메뉴 건너뛰기




Volumn 45, Issue 2, 2006, Pages 135-151

Secretion systems of Gram-negative bacteria - Type II secretion system, the chaperone/usher, autotransporters;Mechanizmy sekrecji bakterii Gram-ujemnych - System sekrecji II typu, sekrecja w biogenezie pilusów, autotransport

Author keywords

Autotransport; Pathogenesis; Secretion; The chaperone usher secretion system; Type II secretion system

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; CHAPERONE; PROTEIN AUTOTRANSPORTER; UNCLASSIFIED DRUG;

EID: 33745940560     PISSN: 00794252     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (3)

References (100)
  • 3
    • 0034064649 scopus 로고    scopus 로고
    • The sigA gene borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation
    • Al-Hasani K., Henderson I., Sakellaris H., Rajakumar K., Grant Y., Nataro J., Robins-Browne R., Adler B.: The sigA gene borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation. Infect. Immun. 68, 2457-2463 (2000)
    • (2000) Infect. Immun. , vol.68 , pp. 2457-2463
    • Al-Hasani, K.1    Henderson, I.2    Sakellaris, H.3    Rajakumar, K.4    Grant, Y.5    Nataro, J.6    Robins-Browne, R.7    Adler, B.8
  • 4
    • 0026074555 scopus 로고
    • Nucleotide sequence and functions of mrk determinants necessary for expression of type 3 fimbriae in Klebsiella pneumoniae
    • Allen B.L., Gerlach G.F., Clegg S.: Nucleotide sequence and functions of mrk determinants necessary for expression of type 3 fimbriae in Klebsiella pneumoniae. J. Bacteriol. 173, 916-920 (1991)
    • (1991) J. Bacteriol. , vol.173 , pp. 916-920
    • Allen, B.L.1    Gerlach, G.F.2    Clegg, S.3
  • 5
    • 0030907570 scopus 로고    scopus 로고
    • Genes involved in the biogenesis and function of type-4 fimbriae in Pseudomonas aeruginosa
    • Aim R.A., Mattick J.S.: Genes involved in the biogenesis and function of type-4 fimbriae in Pseudomonas aeruginosa. Gene 192, 89-98 (1997)
    • (1997) Gene , vol.192 , pp. 89-98
    • Aim, R.A.1    Mattick, J.S.2
  • 6
    • 0029930053 scopus 로고    scopus 로고
    • Identification of a second family of high-molecular-weight adhesion proteins expressed by non-type-able Haemophilus influenzae
    • Barenkamp S.J., St. Geme III J.W.: Identification of a second family of high-molecular-weight adhesion proteins expressed by non-type-able Haemophilus influenzae. Mol. Microbiol. 19, 1215-1223 (1996)
    • (1996) Mol. Microbiol. , vol.19 , pp. 1215-1223
    • Barenkamp, S.J.1    St. Geme III, J.W.2
  • 7
    • 0037407701 scopus 로고    scopus 로고
    • Chaperone-subunit-usher interactions required for donor strand exchange during bacterial pilus assembly
    • Barnhart M.M., Sauer F.G., Pinkner J.S., Hultgren S.J.: Chaperone-Subunit-Usher Interactions Required for Donor Strand Exchange during Bacterial Pilus Assembly. J. Bacterial. 185, 2723-2730 (2003)
    • (2003) J. Bacterial. , vol.185 , pp. 2723-2730
    • Barnhart, M.M.1    Sauer, F.G.2    Pinkner, J.S.3    Hultgren, S.J.4
  • 8
    • 0028913176 scopus 로고
    • Identification and sequence analysis of lpfABCDE, a putative fimbrial operon of Salmonella typhimurium
    • Baumler A.J., Heffron F.: Identification and sequence analysis of lpfABCDE, a putative fimbrial operon of Salmonella typhimurium. J. Bacteriol. 177, 2087-2097 (1995)
    • (1995) J. Bacteriol. , vol.177 , pp. 2087-2097
    • Baumler, A.J.1    Heffron, F.2
  • 9
    • 0029166295 scopus 로고
    • SepA, the major extracellular protein of Shigella flexneri: Autonomous secretion and involvement in tissue invasion
    • Benjelloun-Touimi Z., Sansonetti P.J., Parsot C.: SepA, the major extracellular protein of Shigella flexneri: autonomous secretion and involvement in tissue invasion. Mol. Microbiol. 17, 123-135 (1995)
    • (1995) Mol. Microbiol. , vol.17 , pp. 123-135
    • Benjelloun-Touimi, Z.1    Sansonetti, P.J.2    Parsot, C.3
  • 10
    • 0024517699 scopus 로고
    • Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli
    • Benz, I., Schmidt, M.A.: Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli. Infect. Immun. 57, 1506-1511 (1989)
    • (1989) Infect. Immun. , vol.57 , pp. 1506-1511
    • Benz, I.1    Schmidt, M.A.2
  • 11
    • 0031983616 scopus 로고    scopus 로고
    • Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa
    • Bitter W., Koster M., Latijnhouwers M., De Cock H., Tommassen J.: Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa. Mol. Microbiol. 27, 209-219 (1998)
    • (1998) Mol. Microbiol. , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latijnhouwers, M.3    De Cock, H.4    Tommassen, J.5
  • 12
    • 0029786250 scopus 로고    scopus 로고
