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Volumn 180, Issue 24, 1998, Pages 6450-6458

Campylobacter fetus surface layer proteins are transported by a type I secretion system

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0032425549     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.24.6450-6458.1998     Document Type: Article
Times cited : (45)

References (64)
  • 2
    • 0031748720 scopus 로고    scopus 로고
    • The Caulobacter crescentus paracrystalline S-layer protein is secreted by an ABC transporter (type I) secretion apparatus
    • Awram, P., and J. Smit. 1998. The Caulobacter crescentus paracrystalline S-layer protein is secreted by an ABC transporter (type I) secretion apparatus. J. Bacteriol. 180:3062-3069.
    • (1998) J. Bacteriol. , vol.180 , pp. 3062-3069
    • Awram, P.1    Smit, J.2
  • 3
    • 0001246049 scopus 로고
    • Derivations and genotypes of some mutant derivatives of Escherichia coli K-12
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Bachman, B. J. 1987. Derivations and genotypes of some mutant derivatives of Escherichia coli K-12, p. 1190-1219. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, vol 2. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , vol.2 , pp. 1190-1219
    • Bachman, B.J.1
  • 4
    • 0029806326 scopus 로고    scopus 로고
    • Cloning of the Serratia marcescens hasF gene encoding the Has ABC exporter outer membrane component: A TolC analogue
    • Binet, R., and C. Wandersman. 1997. Cloning of the Serratia marcescens hasF gene encoding the Has ABC exporter outer membrane component: a TolC analogue. Mol. Microbiol. 22:265-273.
    • (1997) Mol. Microbiol. , vol.22 , pp. 265-273
    • Binet, R.1    Wandersman, C.2
  • 5
    • 0029056415 scopus 로고
    • Protein secretion by hybrid bacterial ABC-transporters: Specific functions of the membrane ATPase and the membrane fusion protein
    • Binet, R., and C. Wandersman. 1995. Protein secretion by hybrid bacterial ABC-transporters: specific functions of the membrane ATPase and the membrane fusion protein. EMBO J. 14:2298-2306.
    • (1995) EMBO J. , vol.14 , pp. 2298-2306
    • Binet, R.1    Wandersman, C.2
  • 6
    • 0029785027 scopus 로고    scopus 로고
    • The extreme N-terminus of the Caulobacter crescentus S-layer protein directs export of passenger proteins from the cytoplasm but is not required for secretion of the native protein
    • Bingle, VV. H., K. D. Le, and J. Smit. 1996. The extreme N-terminus of the Caulobacter crescentus S-layer protein directs export of passenger proteins from the cytoplasm but is not required for secretion of the native protein. Can. J. Microbiol. 42:672-684.
    • (1996) Can. J. Microbiol. , vol.42 , pp. 672-684
    • Bingle, V.V.H.1    Le, K.D.2    Smit, J.3
  • 7
    • 0031029608 scopus 로고    scopus 로고
    • Linker mutagenesis of the Caulobacter crescentus S-layer protein: Toward a definition of an N-terminal anchoring region and a C-terminal secretion signal and the potential for heterologous protein secretion
    • Bingle, W. H., J. F. Nomellini, and J. Smit. 1997. Linker mutagenesis of the Caulobacter crescentus S-layer protein: toward a definition of an N-terminal anchoring region and a C-terminal secretion signal and the potential for heterologous protein secretion. J. Bacteriol 179:601-611.
    • (1997) J. Bacteriol , vol.179 , pp. 601-611
    • Bingle, W.H.1    Nomellini, J.F.2    Smit, J.3
  • 8
    • 0027967847 scopus 로고
    • Alkaline phosphatase and a cellulase reporter are not exported from the cytoplasm when fused to large N-terminal portions of the Caulobacter crescentus S-layer protein
    • Bingle, W. H., and J. Smit. 1994. Alkaline phosphatase and a cellulase reporter are not exported from the cytoplasm when fused to large N-terminal portions of the Caulobacter crescentus S-layer protein. Can. J. Microbiol. 40:777-782.
