochemistry, 53, 595-623.
    • (1984) Annual Review of Biochemistry , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 14
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • Eisenberg, D., Weiss, R. M. and Terwilliger, T. C. (1982a) The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature, 299, 371-374.
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 17
    • 0025025261 scopus 로고
    • Progressive alignment and phylogenetic tree construction of protein sequences
    • Feng, D.-F. and Doolittle, R. F. (1990) Progressive alignment and phylogenetic tree construction of protein sequences. Methods in Enzymology, 183, 375-387.
    • (1990) Methods in Enzymology , vol.183 , pp. 375-387
    • Feng, D.-F.1    Doolittle, R.F.2
  • 18
    • 0028019294 scopus 로고
    • Cloning and squencing of a Bordetella pertussis serum resistance locus
    • Fernandez, R. C. and Weiss, A. A. (1994) Cloning and squencing of a Bordetella pertussis serum resistance locus. Infection and Immunity, 62, 4727-4738.
    • (1994) Infection and Immunity , vol.62 , pp. 4727-4738
    • Fernandez, R.C.1    Weiss, A.A.2
  • 19
    • 0029056781 scopus 로고
    • Tracheal colonization factor: A Bordetella pertussis secreted virulence determinant
    • Finn, T. M. and Stevens, L. A. (1995) Tracheal colonization factor: a Bordetella pertussis secreted virulence determinant. Molecular Microbiology, 16, 625-634.
    • (1995) Molecular Microbiology , vol.16 , pp. 625-634
    • Finn, T.M.1    Stevens, L.A.2
  • 20
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D. J. and Robson, B. (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. Journal of Molecular Biology, 120, 97-120.
    • (1978) Journal of Molecular Biology , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 21
    • 0027489247 scopus 로고
    • Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: A general system for the formation of surface-associated protein complexes
    • Hobbs, M. and Mattick, J. S. (1993) Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes. Molecular Microbiology, 10, 233-243.
    • (1993) Molecular Microbiology , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 22
    • 0028824728 scopus 로고
    • Common structural features of IgA1 protease-like outer membrane protein autotransporters
    • Jose, J., Jähnig, F. and Meyer, T. F. (1995) Common structural features of IgA1 protease-like outer membrane protein autotransporters. Molecular Microbiology, 18, 377-382.
    • (1995) Molecular Microbiology , vol.18 , pp. 377-382
    • Jose, J.1    Jähnig, F.2    Meyer, T.F.3
  • 23
    • 0025353145 scopus 로고
    • Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: Conformation-dependent outer membrane translocation
    • Klauser, T., Pohlner, J. and Meyer, T. F. (1990) Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: conformation-dependent outer membrane translocation EMBO Journal, 9, 1991-1999.
    • (1990) EMBO Journal , vol.9 , pp. 1991-1999
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 24
    • 0029591170 scopus 로고
    • The unrelated surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocua and Escherichia coli respectively
    • Kocks, C., Marchand, J.-B., Gouin, E., d'Hauteville, H., Sansonetti, P. J., Carlier, M.-F. and Cossart, P. (1995) The unrelated surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocua and Escherichia coli respectively. Molecular Microbiology, 18, 413-423.
    • (1995) Molecular Microbiology , vol.18 , pp. 413-423
    • Kocks, C.1    Marchand, J.-B.2    Gouin, E.3    D'Hauteville, H.4    Sansonetti, P.J.5    Carlier, M.-F.6    Cossart, P.7
  • 25
    • 0028140564 scopus 로고
    • Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution
    • Kreusch, A., Neubüser, A., Schiltz, E., Weckesser, J. and Schulz, G. E. (1994) Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution. Protein Science, 3, 58-63.
    • (1994) Protein Science , vol.3 , pp. 58-63
    • Kreusch, A.1    Neubüser, A.2    Schiltz, E.3    Weckesser, J.4    Schulz, G.E.5
  • 27
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157, 105-132.
    • (1982) Journal of Molecular Biology , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 28
    • 0030024449 scopus 로고    scopus 로고
    • Actin-based bacterial motility: Towards a definition of the minimal requirements
    • Lasa, I. and Cossart, P. (1996) Actin-based bacterial motility: towards a definition of the minimal requirements. Trends in Cell Biology, 6, 109-114.