    • Expression, secretion and antigenic variation of bacterial S-layer proteins
    • Boot H.J., Pouwels P.H.: Expression, secretion and antigenic variation of bacterial S-layer proteins. Mol. Microbiol. 21, 1117-1123 (1996)
    • (1996) Mol. Microbiol. , vol.21 , pp. 1117-1123
    • Boot, H.J.1    Pouwels, P.H.2
  • 13
    • 0030917724 scopus 로고    scopus 로고
    • EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V
    • Brunder W., Schmidt H., Karch H.: EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V. Mol Microbiol. 24, 767-778 (1997)
    • (1997) Mol Microbiol. , vol.24 , pp. 767-778
    • Brunder, W.1    Schmidt, H.2    Karch, H.3
  • 14
    • 0036532450 scopus 로고    scopus 로고
    • Port of entry - The type III secretion translocon
    • Büttner D., Bonas U.: Port of entry - the type III secretion translocon. Trends Microbiol. 10, 186-192 (2002)
    • (2002) Trends Microbiol. , vol.10 , pp. 186-192
    • Büttner, D.1    Bonas, U.2
  • 15
    • 0032456560 scopus 로고    scopus 로고
    • The apeE gene of Salmonella typhimurium encodes an outer membrane esterase not present in Escherichia coli
    • Carinato M.E., Collin-Osdoby P., Yang X., Knox T.M., Conlin C.A., Miller C.G.: The apeE gene of Salmonella typhimurium encodes an outer membrane esterase not present in Escherichia coli. J. Bacteriol. 180, 3517-3521 (1998)
    • (1998) J. Bacteriol. , vol.180 , pp. 3517-3521
    • Carinato, M.E.1    Collin-Osdoby, P.2    Yang, X.3    Knox, T.M.4    Conlin, C.A.5    Miller, C.G.6
  • 16
    • 0032211618 scopus 로고    scopus 로고
    • Production of acyl-homoserine lactone quorum-sensing signals by gram-negative plant-associated bacteria
    • Cha C., Gao P., Chen Y.C., Shaw P.D., Farrand S.K.: Production of Acyl-Homoserine Lactone Quorum-Sensing Signals by Gram-Negative Plant-Associated Bacteria. Mol. Plant-Microbe Interact, 11, 1119-1129 (1998)
    • (1998) Mol. Plant-Microbe Interact , vol.11 , pp. 1119-1129
    • Cha, C.1    Gao, P.2    Chen, Y.C.3    Shaw, P.D.4    Farrand, S.K.5
  • 18
    • 0027322268 scopus 로고
    • Characterization of three fimbrial genes, sefABC, of Salmonella enteriditis
    • Clouthier S.C., Muller K.H., Doran J.L., Collinson S.K., Kay W.W.: Characterization of three fimbrial genes, sefABC, of Salmonella enteriditis. J. Bacteriol. 175, 2523-2533 (1993)
    • (1993) J. Bacteriol. , vol.175 , pp. 2523-2533
    • Clouthier, S.C.1    Muller, K.H.2    Doran, J.L.3    Collinson, S.K.4    Kay, W.W.5
  • 20
    • 0031774284 scopus 로고    scopus 로고
    • Endochitinase is transported to the extracellular milieu by the eps-encoded general secretory pathway of Vibrio cholerae
    • Connell T.D., Metzger D.J., Lynch J., Folster J.P.: Endochitinase is transported to the extracellular milieu by the eps-encoded general secretory pathway of Vibrio cholerae. J. Bacteriol. 180, 5591-5600 (1998)
    • (1998) J. Bacteriol. , vol.180 , pp. 5591-5600
    • Connell, T.D.1    Metzger, D.J.2    Lynch, J.3    Folster, J.P.4
  • 21
    • 0031665154 scopus 로고    scopus 로고
    • Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization
    • Crago A.M., Koronakis V.: Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol. Microbiol. 30, 47-56 (1998)
    • (1998) Mol. Microbiol. , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 22
    • 0028209927 scopus 로고
    • Sequence analysis of the 190-kDa antigen-encoding gene of Rickettsia conorii (Malish 7 strain)
    • Crocquet-Valdes P.A., Weiss K., Walker D.H.: Sequence analysis of the 190-kDa antigen-encoding gene of Rickettsia conorii (Malish 7 strain). Gene, 140, 115-119 (1994)
    • (1994) Gene , vol.140 , pp. 115-119
    • Crocquet-Valdes, P.A.1    Weiss, K.2    Walker, D.H.3
  • 23
    • 0023441713 scopus 로고
    • Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase
    • d'Enfert C., Ryter A., Pugsley A.P.: Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase. EMBO J. 6, 3531-3538 (1987)
    • (1987) EMBO J. , vol.6 , pp. 3531-3538
    • D'Enfert, C.1    Ryter, A.2    Pugsley, A.P.3
  • 24
    • 0030965150 scopus 로고    scopus 로고
    • The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVfl function
    • Daefler S., Guilvout I., Hardie K.R., Pugsley A.P., Russel M.: The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVfl function. Mol. Microbiol. 24, 465-475 (1997)
    • (1997) Mol. Microbiol. , vol.24 , pp. 465-475
    • Daefler, S.1    Guilvout, I.2    Hardie, K.R.3    Pugsley, A.P.4    Russel, M.5
  • 25
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type I signal peptidases