    • (1994) Can. J. Microbiol. , vol.40 , pp. 777-782
    • Bingle, W.H.1    Smit, J.2
  • 9
    • 0342703125 scopus 로고
    • Definition of form and function for the S-layer of Cavlobacter crescentus
    • T. L. Beveridge and S. F. Koval (ed.), Plenum Press, New York, N.Y.
    • Bingle, W. H., S. G. Walker, and J. Smit. 1993. Definition of form and function for the S-layer of Cavlobacter crescentus, p. 181-194. In T. L. Beveridge and S. F. Koval (ed.), Advances in paracrystalline bacterial surface layers. Plenum Press, New York, N.Y.
    • (1993) Advances in Paracrystalline Bacterial Surface Layers , pp. 181-194
    • Bingle, W.H.1    Walker, S.G.2    Smit, J.3
  • 10
    • 0025701183 scopus 로고
    • Surface array protein of Campylobacter fetus: Cloning and gene structure
    • Blaser, M. J., and E. C. Gotschlich. 1990. Surface array protein of Campylobacter fetus: cloning and gene structure. J. Biol. Chem. 265:14529-14535.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14529-14535
    • Blaser, M.J.1    Gotschlich, E.C.2
  • 11
    • 0027507214 scopus 로고
    • Pathogenesis of Campylobacter fetus infections: Critical role of high-molecular-weight S-layer proteins in virulence
    • Blaser, M. J., and Z. Pei. 1993. Pathogenesis of Campylobacter fetus infections: critical role of high-molecular-weight S-layer proteins in virulence. J. Infect. Dis. 167:372-377.
    • (1993) J. Infect. Dis. , vol.167 , pp. 372-377
    • Blaser, M.J.1    Pei, Z.2
  • 12
    • 0021991825 scopus 로고
    • Susceptibility of Campylobacter isolates to the bactericidal activity in human serum
    • Blaser, M. J., P. F. Smith, and P. A. Kohler. 1985. Susceptibility of Campylobacter isolates to the bactericidal activity in human serum. J. Infect. Dis. 151:227-235.
    • (1985) J. Infect. Dis. , vol.151 , pp. 227-235
    • Blaser, M.J.1    Smith, P.F.2    Kohler, P.A.3
  • 13
    • 0023947952 scopus 로고
    • Pathogenesis of Campylobacter fetus infections: Failure of encapsulated Campylobacter fetus to bind C3b explains serum and phagocytosis resistance
    • Blaser, M. J., P. F. Smith, J. E. Repine, and K. A. Joiner. 1988. Pathogenesis of Campylobacter fetus infections: failure of encapsulated Campylobacter fetus to bind C3b explains serum and phagocytosis resistance. J. Clin. Invest. 81:1434-1444.
    • (1988) J. Clin. Invest. , vol.81 , pp. 1434-1444
    • Blaser, M.J.1    Smith, P.F.2    Repine, J.E.3    Joiner, K.A.4
  • 14
    • 0028075581 scopus 로고
    • High-frequency S-layer protein variation in Campylobacter fetus revealed by sapA mutagenesis
    • Blaser, M. J., E. Wang, M. K. R. Tummuru, R. Washburn, S. Fujimoto, and A. Labigne. 1994. High-frequency S-layer protein variation in Campylobacter fetus revealed by sapA mutagenesis. Mol. Microbiol. 14:453-462.
    • (1994) Mol. Microbiol. , vol.14 , pp. 453-462
    • Blaser, M.J.1    Wang, E.2    Tummuru, M.K.R.3    Washburn, R.4    Fujimoto, S.5    Labigne, A.6
  • 15
    • 0029786250 scopus 로고    scopus 로고
    • Expression, secretion and antigenic variation of bacterial S-layer proteins
    • Boot, H. J., and P. H. Pouwels. 1996. Expression, secretion and antigenic variation of bacterial S-layer proteins. Mol. Microbiol. 21:1117-1123.
    • (1996) Mol. Microbiol. , vol.21 , pp. 1117-1123
    • Boot, H.J.1    Pouwels, P.H.2
  • 16
    • 0030060225 scopus 로고    scopus 로고
    • Random and directed mutagenesis to elucidate the functional importance of helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin
    • Chervaux, C., and I. B. Holland. 1996. Random and directed mutagenesis to elucidate the functional importance of helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin. J. Bacteriol. 178: 1232-1236.
