Morphogenetic expression of Moraxella bovis fimbriae (pili) in Pseudomonas aeruginosa

Beard, M.K. McG.; Mattick, John S.; Moore, Lindsey; Mott, Margaret R.; Marrs, Carl F.; Egerton, J. R.

doi:10.1128/jb.172.5.2601-2607.1990

Cited by 58 publications

(26 citation statements)

References 23 publications

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“…It has been proposed that the infrastructural machinery for production and assembly of type 4 fimbriae is strongly conserved among the pathogens that produce this specific class of fimbriae. This is based on the evidence that the structural subunit from a variety of type 4 fimbriate bacteria can be produced and assembled in P. aeruginosa (3,12,19,27). For this reason, we investigated the possibility that a pilZ homolog exists in other species that produce type 4 fimbriae.…”

Section: Discussionmentioning

confidence: 99%

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Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa

et al. 1996

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The opportunistic pathogen Pseudomonas aeruginosa produces type 4 fimbriae which promote adhesion to epithelial cells and are associated with a form of surface translocation called twitching motility. We have used transposon mutagenesis to identify loci required for fimbrial assembly or function by screening for mutants that lack the spreading colony morphology characteristic of twitching motility. A subset of these mutants is resistant to fimbria-specific phage. One of these mutants (R270) was found to contain a transposon insertion in a new gene, termed pilZ, which is located on chromosomal SpeI fragment I at about 40 min on the P. aeruginosa map, a position remote from other loci involved in fimbrial biogenesis. pilZ appears to be linked to and possibly forms an operon with a gene, holB*, which is homologous to the gene encoding the ␦ subunit of Escherichia coli DNA polymerase III. The product of the pilZ gene is a protein of 118 amino acids (predicted molecular weight, 12,895) which probably has a cytoplasmic location. PilZ appears to be a new class of protein which has not hitherto been represented in the sequence databases, and its function is unknown. Complementation studies indicate that pilZ is able to restore the expression of fimbriae on the surface of P. aeruginosa, as well as twitching motility and sensitivity to fimbria-specific phage when provided in trans to the R270 mutant.Type 4 fimbriae (or common pili) are flexible, filamentous surface appendages which are found in a number of important pathogenic bacteria, including Neisseria gonorrhoeae, Neisseria meningitidis, Moraxella bovis, Dichelobacter nodosus, and Pseudomonas aeruginosa, and which mediate adherence to host epithelial tissue during colonization (33,40,42). Type 4 fimbriae were originally defined by their polar arrangement on the cell and their ability to promote a form of motion called twitching motility (14, 32). Type 4 fimbriae are also characterized by conserved features of the structural subunit proteins which make up the fimbrial strand. These include a short, positively charged leader sequence of six to eight amino acids which is removed during fimbrial assembly, a modified amino acid, Nmethylphenylalanine, as the first residue in the mature protein, and a highly conserved hydrophobic amino-terminal domain (7,42).The biogenesis of type 4 fimbriae is a complex process involving a large network of genes that have thus far been localized to three separate regions of the Pseudomonas chromosome. The largest locus is located on SpeI fragment E at about 70 min on the physical map and contains the fimbrial subunit gene (pilA), two ancillary genes (pilB and pilC), the specific leader peptidase gene (pilD), and the sensor/regulator genes (pilS and pilR) responsible for the transcriptional activation of the fimbrial subunit gene (16,21,41). Recently, two further genes (pilE and pilV) have been localized to this region of the genome, both of which encode proteins possessing prepilinlike leader sequences that appear to be cleaved by the PilD...