    • Dalbey R.E., Lively M.O., Bron S., Van Dijl J.M.: The chemistry and enzymology of the type I signal peptidases. Protein Sci. 6, 1129-1138 (1997)
    • (1997) Protein Sci. , vol.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    Van Dijl, J.M.4
  • 26
    • 0026453267 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes-a new protease family
    • Dalbey R.E., Von Heijne G.: Signal peptidases in prokaryotes and eukaryotes-a new protease family. Trends Biochem. Sci. 17, 474-478 (1992)
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 474-478
    • Dalbey, R.E.1    Von Heijne, G.2
  • 27
    • 0027483426 scopus 로고
    • Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes
    • Dodson K.W., Jacob-Dubuisson F., Striker R.T., Hultgren S.J.: Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes. Proc. Natl. Acad. Sci. USA, 90, 3670-3674 (1993)
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3670-3674
    • Dodson, K.W.1    Jacob-Dubuisson, F.2    Striker, R.T.3    Hultgren, S.J.4
  • 29
    • 0025943752 scopus 로고
    • Structural characterization of protein secretion genes of the bacterial phytopathogen Xanthomonas campestris pathovar campestris: Relatedness to secretion systems of other Gram-negative bacteria
    • Dums F., Dow J.M., Daniels M.J.: Structural characterization of protein secretion genes of the bacterial phytopathogen Xanthomonas campestris pathovar campestris: relatedness to secretion systems of other Gram-negative bacteria. Mol. Gen. Genet. 229, 357-364 (1991)
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 357-364
    • Dums, F.1    Dow, J.M.2    Daniels, M.J.3
  • 30
    • 0036893427 scopus 로고    scopus 로고
    • Functional Comparison of Serine Protease Autotransporters of Enterobacteriaceae
    • Dutta P.R., Capello R., Navaro-Garcia F., Nataro J.P.: Functional Comparison of Serine Protease Autotransporters of Enterobacteriaceae. Infect. Immun. 70, 7105-7113 (2002)
    • (2002) Infect. Immun. , vol.70 , pp. 7105-7113
    • Dutta, P.R.1    Capello, R.2    Navaro-Garcia, F.3    Nataro, J.P.4
  • 31
    • 0031984440 scopus 로고    scopus 로고
    • Bacterial preprotein translocase: Mechanism and conformational dynamics of a processive enzyme
    • Economou A.: Bacterial preprotein translocase: mechanism and conformational dynamics of a processive enzyme. Mol. Microbiol. 27, 511-518 (1998)
    • (1998) Mol. Microbiol. , vol.27 , pp. 511-518
    • Economou, A.1
  • 33
    • 0028019294 scopus 로고
    • Cloning and sequencing of a Bordetella pertussis serum resistance locus
    • Fernandez R.C., Weiss A.A.: Cloning and sequencing of a Bordetella pertussis serum resistance locus. Infect. Immun. 62, 4727-4738 (1994)
    • (1994) Infect. Immun. , vol.62 , pp. 4727-4738
    • Fernandez, R.C.1    Weiss, A.A.2
  • 34
    • 0031413426 scopus 로고    scopus 로고
    • Helicobacter pylori factors involved in the development of gastroduodenal mucosal damage and ulceration
    • Figura N.: Helicobacter pylori factors involved in the development of gastroduodenal mucosal damage and ulceration. J. Clin. Gastroenterol. 25, S149-S163 (1997)
    • (1997) J. Clin. Gastroenterol. , vol.25
    • Figura, N.1
  • 35
    • 0031824189 scopus 로고    scopus 로고
    • Vag 8, a Bordetella pertussis bvg regulated protein
    • Finn T.M., Amsbaugh D.F.: Vag 8, a Bordetella pertussis bvg regulated protein. Infect. Immun. 66, 3985-3989 (1998)
    • (1998) Infect. Immun. , vol.66 , pp. 3985-3989
    • Finn, T.M.1    Amsbaugh, D.F.2
  • 36
    • 0029056781 scopus 로고
    • Tracheal colonization factor: A Bordetella pertussis secreted virulence determinant
    • Finn T.M., Stevens L.A.: Tracheal colonization factor: a Bordetella pertussis secreted virulence determinant. Mol. Microbiol. 16, 625-634 (1995)
    • (1995) Mol. Microbiol. , vol.16 , pp. 625-634
    • Finn, T.M.1    Stevens, L.A.2
  • 37
    • 0027157765 scopus 로고
    • Nucleotide sequence of a 13.9 kb segment of the 90 kb virulence plasmid of Salmonella typhimurium: The presence of a fimbrial biosynthetic gene
    • Friedich M.J., Kinsey N.E., Vila J., Kadner R.J.: Nucleotide sequence of a 13.9 kb segment of the 90 kb virulence plasmid of Salmonella typhimurium: the presence of a fimbrial biosynthetic gene. Mol. Microbiol. 8, 543-558 (1993)
    • (1993) Mol. Microbiol. , vol.8 , pp. 543-558
    • Friedich, M.J.1    Kinsey, N.E.2    Vila, J.3    Kadner, R.J.4
  • 38
    • 0025912385 scopus 로고
    • Expression of the envelope antigen F1 of Yersinia pestis is mediated by the product of cal 1M gene having homology with the chaperone protein PapD of Escherichia coli