    • (1996) J. Bacteriol. , vol.178 , pp. 1232-1236
    • Chervaux, C.1    Holland, I.B.2
  • 17
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 18
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria
    • Dinh, T., I. T. Pauken, and M. H. Saier, Jr. 1994. A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria. J. Bacteriol. 176:3825-3831.
    • (1994) J. Bacteriol. , vol.176 , pp. 3825-3831
    • Dinh, T.1    Pauken, I.T.2    Saier Jr., M.H.3
  • 19
    • 0025033907 scopus 로고
    • Antigenic differences among Campylobacter fetus S-layer proteins
    • Dubreuil, J. D., M. Kostrzynska, J. W. Austin, and T. J. Trust. 1990. Antigenic differences among Campylobacter fetus S-layer proteins. J. Bacteriol. 172:5035-5043.
    • (1990) J. Bacteriol. , vol.172 , pp. 5035-5043
    • Dubreuil, J.D.1    Kostrzynska, M.2    Austin, J.W.3    Trust, T.J.4
  • 20
    • 0029815310 scopus 로고    scopus 로고
    • Protein secretion by heterologous bacterial transporters: The C-terminus secretion signal of the secreted protein confers high recognition specificity
    • Duong, F., A. Lazdunski, and M. Murgier. 1996. Protein secretion by heterologous bacterial transporters: the C-terminus secretion signal of the secreted protein confers high recognition specificity. Mol. Microbiol. 21:459-470.
    • (1996) Mol. Microbiol. , vol.21 , pp. 459-470
    • Duong, F.1    Lazdunski, A.2    Murgier, M.3
  • 21
    • 0028240371 scopus 로고
    • The Pseudomonas fluorescens lipase has a C-terminal secretion signal and is secreted by a three-component bacterial ABC-exporter system
    • Duong, F., C. Soscia, A. Lazdunski, and M. Murgier. 1994. The Pseudomonas fluorescens lipase has a C-terminal secretion signal and is secreted by a three-component bacterial ABC-exporter system. Mol. Microbiol. 11:1117-1126.
    • (1994) Mol. Microbiol. , vol.11 , pp. 1117-1126
    • Duong, F.1    Soscia, C.2    Lazdunski, A.3    Murgier, M.4
  • 22
    • 0029897998 scopus 로고    scopus 로고
    • Generation of Campylobacter fetus S-layer protein diversity utilizes a single promoter on an invertible DNA segment
    • Dworkin, J., and M. J. Blaser. 1996. Generation of Campylobacter fetus S-layer protein diversity utilizes a single promoter on an invertible DNA segment. Mol. Microbiol. 19:1241-1253.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1241-1253
    • Dworkin, J.1    Blaser, M.J.2
  • 23
    • 0030700288 scopus 로고    scopus 로고
    • Molecular mechanisms of Campylobacter fetus surface layer protein expression
    • Dworkin, J., and M. J. Blaser. 1997. Molecular mechanisms of Campylobacter fetus surface layer protein expression. Mol. Microbiol. 26:433-440.
    • (1997) Mol. Microbiol. , vol.26 , pp. 433-440
    • Dworkin, J.1    Blaser, M.J.2
  • 24
    • 0031028714 scopus 로고    scopus 로고
    • Nested DNA inversion as a paradigm of programmed gene rearrangement
    • Dworkin, J., and M. J. Blaser. 1997. Nested DNA inversion as a paradigm of programmed gene rearrangement. Proc. Natl. Acad. Sci. USA 94:985-990.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 985-990
    • Dworkin, J.1    Blaser, M.J.2
  • 25
    • 0030711639 scopus 로고    scopus 로고
    • Nested DNA inversion of Campylobacter fetus S-layer genes is recA dependent
    • Dworkin, J., O. L. Shedd, and M. J. Blaser. 1997. Nested DNA inversion of Campylobacter fetus S-layer genes is recA dependent. J. Bacteriol. 179:7523-7529.
