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D. Faguy, Ken Jarrell, John Kuzio, M Kalmokoff (1994)
Molecular analysis of archael flagellins: similarity to the type IV pilin-transport superfamily widespread in bacteria.Canadian journal of microbiology, 40 1
M. Donnenberg, J. Kaper (1991)
Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vectorInfection and Immunity, 59
P. Whitley, G. Heijne (1993)
The DsbA‐DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domainsFEBS Letters, 332
Jerse Ae, Yu J, Tall Bd, Kaper JB., J. Brunton (1990)
A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells.Proceedings of the National Academy of Sciences of the United States of America, 87
H. Yamanaka, Michio Kameyama, Toshiyuki Baba, Y. Fujii, Keinosuke Okamoto (1994)
Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formationJournal of Bacteriology, 176
M. Kaufman, J. Seyer, R. Taylor (1991)
Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.Genes & development, 5 10
I. Scaletsky, M. Silva, L. Trabulsi (1984)
Distinctive patterns of adherence of enteropathogenic Escherichia coli to HeLa cellsInfection and Immunity, 45
Jeffrey Miller (1992)
A short course in bacterial genetics
H. Parge, K. Forest, M. Hickey, D. Christensen, E. Getzoff, J. Tainer (1995)
Structure of the fibre-forming protein pilin at 2.6 Å resolutionNature, 378
M. Strom, S. Lory (1991)
Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly.The Journal of biological chemistry, 266 3
J. Nataro, K Maher, P. Mackie, J. Kaper (1987)
Characterization of plasmids encoding the adherence factor of enteropathogenic Escherichia coliInfection and Immunity, 55
M. Donnenberg, Jun Yu, J. Kaper (1993)
A second chromosomal gene necessary for intimate attachment of enteropathogenic Escherichia coli to epithelial cellsJournal of Bacteriology, 175
M. Donnenberg, J. Girón, J. Nataro, J. Kaper (1992)
A plasmid‐encoded type IV fimbrial gene of enteropathogenic Escherichia coli associated with localized adherenceMolecular Microbiology, 6
K. Dodson, F. Jacob-Dubuisson, R. Striker, S. Hultgren (1993)
Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes.Proceedings of the National Academy of Sciences of the United States of America, 90
Jun Yu, Helen Webb, T. Hirst (1992)
A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio choleraeMolecular Microbiology, 6
J. Peek, Ronald Taylor (1992)
Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae.Proceedings of the National Academy of Sciences of the United States of America, 89 13
(1995)
Enteropathogenic Escherichia coli. In Infections of the Gastrointestinal Tract
I. Bortoli-German, E. Brun, Béatrice Py, M. Chippaux, F. Barras (1994)
Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemiMolecular Microbiology, 11
K. Stone, Hong-zhong Zhang, Lisa Carlson, M. Donnenberg (1996)
A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilusMolecular Microbiology, 20
A. Doig, D. Williams (1991)
Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability.Journal of molecular biology, 217 2
J. Bardwell, K. McGovern, J. Beckwith (1991)
Identification of a protein required for disulfide bond formation in vivoCell, 67
Y. Kohara, K. Akiyama, K. Isono (1987)
The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic libraryCell, 50
Frederik Lindberg, J. Tennent, S. Hultgren, Björn Lund, Staff Normark (1989)
PapD, a periplasmic transport protein in P-pilus biogenesisJournal of Bacteriology, 171
A. Allaoui, J. Mounier, M. Prevost, P. Sansonetti, C. Parsot (1992)
icsB: a Shigella flexneri virulence gene necessary for the lysis of protrusions during intercellular spreadMolecular Microbiology, 6
Y. Taniyama, R. Kuroki, F. Omura, C. Seko, M. Kikuchi (1991)
Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme.The Journal of biological chemistry, 266 10
M. Farinha, B. Conway, L. Glasier, N. Ellert, R. Irvin, R. Sherburne, W. Paranchych (1994)
Alteration of the pilin adhesin of Pseudomonas aeruginosa PAO results in normal pilus biogenesis but a loss of adherence to human pneumocyte cells and decreased virulence in miceInfection and Immunity, 62
Françoise Jacob-Dubuisson, J. Pinkner, Zheng Xu, R. Striker, Anita Padmanhaban, S. Hultgren (1994)
PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA.Proceedings of the National Academy of Sciences of the United States of America, 91 24
E. Chen, P. Seeburg (1985)
Supercoil sequencing: a fast and simple method for sequencing plasmid DNA.DNA, 4 2
K. Lee, H. Sheth, Wah Wong, R. Sherburne, William Paranchych, Robert Hodges, C. Lingwood, H. Krivan, Randall Irvin (1994)
The binding of Pseudomonas aeruginosa pili to glycosphingolipids is a tip‐associated event involving the C‐terminal region of the structural pilin subunitMolecular Microbiology, 11
H. Seifert, C. Wright, C. Wright, A. Jerse, M. Cohen, J. Cannon (1994)
Multiple gonococcal pilin antigenic variants are produced during experimental human infections.The Journal of clinical investigation, 93 6
M. Strom, S. Lory (1993)