    • Galyov E.E., Karlishev A.V., Chernovskaya T.V., Dolgikh D.A., Smirnov O.Y., Volkovoy K.I., Abramov V.M., Zav*yalov V.P.: Expression of the envelope antigen F1 of Yersinia pestis is mediated by the product of cal 1M gene having homology with the chaperone protein PapD of Escherichia coli. FEBS Lett. 286, 79-82 (1991)
    • (1991) FEBS Lett. , vol.286 , pp. 79-82
    • Galyov, E.E.1    Karlishev, A.V.2    Chernovskaya, T.V.3    Dolgikh, D.A.4    Smirnov, O.Y.5    Volkovoy, K.I.6    Abramov, V.M.7    Zavyalov, V.P.8
  • 39
    • 0028149058 scopus 로고
    • Nucleotide sequence of the afimbrial adhesin encoding afa-3 gene cluster and its translocation via flanking IS1 insertion sequences
    • Garcia M.I., Labigne A., LeBouguenec C.: Nucleotide sequence of the afimbrial adhesin encoding afa-3 gene cluster and its translocation via flanking IS1 insertion sequences. J. Bacteriol. 176, 7601-7613 (1994)
    • (1994) J. Bacteriol. , vol.176 , pp. 7601-7613
    • Garcia, M.I.1    Labigne, A.2    Lebouguenec, C.3
  • 40
    • 0025157866 scopus 로고
    • Characterization of the 120-kDa surface protein gene of Rickettsia rickettsii (R strain)
    • Gilmore R.D., Jr.: Characterization of the 120-kDa surface protein gene of Rickettsia rickettsii (R strain). Ann. N.Y. Acad. Sci. 590, 459-467 (1990)
    • (1990) Ann. N.Y. Acad. Sci. , vol.590 , pp. 459-467
    • Gilmore Jr., R.D.1
  • 41
    • 0023809580 scopus 로고
    • CS31A, a new K88-related fimbrial antigen on bovine enteropathogenic and septicemic Escherichia coli strains
    • Girdeau J.P., Vartanian M.D., Ollier J.L., Contrepois M.: CS31A, a new K88-related fimbrial antigen on bovine enteropathogenic and septicemic Escherichia coli strains. Infect. Immun. 56, 2180-2188 (1988)
    • (1988) Infect. Immun. , vol.56 , pp. 2180-2188
    • Girdeau, J.P.1    Vartanian, M.D.2    Ollier, J.L.3    Contrepois, M.4
  • 42
    • 0027430730 scopus 로고
    • Shigella subversion of the cellular cytoskeleton: A strategy for epithelial colonization
    • Goldberg M.B., Sansonetti P.J.: Shigella subversion of the cellular cytoskeleton: a strategy for epithelial colonization. Infect. Immun. 61, 4941-4946 (1993)
    • (1993) Infect. Immun. , vol.61 , pp. 4941-4946
    • Goldberg, M.B.1    Sansonetti, P.J.2
  • 43
    • 0028922083 scopus 로고
    • Pasteurella haemolytica serotype 2 contains the gene for a non-capsular serotype 1-specific antigen
    • Gonzalez C.T., Maheswaran S.K., Murtaugh M.P.: Pasteurella haemolytica serotype 2 contains the gene for a non-capsular serotype 1-specific antigen. Infect. Immun. 63, 1340-1348 (1995)
    • (1995) Infect. Immun. , vol.63 , pp. 1340-1348
    • Gonzalez, C.T.1    Maheswaran, S.K.2    Murtaugh, M.P.3
  • 45
    • 0033810425 scopus 로고    scopus 로고
    • Identification of SAT, an autotransporter toxin produced by uropathogenic Escherichia coli
    • Guyer D.M., Henderson I.R., Nataro J.P., Mobley H.L. Identification of SAT, an autotransporter toxin produced by uropathogenic Escherichia coli. Mol. Microbiol. 38, 53-66 (2000)
    • (2000) Mol. Microbiol. , vol.38 , pp. 53-66
    • Guyer, D.M.1    Henderson, I.R.2    Nataro, J.P.3    Mobley, H.L.4
  • 46
    • 0031796439 scopus 로고    scopus 로고
    • Evaluation of immunoglobulin A1 (IgAl) protease and IgA1 protease-inhibitory activity in human female genital infection with Neisseria gonorrhoeae
    • Hedges S.R., Mayo M.S., Kallman L., Mestecky J., Hook III E.W., Russell M.W.: Evaluation of immunoglobulin A1 (IgAl) protease and IgA1 protease-inhibitory activity in human female genital infection with Neisseria gonorrhoeae. Infect. Immun. 66, 5826-5832 (1998)
    • (1998) Infect. Immun. , vol.66 , pp. 5826-5832
    • Hedges, S.R.1    Mayo, M.S.2    Kallman, L.3    Mestecky, J.4    Hook III, E.W.5    Russell, M.W.6
  • 47
    • 0032940207 scopus 로고    scopus 로고
    • The major phase-variable outer membrane protein of Escherichia coli structurally resembles the immunoglobulinA1 protease class of exported protein and is regulated by a novel mechanism involving Dam and OxyR
    • Henderson I.R., Owen P.: The major phase-variable outer membrane protein of Escherichia coli structurally resembles the immunoglobulinA1 protease class of exported protein and is regulated by a novel mechanism involving Dam and OxyR. J. Bacteriol. 181, 2132-2141 (1999)
    • (1999) J. Bacteriol. , vol.181 , pp. 2132-2141
    • Henderson, I.R.1    Owen, P.2
  • 48
    • 0032734808 scopus 로고    scopus 로고
    • Characterization of Pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli
    • Henderson I.R., Czeczulin J., Eslava C., Noriega F., Nataro J.P.: Characterization of Pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli. Infect. Immun. 67, 5587-5596 (1999)