    • (1997) J. Bacteriol. , vol.179 , pp. 7523-7529
    • Dworkin, J.1    Shedd, O.L.2    Blaser, M.J.3
  • 26
    • 0028946548 scopus 로고
    • A lipopolysaccharide-binding domain of the Campylobacter fetus S-layer protein resides within the conserved N terminus of a family of silent and divergent homologs
    • Dworkin, J., M. K. R. Tummuru, and M. J. Blaser. 1995. A lipopolysaccharide-binding domain of the Campylobacter fetus S-layer protein resides within the conserved N terminus of a family of silent and divergent homologs. J. Bacteriol. 177:1734-1741.
    • (1995) J. Bacteriol. , vol.177 , pp. 1734-1741
    • Dworkin, J.1    Tummuru, M.K.R.2    Blaser, M.J.3
  • 27
    • 0029030845 scopus 로고
    • Segmental conservation of sapA sequences in type B Campylobacter fetus cells
    • Dworkin, J., M. K. R. Tummuru, and M. J. Blaser. 1995. Segmental conservation of sapA sequences in type B Campylobacter fetus cells. J. Biol. Chem. 270:15093-15101.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15093-15101
    • Dworkin, J.1    Tummuru, M.K.R.2    Blaser, M.J.3
  • 28
    • 0022254465 scopus 로고
    • Escherichia coli hemolysin is released extracellularly without cleavage of a signal peptide
    • Felmlee, T., S. Pellett, E.-Y. Lee, and R. A. Welch. 1985. Escherichia coli hemolysin is released extracellularly without cleavage of a signal peptide. J. Bacteriol. 163:88-93.
    • (1985) J. Bacteriol. , vol.163 , pp. 88-93
    • Felmlee, T.1    Pellett, S.2    Lee, E.-Y.3    Welch, R.A.4
  • 29
    • 0030889859 scopus 로고    scopus 로고
    • Surface proteins and a novel transcription factor regulate the expression of the S-layer gene in Thermus thermophilus HB8
    • Fernandez-Herrero, L. A., G. Olabarria, and J. Berenguer. 1997. Surface proteins and a novel transcription factor regulate the expression of the S-layer gene in Thermus thermophilus HB8. Mol. Microbiol. 24:61-72.
    • (1997) Mol. Microbiol. , vol.24 , pp. 61-72
    • Fernandez-Herrero, L.A.1    Olabarria, G.2    Berenguer, J.3
  • 30
    • 0031814273 scopus 로고    scopus 로고
    • Heterogeneity in levels of vacuolating cytotoxin gene (vacA) transcription among Helicobacter pylori strains
    • Forsyth, M. H., J. C. Atherton, M. J. Blaser, and T. L. Cover. 1998. Heterogeneity in levels of vacuolating cytotoxin gene (vacA) transcription among Helicobacter pylori strains. Infect. Immun. 66:3088-3094.
    • (1998) Infect. Immun. , vol.66 , pp. 3088-3094
    • Forsyth, M.H.1    Atherton, J.C.2    Blaser, M.J.3    Cover, T.L.4
  • 31
    • 0029615383 scopus 로고
    • Southern blotting analyses of strains of Campylobacter fetus using the conserved region of sapA
    • Fujita, M., T. Morooka, S. Fujimoto, T. Morija, and K. Amako. 1995. Southern blotting analyses of strains of Campylobacter fetus using the conserved region of sapA. Arch. Microbiol. 164:444-447.
    • (1995) Arch. Microbiol. , vol.164 , pp. 444-447
    • Fujita, M.1    Morooka, T.2    Fujimoto, S.3    Morija, T.4    Amako, K.5
  • 32
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., D. J. Osguthorpe, and B. Robson. 1978. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 33
    • 0345384691 scopus 로고
    • A carboxy-terminal four amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway
    • Ghigo, J. M., and C. Wandersman. 1994. A carboxy-terminal four amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway. J. Biol. Chem. 269:1-7.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-7
    • Ghigo, J.M.1    Wandersman, C.2
  • 34
    • 0025134451 scopus 로고
    • Genetic analysis of an MDR-like export system: The secretion of colicin V
    • Gilson, L., H. K. Mahanty, and R. Kolter. 1990. Genetic analysis of an MDR-like export system: the secretion of colicin V. EMBO J. 9:3875-3884.