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Section: Discussionmentioning

confidence: 99%

“…This is indicated by the observation that P. aeruginosa is capable of producing fimbriae composed of heterologous subunits expressed from cloned subunit genes from D. nodosus, M. bovis, and N. gonorrhoeae (3,19,27). A number of homologs to the fimbria-associated genes of P. aeruginosa have been identified in other type 4 fimbriate bacteria (20,24).…”

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Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa

et al. 1996

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“…Bacteria bearing plasmids carrying cloned genes were grown on medium containing 150 g of carbenicillin per ml. Basic electron microscopy procedures were as described in the legend to on May 9, 2018 by guest http://jb.asm.org/ ginosa can form type IV pili from pilin subunits encoded by genes cloned from other species of bacteria (4,15,20,23,40), we tested whether PpdD could form pili in P. aeruginosa PAK A Ϫ lacking endogenous type IV pilin. Typical type IV pili were observed by electron microscopy in the control strains PAK and PAK A Ϫ A ϩ ( Fig.…”

Section: Figmentioning

confidence: 99%

PpdD Type IV Pilin of Escherichia coli K-12 Can Be Assembled into Pili in Pseudomonas aeruginosa

Sauvonnet¹,

Gounon

Pugsley³

2000

J Bacteriol

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Escherichia coli K-12 possesses at least 16 chromosomal genes related to genes involved in the formation of type IV pili in other gram-negative bacteria. However, E. coli K-12 does not produce type IV pili when grown under standard laboratory conditions. The results of reverse transcription-PCR, operon fusion analysis, and immunoblotting demonstrated that several of the putative E. coli piliation genes are expressed at very low levels. Increasing the level of expression of the major pilin gene (ppdD) and the linked assembly genes hofB and hofC (homologues of the Pseudomonas aeruginosa type IV pilus assembly genes pilB and pilC) did not lead to pilus production. However, expression of the ppdD gene in P. aeruginosa led to assembly of PpdD into pili that were recognized by antibodies directed against the PpdD protein. Assembly of PpdD into pili in P. aeruginosa was dependent on the expression of the pilB and pilC genes and independent of expression of the P. aeruginosa pilin structural gene pilA.

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“…These polypeptides, which range in molecular mass from 15 to about 18 kDa, contain a short, positively charged leader sequence of six or seven amino acids, an unusual modified amino acid at the amino terminus of the mature protein (usually N-methylphenylalanine), and a conserved and hydrophobic amino-terminal domain (13,38). Previous research has suggested that many components of the type IV fimbria biogenesis apparatus are likely to be functionally conserved across bacterial species (2,21,25,31). In some species, several of the genes involved in biogenesis of type IV fimbriae are clustered together close to the pilin structural gene.…”

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A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli

1994

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Enteropathogenic Escherichia coli, a leading agent of infantile diarrhea worldwide, adheres to tissue culture cells in a pattern called "localized adherence." Localized adherence is associated with bundle-forming pili encoded by the plasmid bfpA gene, the product of which is homologous with the major structural subunit proteins of type IV fimbriae in other bacteria. Several of these proteins have been shown to be processed from a precursor by a specific prepilin peptidase. We cloned restriction fragments downstream of the bfpA gene into an E. coli-Pseudomonas aeruginosa shuttle vector and mobilized them into a P. aeruginosa prepilin peptidase (pilD) mutant. A plasmid containing a 1.3-kb PstI-BamHI fragment was able to complement the pilD mutation, as demonstrated by restoration of sensitivity to the pilus-specific bacteriophage PO4. The DNA sequence of this fragment revealed an open reading frame, designated bfpP, the predicted product of which is homologous to other prepilin peptidases, including TcpJ of Vibrio cholerae (30% identical amino acids), PulO of Klebsiella oxytoca (29%), and PilD of P. aeruginosa (28%). A bfpA::TnphoA mutant complemented with a bfpA-containing DNA fragment only partially processes the BfpA protein. When complemented with a larger fragment containing bfpP as well as bfpA, the mutant expresses the fully processed BfpA protein. P. aeruginosa PAK, but not a pilD mutant of PAK, expresses mature BfpA protein when the bfpA gene is mobilized into this strain. Thus, as in other type IV fimbria systems, enteropathogenic E. coli utilizes a specific prepilin peptidase to process the major subunit of the bundle-forming pilus. This prepilin petidase contains sequence and reciprocal functional homologies with the PilD protein of P. aeruginosa.

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Morphogenetic expression of Moraxella bovis fimbriae (pili) in Pseudomonas aeruginosa

Cited by 58 publications

References 23 publications

Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa

Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa

PpdD Type IV Pilin of Escherichia coli K-12 Can Be Assembled into Pili in Pseudomonas aeruginosa

A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli

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