    • (1999) Infect. Immun. , vol.67 , pp. 5587-5596
    • Henderson, I.R.1    Czeczulin, J.2    Eslava, C.3    Noriega, F.4    Nataro, J.P.5
  • 49
    • 0034541135 scopus 로고    scopus 로고
    • Autotransporter proteins, evolution and redefining protein secretion
    • Henderson I.R., Capello R., Nataro J.P.: Autotransporter proteins, evolution and redefining protein secretion. Trends Microbiol. 8, 529-532 (2000)
    • (2000) Trends Microbiol. , vol.8 , pp. 529-532
    • Henderson, I.R.1    Capello, R.2    Nataro, J.P.3
  • 50
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson I.R., Nataro J.P.: Virulence Functions of Autotransporter Proteins. Infect. Immun. 69, 1231-1243 (2001)
    • (2001) Infect. Immun. , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 51
    • 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., Mattick J.S., 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. Mol. Microbiol. 10, 233-243 (1993)
    • (1993) Mol. Microbiol. , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 52
    • 0021357060 scopus 로고
    • Frequency of gene sequences necessary for pyelonephritis-associated pili expression among isolates of Enterobacteriaceae from human extraintestinal infections
    • Hull R.A., Hull S.I., Falkow S.: Frequency of gene sequences necessary for pyelonephritis-associated pili expression among isolates of Enterobacteriaceae from human extraintestinal infections. Infect. Immun. 43, 1064-1067 (1984)
    • (1984) Infect. Immun. , vol.43 , pp. 1064-1067
    • Hull, R.A.1    Hull, S.I.2    Falkow, S.3
  • 55
    • 0027528505 scopus 로고
    • Initiation of assembly and association of the structural elements of a bacterial pilus depend on two specialized tip proteins
    • Jacob-Dubuisson F., Heuser J., Dodson K., Normark S., Hultgren S.: Initiation of assembly and association of the structural elements of a bacterial pilus depend on two specialized tip proteins. EMBO J. 12, 837-847 (1993)
    • (1993) EMBO J. , vol.12 , pp. 837-847
    • Jacob-Dubuisson, F.1    Heuser, J.2    Dodson, K.3    Normark, S.4    Hultgren, S.5
  • 56
    • 0035035580 scopus 로고    scopus 로고
    • Two-partner secretion in Gram-negative bacteria: A trifty, specific pathway for large virulence proteins
    • Jacob-Dubuisson F., Locht C., Antoine R.: Two-partner secretion in Gram-negative bacteria: a trifty, specific pathway for large virulence proteins. Mol. Microbiol. 40, 306-313 (2001)
    • (2001) Mol. Microbiol. , vol.40 , pp. 306-313
    • Jacob-Dubuisson, F.1    Locht, C.2    Antoine, R.3
  • 57
    • 0024850733 scopus 로고
    • Genes for biosynthesis and assembly of CS3 pili of CFA/II enterotoxigenic Escherichia coli: Novel regulation of pilus production by bypassing an amber codon
    • Jalajakumari M.B., Thomas C.J., Halter R., Manning P.A.: Genes for biosynthesis and assembly of CS3 pili of CFA/II enterotoxigenic Escherichia coli: novel regulation of pilus production by bypassing an amber codon. Mol. Microbiol. 3, 1685-1695 (1989)
    • (1989) Mol. Microbiol. , vol.3 , pp. 1685-1695
    • Jalajakumari, M.B.1    Thomas, C.J.2    Halter, R.3    Manning, P.A.4
  • 59
    • 0027167643 scopus 로고
    • The lux autoinducer regulates the production of exoenzyme virulence determinants in Erwinia carotovora and Pseudomonas aeruginosa
    • Jones S., Yu B., Bainton N.J., Birdsall M., Bycroft B., Chhabra S.R., Cox A.J., Golby P., Reeves P.J., Stephens S.: The lux autoinducer regulates the production of exoenzyme virulence determinants in Erwinia carotovora and Pseudomonas aeruginosa. EMBO J. 12, 2477-2482 (1993)
    • (1993) EMBO J. , vol.12 , pp. 2477-2482
    • Jones, S.1    Yu, B.2    Bainton, N.J.3    Birdsall, M.4    Bycroft, B.5    Chhabra, S.R.6    Cox, A.J.7    Golby, P.8    Reeves, P.J.9    Stephens, S.10
  • 60
    • 0032779040 scopus 로고    scopus 로고
    • The ABC-exporter genes involved in the lipase secretion are clustered with the genes for lipase, alkaline protease, and serine protease homologues in Pseudomonas fluorescens no. 33
    • Kawai E., Idei A., Kumura H., Shimazaki K., Akatsuka H., Omori K.: The ABC-exporter genes involved in the lipase secretion are clustered with the genes for lipase, alkaline protease, and serine protease homologues in Pseudomonas fluorescens no. 33. Biochim. Biophys. Acta, 1446, 377-382 (1999)
    • (1999) Biochim. Biophys. Acta , vol.1446 , pp. 377-382
    • Kawai, E.1    Idei, A.2    Kumura, H.3    Shimazaki, K.4    Akatsuka, H.5    Omori, K.6
  • 61
    • 0024415192 scopus 로고