    • (1990) EMBO J. , vol.9 , pp. 3875-3884
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 35
    • 0018219870 scopus 로고
    • Campylobacteriosis in man: Pathogenic mechanisms and review of 91 bloodstream infections
    • Guerrant, R. L., R. G. Lahita, W. C. Winn, and R. B. Roberts. 1978. Campylobacteriosis in man: pathogenic mechanisms and review of 91 bloodstream infections. Am. J. Med. 65:584-592.
    • (1978) Am. J. Med. , vol.65 , pp. 584-592
    • Guerrant, R.L.1    Lahita, R.G.2    Winn, W.C.3    Roberts, R.B.4
  • 36
    • 0026009410 scopus 로고
    • Pseudomonas aeruginosa alkaline protease: Evidence for secretion genes and study of secretion mechanism
    • Guzzo, J., J.-M. Pages, F. Duong, A. Lazdunski, and M. Murgier. 1991. Pseudomonas aeruginosa alkaline protease: evidence for secretion genes and study of secretion mechanism. J. Bacteriol. 173:5290-5297.
    • (1991) J. Bacteriol. , vol.173 , pp. 5290-5297
    • Guzzo, J.1    Pages, J.-M.2    Duong, F.3    Lazdunski, A.4    Murgier, M.5
  • 37
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557
    • Hanahan, D.1
  • 38
    • 0031780199 scopus 로고    scopus 로고
    • Serratia marcescens S-layer protein is secreted extracellularly via an ATP-binding cassette exporter, the Lip system
    • Kawai, E., H. Akatsuka, A. Idei, T. Shibatani, and K. Omori. 1998. Serratia marcescens S-layer protein is secreted extracellularly via an ATP-binding cassette exporter, the Lip system. Mol. Microbiol. 27:941-952.
    • (1998) Mol. Microbiol. , vol.27 , pp. 941-952
    • Kawai, E.1    Akatsuka, H.2    Idei, A.3    Shibatani, T.4    Omori, K.5
  • 39
    • 0026683501 scopus 로고
    • Identification of individual amino acids required for secretion within the haemolysin (HlyA) C-terminal targeting region
    • Kenny, B., S. Taylor, and I. B. Holland. 1992. Identification of individual amino acids required for secretion within the haemolysin (HlyA) C-terminal targeting region. Mol. Microbiol. 6:1477-1489.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1477-1489
    • Kenny, B.1    Taylor, S.2    Holland, I.B.3
  • 40
    • 0028915106 scopus 로고
    • Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB
    • Koronakis, E., C. Hughes, I. Milislav, and V. Koronakis. 1995. Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB. Mol. Microbiol. 16:87-96.
    • (1995) Mol. Microbiol. , vol.16 , pp. 87-96
    • Koronakis, E.1    Hughes, C.2    Milislav, I.3    Koronakis, V.4
  • 41
    • 0029744875 scopus 로고    scopus 로고
    • Synthesis, maturation and export of the E. coli hemolysin
    • Koronakis, V., and C. Hughes. 1996. Synthesis, maturation and export of the E. coli hemolysin. Med. Microbiol. Immunol. 185:65-71.
    • (1996) Med. Microbiol. Immunol. , vol.185 , pp. 65-71
    • Koronakis, V.1    Hughes, C.2
  • 42
    • 0031014882 scopus 로고    scopus 로고
    • Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals
    • Koronakis, V., J. Li, E. Koronakis, and K. Stauffer. 1997. Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals. Mol. Microbiol. 23:617-626.
    • (1997) Mol. Microbiol. , vol.23 , pp. 617-626
    • Koronakis, V.1    Li, J.2    Koronakis, E.3    Stauffer, K.4
  • 43
    • 0025979283 scopus 로고
    • Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity
    • Labigne, A., V. Cussac, and P. Courcoux. 1991. Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity. J. Bacteriol. 173:1920-1931.