Structure-function and biogenesis of the type IV pili.Annual review of microbiology, 47
Hong-Zhong Zhang, Stephen Lory, M. Donnenberg (1994)
A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coliJournal of Bacteriology, 176
L. Saiman, A. Prince (1993)
Pseudomonas aeruginosa pili bind to asialoGM1 which is increased on the surface of cystic fibrosis epithelial cells.The Journal of clinical investigation, 92 4
M. Hobbs, J. Mattick (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 complexesMolecular Microbiology, 10
S. Kamitani, Y. Akiyama, Koreaki Ito (1992)
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.The EMBO Journal, 11
K. Strauch, Jon Beckwith (1988)
An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins.Proceedings of the National Academy of Sciences of the United States of America, 85 5
G. Chikami, J. Fierer, D. Guiney (1985)
Plasmid-mediated virulence in Salmonella dublin demonstrated by use of a Tn5-oriT constructInfection and Immunity, 50
M. Levine, J. Nataro, H. Karch, M. Baldini, J. Kaper, R. Black, M. Clements, A. O’Brien (1985)
The diarrheal response of humans to some classic serotypes of enteropathogenic Escherichia coli is dependent on a plasmid encoding an enteroadhesiveness factor.The Journal of infectious diseases, 152 3
B. Pasloske, W. Paranchych (1988)
The expression of mutant pilins in Pseudomonas aeruginosa: fifth position glutamate affects pilin methylationMolecular Microbiology, 2
J. Tomb (1992)
A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd.Proceedings of the National Academy of Sciences of the United States of America, 89 21
M. Donnenberg, Stephen Calderwood, A. Donohue‐Rolfe, G. Keusch, J. Kaper (1990)
Construction and analysis of TnphoA mutants of enteropathogenic Escherichia coli unable to invade HEp-2 cellsInfection and Immunity, 58
A. Feinberg, B. Vogelstein (1983)
A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity.Analytical biochemistry, 132 1
R. Ménard, P. Sansonetti, C. Parsot (1993)
Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cellsJournal of Bacteriology, 175
D. Sun, J. Seyer, I. Kovari, R. Sumrada, R. Taylor (1991)
Localization of protective epitopes within the pilin subunit of the Vibrio cholerae toxin-coregulated pilusInfection and Immunity, 59
C. Jones, J. Pinkner, R. Rotht, John HEUSERt, A. Nicholes, S. Abraham, ScoTr Hultgren (1995)
FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae.Proceedings of the National Academy of Sciences of the United States of America, 92 6
Frank Dailey, Howard Berg (1993)
Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America, 90
William Paranchych, Laura Frost (1988)
The physiology and biochemistry of pili.Advances in microbial physiology, 29
J. Girón, A. Ho, G. Schoolnik (1991)
An inducible bundle-forming pilus of enteropathogenic Escherichia coli.Science, 254 5032
M. Strom, D. Nunn, S. Lory (1993)
A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family.Proceedings of the National Academy of Sciences of the United States of America, 90
M. Kuehn, J. Heuser, S. Normark, S. Hultgren (1992)
P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tipsNature, 356
P. Reeves, Paul Douglas, G. Salmond (1994)
Beta‐lactamase topology probe analysis of the OutO NMePhe peptidase, and six other Out protein components of the Erwinia carotovora general secretion pathway apparatusMolecular Microbiology, 12
The periplasmic Escherichia coli enzyme DsbA catalyses the efficient formation of disulphide linkages in numerous extracytoplasmic proteins. Enteropathogenic E. coli, a major cause of infantile diarrhoea worldwide, expresses a type IV fimbria known as the bundle‐forming pilus that promotes adherence to tissue‐culture cells. In this study, we report that transposon insertions in the dsbA locus abolish adherence and dramatically reduce the level of bundlin, the major structural subunit of the pilus encoded by the bfpA locus. Adherence and bundlin levels are restored by complementation with the cloned dsbA gene. DsbA has no effect on bfpA transcription as measured with bfpA–lacZ fusions. Replacement of either cysteine codon 129 or 179 of bfpA with a serine codon results in reduced levels of bundlin, similar to the effect of the dsbA mutation. As is the case with dsbA mutants, this decreased level of bundlin is not due to decreased transcription. The half‐life of bundlin as detected by pulse‐chase experiments is dramatically reduced in a dsbA mutant in comparison to the wild type. The effect of DsbA on bundlin oxidation is independent of signal‐peptide processing. Thus, we demonstrate that the DsbA enzyme is critical for the biogenesis of a type IV fimbria because of the essential role of a disulphide bond in the stability of the major structural subunit. These data illuminate the early steps in the biogenesis of type IV fimbriae by demonstrating that newly synthesized prepilin is a transmembrane protein accessible to periplasmic and cytoplasmic processing enzymes.
Molecular Microbiology – Wiley
Published: Aug 1, 1996
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