    • Adhesin and ultrastructural properties of human enterotoxigenic Escherichia coli producing colonization factor antigens III and IV
    • Knutton S., McConnel M.M., Rowe B., McNeish A.S.: Adhesin and ultrastructural properties of human enterotoxigenic Escherichia coli producing colonization factor antigens III and IV. Infect. Immun. 57, 3364-3371 (1989)
    • (1989) Infect. Immun. , vol.57 , pp. 3364-3371
    • Knutton, S.1    McConnel, M.M.2    Rowe, B.3    McNeish, A.S.4
  • 62
    • 0030716279 scopus 로고    scopus 로고
    • The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex
    • Koster M., Bitter W., de Cock H., Allaoui A., Cornelis G.R., Tommassen, J.: The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol. Microbiol. 26, 789-797 (1997)
    • (1997) Mol. Microbiol. , vol.26 , pp. 789-797
    • Koster, M.1    Bitter, W.2    De Cock, H.3    Allaoui, A.4    Cornelis, G.R.5    Tommassen, J.6
  • 63
    • 0025310329 scopus 로고
    • Direct evidence that the FimH protein is the mannose-specific adhesin of Escherichia coli type 1 fimbriae
    • Krogfelt K.A., Bergmans H., Klemm P.: Direct evidence that the FimH protein is the mannose-specific adhesin of Escherichia coli type 1 fimbriae. Infect. Immun. 58, 1995-1998 (1990)
    • (1990) Infect. Immun. , vol.58 , pp. 1995-1998
    • Krogfelt, K.A.1    Bergmans, H.2    Klemm, P.3
  • 64
    • 0026564086 scopus 로고
    • Analysis of eight out genes in a cluster required for pectic enzyme secretion by Erwinia chrysanthemi: Sequence comparison with secretion genes from other gram-negative bacteria
    • Lindeberg M., Collmer A.: Analysis of eight out genes in a cluster required for pectic enzyme secretion by Erwinia chrysanthemi: sequence comparison with secretion genes from other gram-negative bacteria. J. Bacteriol. 174, 7385-7397 (1992)
    • (1992) J. Bacteriol. , vol.174 , pp. 7385-7397
    • Lindeberg, M.1    Collmer, A.2
  • 65
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal C., Elsinghorst E.A.: Identification of a glycoprotein produced by enterotoxigenic Escherichia coli. Infect. Immun. 67, 4084-4091 (1999)
    • (1999) Infect. Immun. , vol.67 , pp. 4084-4091
    • Lindenthal, C.1    Elsinghorst, E.A.2
  • 66
    • 1842293999 scopus 로고    scopus 로고
    • The filamentous phage pIV multimer visualized by scanning transmission electron microscopy
    • Linderoth N.A., Simon M.N., Russel M.: The filamentous phage pIV multimer visualized by scanning transmission electron microscopy. Science, 278, 1635-1638 (1997)
    • (1997) Science , vol.278 , pp. 1635-1638
    • Linderoth, N.A.1    Simon, M.N.2    Russel, M.3
  • 67
    • 0027152069 scopus 로고
    • Yersinia pestis pH 6 antigen forms fimbriae and is induced by intracellular association with macrophages
    • Lindler L.E., Tall B.D.: Yersinia pestis pH 6 antigen forms fimbriae and is induced by intracellular association with macrophages. Mol. Microbiol. 8, 311-324 (1993)
    • (1993) Mol. Microbiol. , vol.8 , pp. 311-324
    • Lindler, L.E.1    Tall, B.D.2
  • 69
    • 0026706341 scopus 로고
    • Common accessory genes for the Bordetella pertussis filamentous hemagglutinin and fimbriae share sequence similarities with the papC and papD gene families
    • Locht C., Geoffroy M.C., Renauld G.: Common accessory genes for the Bordetella pertussis filamentous hemagglutinin and fimbriae share sequence similarities with the papC and papD gene families. EMBO J. 11, 3175-3183 (1992)
    • (1992) EMBO J. , vol.11 , pp. 3175-3183
    • Locht, C.1    Geoffroy, M.C.2    Renauld, G.3
  • 70
    • 0023975224 scopus 로고
    • Uropathogenic Escherichia coli can express serologically identical pili of different receptor binding specificities
    • Lund B., Marklund B.I., Stromberg N., Lindberg F., Karlsson K.A., Normark S.: Uropathogenic Escherichia coli can express serologically identical pili of different receptor binding specificities. Mol. Microbiol. 2, 255-263 (1988)
    • (1988) Mol. Microbiol. , vol.2 , pp. 255-263
    • Lund, B.1    Marklund, B.I.2    Stromberg, N.3    Lindberg, F.4    Karlsson, K.A.5    Normark, S.6
  • 71
    • 0033612142 scopus 로고    scopus 로고
    • An aqueous channel for filamentous phage export
    • Marciano D.K., Russel M., Simon S.M.: An aqueous channel for filamentous phage export. Science, 284, 1516-1519 (1998)
    • (1998) Science , vol.284 , pp. 1516-1519
    • Marciano, D.K.1    Russel, M.2    Simon, S.M.3
  • 72
    • 0022365856 scopus 로고    scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • Michaelis S., Chapon C., D'Enfert C., Pugsley A.P., Schwartz M.: Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae J. Bacteriol. 164, 633-638.