    • (1991) J. Bacteriol. , vol.173 , pp. 1920-1931
    • Labigne, A.1    Cussac, V.2    Courcoux, P.3
  • 44
    • 0023917709 scopus 로고
    • Gene disruption and replacement as a feasible approach for mutagenesis of Campylobacter jejuni
    • Labigne-Roussel, A., P. Courcoux, and L. Tompkins. 1988. Gene disruption and replacement as a feasible approach for mutagenesis of Campylobacter jejuni. J. Bacteriol. 170:1704-1708.
    • (1988) J. Bacteriol. , vol.170 , pp. 1704-1708
    • Labigne-Roussel, A.1    Courcoux, P.2    Tompkins, L.3
  • 45
    • 0025825577 scopus 로고
    • Cloning and expression in Escherichia coli of the Serratia marcescens metalloprotease gene: Secretion of the protease from E. coli in the presence of the Erwinia chrysanthemi protease secretion functions
    • Létoffé, S., P. Delepelaire, and C. Wandersman. 1991. Cloning and expression in Escherichia coli of the Serratia marcescens metalloprotease gene: secretion of the protease from E. coli in the presence of the Erwinia chrysanthemi protease secretion functions. J. Bacteriol. 173:2160-2166.
    • (1991) J. Bacteriol. , vol.173 , pp. 2160-2166
    • Létoffé, S.1    Delepelaire, P.2    Wandersman, C.3
  • 46
    • 0029908021 scopus 로고    scopus 로고
    • Protein secretion in Gram-negative bacteria: Assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding
    • Létoffé, S., P. Delepelaire, and C. Wandersman. 1996. Protein secretion in Gram-negative bacteria: assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding. EMBO J. 15:5804-5811.
    • (1996) EMBO J. , vol.15 , pp. 5804-5811
    • Létoffé, S.1    Delepelaire, P.2    Wandersman, C.3
  • 47
    • 0026780472 scopus 로고
    • Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: Involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B
    • étoffé, S., and C. Wandersman. 1992. Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B. J. Bacteriol. 174: 4920-4927.
    • (1992) J. Bacteriol. , vol.174 , pp. 4920-4927
    • Étoffé, S.1    Wandersman, C.2
  • 48
    • 0016651969 scopus 로고
    • Superficial antigens of Campylobacter (Vibrio) fetus: Characterization of an antiphagocytic component
    • McCoy, E. C., D. Doyle, K. Burda, L. B. Corbeil, and A. J. Winter. 1975. Superficial antigens of Campylobacter (Vibrio) fetus: characterization of an antiphagocytic component. Infect. Immun. 11:517-525.
    • (1975) Infect. Immun. , vol.11 , pp. 517-525
    • McCoy, E.C.1    Doyle, D.2    Burda, K.3    Corbeil, L.B.4    Winter, A.J.5
  • 49
    • 0025275445 scopus 로고
    • Pathogenesis of Campylobacter fetus infections: Role of surface array proteins in virulence in a mouse model
    • Pei, Z., and M. J. Blaser. 1990. Pathogenesis of Campylobacter fetus infections: role of surface array proteins in virulence in a mouse model. J. Clin. Invest. 85:1036-1043.
    • (1990) J. Clin. Invest. , vol.85 , pp. 1036-1043
    • Pei, Z.1    Blaser, M.J.2
  • 50
    • 0023915405 scopus 로고
    • Purification and characterization of a family of high molecular weight surface-array proteins from Campylobacter fetus
    • Pei, Z., R. T. I. Ellison, R. Lewis, and M. J. Blaser. 1988. Purification and characterization of a family of high molecular weight surface-array proteins from Campylobacter fetus. J. Biol. Chem. 263:6416-6420.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6416-6420
    • Pei, Z.1    Ellison, R.T.I.2    Lewis, R.3    Blaser, M.J.4
  • 51
    • 0027434697 scopus 로고
    • Membrane traffic wardens and protein secretion in gram-negative bacteria
    • Salmond, G. P. C., and P. J. Reeves. 1993. Membrane traffic wardens and protein secretion in gram-negative bacteria. Trends Biochem. Sci. 18:8-12.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 8-12
    • Salmond, G.P.C.1    Reeves, P.J.2
  • 53
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 55
    • 0017832453 scopus 로고
    • The genus Campylobacter
    • Smibert, R. M. 1978. The genus Campylobacter. Annu. Rev. Microbiol. 32: 673-709.