    • (1996) Trends in Cell Biology , vol.6 , pp. 109-114
    • Lasa, I.1    Cossart, P.2
  • 29
    • 0026738409 scopus 로고
    • Cloning, nucleotide sequence and heterologous expression of the protective outer-membrane protein P.68 pertactin from Bordetella bronchiseptica
    • Li, J., Fairweather, N. F., Novotny, P., Dougan, G. and Charles, I. G. (1992) Cloning, nucleotide sequence and heterologous expression of the protective outer-membrane protein P.68 pertactin from Bordetella bronchiseptica. Journal of General Microbiology, 138, 1697-1705.
    • (1992) Journal of General Microbiology , vol.138 , pp. 1697-1705
    • Li, J.1    Fairweather, N.F.2    Novotny, P.3    Dougan, G.4    Charles, I.G.5
  • 30
    • 0028911149 scopus 로고
    • Comparative characterization of the iga gene encoding IgA1 protease in Neisseria meningitidis, Neisseria gonorrhoeae and Haemophilus influenzae
    • Lomholt, H., Poulsen K. and Kilian, M. (1995) Comparative characterization of the iga gene encoding IgA1 protease in Neisseria meningitidis, Neisseria gonorrhoeae and Haemophilus influenzae. Molecular Microbiology, 15, 495-506.
    • (1995) Molecular Microbiology , vol.15 , pp. 495-506
    • Lomholt, H.1    Poulsen, K.2    Kilian, M.3
  • 31
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas, D. and Raina, S. (1997) Protein folding in the bacterial periplasm. Journal of Bacteriology, 179, 2465-2471.
    • (1997) Journal of Bacteriology , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 32
    • 0030273775 scopus 로고    scopus 로고
    • Molecular and structural aspects of fimbriae biosynthesis and assembly in Escherichia coli
    • Mol, O. and Oudega, B. (1996) Molecular and structural aspects of fimbriae biosynthesis and assembly in Escherichia coli. FEMS Microbiology Reviews, 19, 25-52.
    • (1996) FEMS Microbiology Reviews , vol.19 , pp. 25-52
    • Mol, O.1    Oudega, B.2
  • 33
    • 0028670436 scopus 로고
    • Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme
    • Ohnishi, Y., Nishiyama, M., Horinouchi, S. and Beppu, T. (1994) Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme. Journal of Biological Chemistry, 269, 32800-32806.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 32800-32806
    • Ohnishi, Y.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 34
    • 0028270818 scopus 로고
    • Identification and molecular characterization of a major ring-forming surface protein from the gastric pathogen Helicobacter mustelae
    • O'Toole, P. W., Austin, J. W. and Trust, T. J. (1994) Identification and molecular characterization of a major ring-forming surface protein from the gastric pathogen Helicobacter mustelae. Molecular Microbiology, 11, 349-361.
    • (1994) Molecular Microbiology , vol.11 , pp. 349-361
    • O'Toole, P.W.1    Austin, J.W.2    Trust, T.J.3
  • 35
    • 0030843523 scopus 로고    scopus 로고
    • Computer-based analyses of the protein constituents of transport systems catalyzing export of complex carbohydrates in bacteria
    • in press
    • Paulsen, I. T., Beness, A. M. and Saier, M. H., Jr (1997) Computer-based analyses of the protein constituents of transport systems catalyzing export of complex carbohydrates in bacteria. Microbiology, in press.
    • (1997) Microbiology
    • Paulsen, I.T.1    Beness, A.M.2    Saier Jr., M.H.3
  • 37
    • 0023128808 scopus 로고
    • Gene structure and extra-cellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner, J., Halter, R., Beyreuther, K. and Meyer, T. F. (1987) Gene structure and extra-cellular secretion of Neisseria gonorrhoeae IgA protease. Nature, 325, 458-462.
    • (1987) Nature , vol.325 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 38
    • 0026717378 scopus 로고
    • A comparative genetic study of serologically distinct Haemophilus influenzae type 1 immunoglobulin A1 proteases
    • Poulsen, K., Reinholdt, J. and Kilian, M. (1992) A comparative genetic study of serologically distinct Haemophilus influenzae type 1 immunoglobulin A1 proteases. Journal of Bacteriology, 174, 2913-2921.1
    • (1992) Journal of Bacteriology , vol.174 , pp. 2913-29211
    • Poulsen, K.1    Reinholdt, J.2    Kilian, M.3
  • 39
    • 0028348785 scopus 로고
    • Isolation and characterization of a gene involved in hemagglutination by an avian pathogenic Escherichia coli strain
    • Provence, D. L. and Curtiss, R., III (1994) Isolation and characterization of a gene involved in hemagglutination by an avian pathogenic Escherichia coli strain. Infection and Immunity, 62, 1369-1380.