    • J. Bacteriol. , vol.164 , pp. 633-638
    • Michaelis, S.1    Chapon, C.2    D'Enfert, C.3    Pugsley, A.P.4    Schwartz, M.5
  • 73
    • 0004969979 scopus 로고
    • Isolation and characterization of the α-sialyl-β-2,3- galactosyl-specific adhesin from fimbriated Escherichia coli
    • Moch T., Hoschutzky H., Hacker J., Kroncke K.D., Jann K.: Isolation and characterization of the α-sialyl-β-2,3-galactosyl-specific adhesin from fimbriated Escherichia coli. Proc. Natl. Acad. Sci. USA, 84, 3462-3466 (1987)
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3462-3466
    • Moch, T.1    Hoschutzky, H.2    Hacker, J.3    Kroncke, K.D.4    Jann, K.5
  • 74
    • 0030928054 scopus 로고    scopus 로고
    • The synthesis, secretion and role in virulence of the paracrystalline surface protein layers of Aeromonas salmonicida and A. hydrophila
    • Noonan B., Trust T.J.: The synthesis, secretion and role in virulence of the paracrystalline surface protein layers of Aeromonas salmonicida and A. hydrophila. FEMS Microbiol. Lett. 154, 1-7 (1997)
    • (1997) FEMS Microbiol. Lett. , vol.154 , pp. 1-7
    • Noonan, B.1    Trust, T.J.2
  • 75
    • 0033214349 scopus 로고    scopus 로고
    • Bacterial Type II protein export and pilus biogenesis: More than just homologies?
    • Nunn D.: Bacterial Type II protein export and pilus biogenesis: more than just homologies? Trends Cell Biol. 9, 402-408 (1999)
    • (1999) Trends Cell Biol. , vol.9 , pp. 402-408
    • Nunn, D.1
  • 76
    • 0030955804 scopus 로고    scopus 로고
    • Two genes encoding serine protease homologues in Serratia marcescens and characterization of their products in Escherichia coli
    • Ohnishi Y., Beppu T., Horinouchi S.: Two genes encoding serine protease homologues in Serratia marcescens and characterization of their products in Escherichia coli. J. Biochem. (Tokyo), 121, 902-913 (1997)
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 902-913
    • Ohnishi, Y.1    Beppu, T.2    Horinouchi, S.3
  • 77
    • 0032555939 scopus 로고    scopus 로고
    • Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1
    • Otto B.R., van Dooren S.J.M., Nuijens J.H., Luirink J., Oudega B.: Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1. J. Exp. Med. 188, 1091-1103 (1998)
    • (1998) J. Exp. Med. , vol.188 , pp. 1091-1103
    • Otto, B.R.1    Van Dooren, S.J.M.2    Nuijens, J.H.3    Luirink, J.4    Oudega, B.5
  • 78
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner J., Halter R., Beyreuther K., Meyer T.F.: Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature, 325, 458-462 (1987)
    • (1987) Nature , vol.325 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 79
    • 0344915159 scopus 로고    scopus 로고
    • Membrane association and multimerization of secreton component PulC
    • Possot O.M., Gerard-Vincent M., Pugsley A.P.: Membrane association and multimerization of secreton component PulC. J. Bacteriol. 181, 4004-4011 (1999)
    • (1999) J. Bacteriol. , vol.181 , pp. 4004-4011
    • Possot, O.M.1    Gerard-Vincent, M.2    Pugsley, A.P.3
  • 80
    • 0030920684 scopus 로고    scopus 로고
    • The conserved tetracysteine motif in the general secretory pathway component PulE is required for efficient pullulanase secretion
    • Possot O.M., Pugsley A.P.: The conserved tetracysteine motif in the general secretory pathway component PulE is required for efficient pullulanase secretion. Gene, 192, 45-50 (1997)
    • (1997) Gene , vol.192 , pp. 45-50
    • Possot, O.M.1    Pugsley, A.P.2
  • 81
    • 0024417495 scopus 로고
    • Cloning and sequencing of the immunoglobulin A1 protease gene (iga) of Haemophilus influenzae serotype
    • Poulsen K., Brandt J., Hjorth J.P., Thogersen H.C., Kilian M.: Cloning and sequencing of the immunoglobulin A1 protease gene (iga) of Haemophilus influenzae serotype b. Infect. Immun. 57, 3097-3105 (1989)
    • (1989) Infect. Immun. , vol.57 , pp. 3097-3105
    • Poulsen, K.1    Brandt, J.2    Hjorth, J.P.3    Thogersen, H.C.4    Kilian, M.5
  • 82
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley A.P.: The complete general secretory pathway in Gram-negative bacteria. Microbiol. Rev. 57, 50-108 (1993)
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 83
    • 0029855069 scopus 로고    scopus 로고
    • Duplication of pilus gene complexes of Haemophilus influenzae biogroup aegyptius
    • Read T.D., Dowdell M., Satola S.W., Farley M.M.: Duplication of pilus gene complexes of Haemophilus influenzae biogroup aegyptius. J. Bacteriol. 178, 6564-6570 (1996)
    • (1996) J. Bacteriol. , vol.178 , pp. 6564-6570
    • Read, T.D.1    Dowdell, M.2    Satola, S.W.3    Farley, M.M.4
  • 85
