The Physiology and Biochemistry of Pili

Paranchych, W.; Frost, Laura S.

doi:10.1016/s0065-2911(08)60346-x

Cited by 155 publications

(117 citation statements)

References 345 publications

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“…The pilin protein itself has been studied in detail. This protein makes up most, if not all, of the subunits of the pilus, where it is arranged in a helical array (Paranchych & Frost, 1988). The pilin proteins of several bacterial species are known to be modified by glycosylation and\or phosphorylation (Virji et al, 1993 ;Stimson et al, 1995 ;Castric, 1995 ;Forest et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

BfpU, a soluble protein essential for type IV pilus biogenesis in enteropathogenic Escherichia coli

et al. 2002

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A cluster of 14 genes located on the large plasmid of enteropathogenic Escherichia coli (EPEC) strains is sufficient to direct the biogenesis of the type IV bundle-forming pilus (BFP) in a recombinant E. coli host. The fifth gene in the cluster, bfpU, encodes a protein that is predicted to be localized to the periplasmic space. To determine whether BfpU is necessary for pilus biogenesis, the authors constructed a non-polar bfpU mutant EPEC strain by allelic exchange. The mutant strain was unable to perform localized adherence and auto-aggregation, two phenotypes associated with BFP expression, and it failed to make BFP. These phenotypes were restored to the bfpU mutant by a plasmid containing bfpU. There was no difference between the wild-type and bfpU mutant strains in their expression or processing of the pre-pilin protein or in their localization of the pilin protein in the inner and outer membranes. Fractionation studies revealed that BfpU is completely soluble and is detected in both the periplasm and the cytoplasm. Thus, BfpU represents a novel protein required for type IV pilus assembly.

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Section: Introductionmentioning

confidence: 99%

BfpU, a soluble protein essential for type IV pilus biogenesis in enteropathogenic Escherichia coli

et al. 2002

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“…They appear to mediate attachment of the cell to epithelial cells (Paranchych and Frost, 1988) as well as a form of surface translocation termed twitching motility (Henrichsen , 1975;Bradley, 1980). They have a polar location on the cell (Ottow, 1975) and in at least some species are associated with a high natural competence for transformation (B0vre and Fmholm, 1972), probably as the means of promoting genetic exchange within the population (Seifert et al , 1988) .…”

Section: Introductionmentioning

confidence: 99%

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

Mattick

1993

Molecular Microbiology

361

286

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Summary The Pseudomonas aeruginosa genes pilB‐D and pilQ are necessary for the assembly of type 4 fimbriae. Homologues of these genes and of the subunit (pilin) gene have been described in various different bacterial species, but not always in association with type 4 fimbrial biosynthesis and function. Pil‐like proteins are also involved in protein secretion, DNA transfer by conjugation and transformation, and morphogenesis of filamentous bacteriophages. It seems likely that the Pil homologues function in the processing and export of proteins resembling type 4 fimbrial sub‐units, and in their organization into fimbrial‐like structures. These may either be true type 4 fimbriae, or components of protein complexes which act in the transport of macromolecules (DNA or protein) into or out of the cell. Some PilB‐like and PilQ‐like proteins are apparently also involved in the assembly of non‐type 4 polymeric structures (filamentous phage virions and conjugative pili). The diverse studies summarized in this review are providing insight into an extensive infrastructural system which appears to be utilized in the formation of a variety of cell surface‐associated complexes.

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“…Fimbriae (also called pili) comprise a class of nonflagellar, proteinaceous filaments produced on the surface of a wide range of bacteria (11,43,46). Detailed studies of several fimbriae from a variety of animal and human pathogens have revealed these appendages to be highly organized, complex structures which in some cases facilitate bacterial adherence to specific host tissues (21,45,46,56).…”

mentioning

confidence: 99%

“…Detailed studies of several fimbriae from a variety of animal and human pathogens have revealed these appendages to be highly organized, complex structures which in some cases facilitate bacterial adherence to specific host tissues (21,45,46,56). Fimbriae are polymers composed mainly of a single protein species named fimbrin, which usually forms filaments 2 to 7 nm wide.…”

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confidence: 99%

Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis

et al. 1991

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Novel fimbriae were isolated and purified from the human enteropathogen SalmoneUa enteritidis 27655. These fimbriae were thin (measuring 3 to 4 nm in diameter), were extremely aggregative, and remained cell associated despite attempts to separate them from blended cells by centrifugation. The thin fimbriae were not solubilized in 5 M NaOH or in boiling 0.5% deoxycholate, 8 M urea, or 1 to 2% sodium dodecyl sulfate (SDS) with or without 5% 13-mercaptoethanol. Therefore, an unconventional purification procedure based on the removal of contaminating cell macromolecules in sonicated cell extracts by enzymatic digestion and preparative SDS-polyacrylamide gel electrophoresis (PAGE) was used. The insoluble fimbriae recovered from the well of the gel required depolymerization in formic acid prior to analysis by SDS-PAGE. Acid depolymerization revealed that the fimbriae were composed of fimbrin subunits, each with an apparent molecular mass of 17 kDa. Although their biochemical characteristics and amino acid composition were typical of fimbriae in general, these thin fimbriae were clearly distinct from other previously characterized fimbriae. Moreover, their fimbrin subunits had a unique N-terminal amino acid sequence. Native fimbriae on whole cells were specifically labeled with immune serum raised to the purified fimbriae. This immune serum also reacted with the denatured 17-kDa fimbrin protein in Western blots. The polyclonal immune serum did not cross-react with the other two native fimbrial types produced by this strain or with their respective fimbrins on Western blots (immunoblots). Therefore, these fimbriae represent the third fimbrial type produced by the enteropathogen S. enteritidis.

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The Physiology and Biochemistry of Pili

Cited by 155 publications

References 345 publications

BfpU, a soluble protein essential for type IV pilus biogenesis in enteropathogenic Escherichia coli

BfpU, a soluble protein essential for type IV pilus biogenesis in enteropathogenic Escherichia coli

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

Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis

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