    • (1994) Infection and Immunity , vol.62 , pp. 1369-1380
    • Provence, D.L.1    Curtiss III, R.2
  • 40
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley, A. P. (1993) The complete general secretory pathway in Gram-negative bacteria. Microbiological Reviews, 57, 50-108.
    • (1993) Microbiological Reviews , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 41
    • 0028345374 scopus 로고
    • Computer-aided analyses of transport protein sequences: Gleaning evidence concerning function, structure, biogenesis, and evolution
    • Saier, M. H., Jr (1994) Computer-aided analyses of transport protein sequences: gleaning evidence concerning function, structure, biogenesis, and evolution. Microbiological Reviews, 58, 71-93.
    • (1994) Microbiological Reviews , vol.58 , pp. 71-93
    • Saier Jr., M.H.1
  • 42
    • 0030309453 scopus 로고    scopus 로고
    • Phylogentic approaches to the identification and characterization of protein families and superfamilies
    • Saier, M. H. Jr (1996) Phylogentic approaches to the identification and characterization of protein families and superfamilies. Microbial & Comparative Genomics, 1, 129-150.
    • (1996) Microbial & Comparative Genomics , vol.1 , pp. 129-150
    • Saier Jr., M.H.1
  • 43
    • 0028365952 scopus 로고
    • Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport
    • Saier, M. H., Jr, Tam, R., Reizer, A. and Reizer, J. (1994) Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Molecular Microbiology, 11, 841-847.
    • (1994) Molecular Microbiology , vol.11 , pp. 841-847
    • Saier Jr., M.H.1    Tam, R.2    Reizer, A.3    Reizer, J.4
  • 44
    • 85036684729 scopus 로고
    • Insertion of proteins into bacterial membranes: Mechanism, characteristics, and comparisons with the eucaryotic process
    • Saier, M. H., Jr, Werner, P. K. and Müller, M. (1989) Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process. Microbial & Comparative Genomics, 1, 129-150.
    • (1989) Microbial & Comparative Genomics , vol.1 , pp. 129-150
    • Saier Jr., M.H.1    Werner, P.K.2    Müller, M.3
  • 45
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G. and Dobberstein, B. (1996) Common principles of protein translocation across membranes. Science, 271, 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 46
    • 0027640084 scopus 로고
    • Bacterial porins: Structure and function
    • Schulz, G. E. (1993) Bacterial porins: structure and function. Current Opinion in Cell Biology, 5, 701-707.
    • (1993) Current Opinion in Cell Biology , vol.5 , pp. 701-707
    • Schulz, G.E.1
  • 47
    • 0029961503 scopus 로고    scopus 로고
    • Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins
    • Stein, M., Kenny, B., Stein, M. A. and Finlay, B. B. (1996) Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins. Journal of Bacteriology, 178, 6546-6554
    • (1996) Journal of Bacteriology , vol.178 , pp. 6546-6554
    • Stein, M.1    Kenny, B.2    Stein, M.A.3    Finlay, B.B.4
  • 48
    • 0027987985 scopus 로고
    • A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells
    • St Geme, J. W., III, de la Morena, M. L. and Falkow, S. (1994) A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells. Molecular Microbiology, 14, 217-233.
    • (1994) Molecular Microbiology , vol.14 , pp. 217-233
    • St Geme III, J.W.1    De La Morena, M.L.2    Falkow, S.3
  • 50
    • 0028951802 scopus 로고
    • The hrp gene locus of Pseudomonas solanacearum, which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex
    • Van Gijsegem, F., Gough, C., Zischek, C., Niqueux, E., Arlat, M., Genin, S., Barberis, P., German, S., Castello, P. and Boucher, C. (1995). The hrp gene locus of Pseudomonas solanacearum, which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex. Molecular Microbiology, 15, 1095-1114.
    • (1995) Molecular Microbiology , vol.15 , pp. 1095-1114
    • Van Gijsegem, F.1    Gough, C.2    Zischek, C.3    Niqueux, E.4    Arlat, M.5    Genin, S.6    Barberis, P.7    German, S.8    Castello, P.9    Boucher, C.10
  • 52
    • 0022652268 scopus 로고
    • Specific excretion of Serratia marcescens protease through the outer membrane of Escherichia coli
    • Yanagida, N., Ouzumi, T. and Beppu, T. (1986) Specific excretion of Serratia marcescens protease through the outer membrane of Escherichia coli. Journal of Bacteriology, 166, 937-944.
    • (1986) Journal of Bacteriology , vol.166 , pp. 937-944
    • Yanagida, N.1    Ouzumi, T.2    Beppu, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.