    • 0027293725 scopus 로고
    • Analysis of the structure and subcellular location of filamentous phage pIV
    • Russel M., Kazmierczak B.: Analysis of the structure and subcellular location of filamentous phage pIV. J. Bacteriol. 175, 3998-4007 (1993)
    • (1993) J. Bacteriol. , vol.175 , pp. 3998-4007
    • Russel, M.1    Kazmierczak, B.2
  • 86
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: Type II protein secretion systems
    • Russel M.: Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J. Mol. Biol. 279, 485-499 (1998)
    • (1998) J. Mol. Biol. , vol.279 , pp. 485-499
    • Russel, M.1
  • 88
    • 0035029580 scopus 로고    scopus 로고
    • Biology of type II secretion
    • Sandkvist M.: Biology of type II secretion. Mol. Microbiol. 40, 271-283 (2001)
    • (2001) Mol. Microbiol. , vol.40 , pp. 271-283
    • Sandkvist, M.1
  • 89
    • 0035019730 scopus 로고    scopus 로고
    • Type II secretion and pathogenesis
    • Sandkvist M.: Type II Secretion and Pathogenesis. Infect. Immun. 69, 3523-3535 (2001)
    • (2001) Infect. Immun. , vol.69 , pp. 3523-3535
    • Sandkvist, M.1
  • 90
    • 0029027629 scopus 로고
    • Bacterial prolipoprotein signal peptidase
    • Sankaran K., Wu H.C.: Bacterial prolipoprotein signal peptidase. Methods Enzymol. 248, 169-180 (1995)
    • (1995) Methods Enzymol. , vol.248 , pp. 169-180
    • Sankaran, K.1    Wu, H.C.2
  • 91
    • 0032522714 scopus 로고    scopus 로고
    • Ramifications of kinetic partitioning on usher-mediated pilus biogenesis
    • Saulino E.T., Thanassi D.G., Pinkner J.S., Hultgren S.J.: Ramifications of kinetic partitioning on usher-mediated pilus biogenesis. EMBO J. 17, 2177-2185 (1998)
    • (1998) EMBO J. , vol.17 , pp. 2177-2185
    • Saulino, E.T.1    Thanassi, D.G.2    Pinkner, J.S.3    Hultgren, S.J.4
  • 92
    • 0027964811 scopus 로고
    • Identification and characterization of a gene cluster mediating enteroaggregative Escherichia coli aggregative adherence fimbria I biogenesis
    • Savarino S., Fox, P. Yikang, D. Nataro J.P.: Identification and characterization of a gene cluster mediating enteroaggregative Escherichia coli aggregative adherence fimbria I biogenesis. J. Bacteriol. 176, 4949-4957 (1994)
    • (1994) J. Bacteriol. , vol.176 , pp. 4949-4957
    • Savarino, S.1    Fox, P.2    Yikang, D.3    Nataro, J.P.4
  • 93
    • 0032989015 scopus 로고    scopus 로고
    • Bacterial adhesins: Common themes and variations in architecture and assembly
    • Soto G.E., Hulgren S.J.: Bacterial adhesins: common themes and variations in architecture and assembly. J. Bacterial. 181, 1059-1071 (1999)
    • (1999) J. Bacterial. , vol.181 , pp. 1059-1071
    • Soto, G.E.1    Hulgren, S.J.2
  • 94
    • 0029861822 scopus 로고    scopus 로고
    • Characterization of the genetic locus encoding Haemophilus influenzae type b surface fibrils
    • St. Geme J.W. III, Cutter D., Barenkamp S.J.: Characterization of the genetic locus encoding Haemophilus influenzae type b surface fibrils. J. Bacteriol. 178, 6281-6287 (1996)
    • (1996) J. Bacteriol. , vol.178 , pp. 6281-6287
    • St. Geme III, J.W.1    Cutter, D.2    Barenkamp, S.J.3
  • 95
    • 0027987985 scopus 로고
    • A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells
    • St. Gerne J.W. III, de la Morena M.L., Falkow S.: A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells. Mol. Microbiol. 14, 217-233 (1994)
    • (1994) Mol. Microbiol. , vol.14 , pp. 217-233
    • St. Gerne III, J.W.1    De La Morena, M.L.2    Falkow, S.3
  • 97
    • 0036842083 scopus 로고    scopus 로고
    • Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis
    • Thanassi D.G., Stathopoulos C., Dodson K., Geiger D., Hultgren S.J.: Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis. J. Bacteriol. 184, 6260-6269 (2002)
    • (2002) J. Bacteriol. , vol.184 , pp. 6260-6269
    • Thanassi, D.G.1    Stathopoulos, C.2    Dodson, K.3    Geiger, D.4    Hultgren, S.J.5
  • 99
    • 0030057090 scopus 로고    scopus 로고
    • Lysogenic conversion by a filamentous phage encoding cholera toxin
    • Waldor M.K., Mekalanos J.J.: Lysogenic conversion by a filamentous phage encoding cholera toxin. Science, 272, 1910-1914 (1996)
    • (1996) Science , vol.272 , pp. 1910-1914
    • Waldor, M.K.1    Mekalanos, J.J.2
  • 100
    • 0032721432 scopus 로고    scopus 로고
    • A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa
    • Wilhelm S., Tommassen J., Jaeger K.E.: A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa. J. Bacteriol. 181, 6977-6986 (1999)
    • (1999) J. Bacteriol. , vol.181 , pp. 6977-6986
    • Wilhelm, S.1    Tommassen, J.2    Jaeger, K.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.