    • (1978) Annu. Rev. Microbiol. , vol.32 , pp. 673-709
    • Smibert, R.M.1
  • 56
    • 0026009429 scopus 로고
    • Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin
    • Stanley, P., V. Koronakis, and C. Hughes. 1991. Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin. Mol. Microbiol. 5:2391-2403.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2391-2403
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 57
    • 0026560394 scopus 로고
    • Production of active Serratia marcescens metalloprotease from Escherichia coli by α-hemolysin HlyB and HlyD
    • Suh, Y., and M. J. Benedik, 1992. Production of active Serratia marcescens metalloprotease from Escherichia coli by α-hemolysin HlyB and HlyD. J. Bacteriol. 174:2361-2366.
    • (1992) J. Bacteriol. , vol.174 , pp. 2361-2366
    • Suh, Y.1    Benedik, M.J.2
  • 59
    • 0026697670 scopus 로고
    • Characterization of the Campylobacter fetus sapA promoter: Evidence that the sapA promoter is deleted in spontaneous mutant strains
    • Tummuru, M. K. R., and M. J. Blaser. 1992. Characterization of the Campylobacter fetus sapA promoter: evidence that the sapA promoter is deleted in spontaneous mutant strains. J. Bacteriol. 174:5916-5922.
    • (1992) J. Bacteriol. , vol.174 , pp. 5916-5922
    • Tummuru, M.K.R.1    Blaser, M.J.2
  • 60
    • 0027240586 scopus 로고
    • Rearrangement of sapA homologs with conserved and variable regions in Campylobacter fetus
    • Tummuru, M. K. R., and M. J. Blaser. 1993. Rearrangement of sapA homologs with conserved and variable regions in Campylobacter fetus. Proc. Natl. Acad. Sci. USA 90:7265-7269.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7265-7269
    • Tummuru, M.K.R.1    Blaser, M.J.2
  • 61
    • 0026669327 scopus 로고
    • Secretion across the bacterial outer membrane
    • Wandersman, C. 1992. Secretion across the bacterial outer membrane. Trends Genet. 8:317-321.
    • (1992) Trends Genet. , vol.8 , pp. 317-321
    • Wandersman, C.1
  • 62
    • 0032037667 scopus 로고    scopus 로고
    • A new member of the S-layer protein family: Characterization of the crs gene from Campylobacter rectus
    • Wang, B., E. Kraig, and D. Kolodrubetz. 1998. A new member of the S-layer protein family: characterization of the crs gene from Campylobacter rectus. Infect. Immun. 66:1521-1526.
    • (1998) Infect. Immun. , vol.66 , pp. 1521-1526
    • Wang, B.1    Kraig, E.2    Kolodrubetz, D.3
  • 63
    • 0026567323 scopus 로고
    • Translational control of pyrC expression mediated by nucleotide-sensitive selection of transcriptional start sites in Escherichia coli
    • Wilson, H. R., C. D. Archer, J. Liu, and C. L. Turnbough, Jr. 1992. Translational control of pyrC expression mediated by nucleotide-sensitive selection of transcriptional start sites in Escherichia coli. J. Bacteriol. 174: 514-524.
    • (1992) J. Bacteriol. , vol.174 , pp. 514-524
    • Wilson, H.R.1    Archer, C.D.2    Liu, J.3    Turnbough Jr., C.L.4
  • 64
    • 0028285221 scopus 로고
    • C-terminal secretion signal of an Erwinia chrysanthemi protease secreted by a signal peptide-independent pathway: Proton NMR and CD conformational studies in membrane-mimetic environments
    • Wolff, N., J.-M. Ghigo, F. Delepelaire, C. Wandersman, and M. Delepierre. 1994. C-terminal secretion signal of an Erwinia chrysanthemi protease secreted by a signal peptide-independent pathway: proton NMR and CD conformational studies in membrane-mimetic environments. Biochemistry 33:6792-6801.
    • (1994) Biochemistry , vol.33 , pp. 6792-6801
    • Wolff, N.1    Ghigo, J.-M.2    Delepelaire, F.3    Wandersman, C.4    Delepierre, M.5


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