Helical structure of P pili from Escherichia coli

Gong, Minfang; Makowski, Lee

doi:10.1016/0022-2836(92)90860-m

Cited by 89 publications

(40 citation statements)

References 15 publications

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“…Fimbrins are polymerized by hydrophobic and hydrophilic interactions to form either thick (7-to 8-nm), rigid structures, thin (2-to 4-nm), flexible filaments, or composites of both (13,16,19). The characterization of fimbrial biosynthesis has shown that the regulation and assembly of some fimbriae are accomplished by several accessory proteins (17).…”

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confidence: 99%

Salmonella enteritidis agfBAC operon encoding thin, aggregative fimbriae

et al. 1996

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Salmonella enteritidis produces thin, aggregative fimbriae, named SEF17, which are composed of polymerized AgfA fimbrin proteins. DNA sequence analysis of a 2-kb region of S. enteritidis DNA revealed three contiguous genes, agfBAC. The 453-bp agfA gene encodes the AgfA fimbrin, which was predicted to be 74% identical and 86% similar in primary sequence to the Escherichia coli curli structural protein, CsgA. pHAG, a pUC18 derivative containing a 3.0-kb HindIII fragment encoding agfBAC, directed the in vitro expression of the major AgfA fimbrin, with an M r of 17,000, and a minor AgfB protein, with an M r of 16,000, encoded by the 453-bp agfB gene. AgfA was not expressed from pDAG, a pUC18 derivative containing a 3.1-kb DraI DNA fragment encoding agfA but not agfB. Primer extension analysis identified two adjacent transcription start sites located immediately upstream of agfB in positions analogous to those of the E. coli curlin csgBA operon. No transcription start sites were located immediately upstream of agfA or agfC. Northern (RNA) blot analysis confirmed that transcription of agfA was initiated from the agfB promoter region. Secondary-structure analysis of the putative mRNA transcript for agfBAC predicted the formation of a stem-loop structure (⌬G؇, ؊22 kcal/mol [؊91 kJ/mol]) in the intercistronic region between agfA and agfC, which may be involved in stabilization of the agfBA portion of the agfBAC transcript. agfBAC and flanking regions had a high degree of sequence similarity with those counterparts of the E. coli curlin csgBA region for which sequence data are available. These data are demonstrative of the high degree of similarity between S. enteritidis SEF17 fimbriae and E. coli curli with respect to fimbrin amino acid sequence and genetic organization and, therefore, are indicative of a common and relatively recent ancestry.

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confidence: 99%

Salmonella enteritidis agfBAC operon encoding thin, aggregative fimbriae

et al. 1996

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“…The B max for pili binding to small intestinal and colonic SLP were 100 and 48 nmol of p-NP, respectively. Whole pili contain multiple proteins that may facilitate selective interactions with host membranes [1,3]. Although P pili have been shown to bind to other epitopes (immobilized ¢bronectin, for example) by means of the PapE and PapF proteins and independent of the PapG adhesin [9], this seems an unlikely explanation of these results, as the PapD^PapG complex also binds to SLP (Fig.…”

Section: Binding Of P Pili and Papd^papg Adhesin Complex To Mvm And Slpmentioning

confidence: 99%

“…P pili are heteropolymeric composite ¢bers consisting of a thin tip ¢brillum, joined to the distal ends of helical pilus rods [2]. PapA forms the bulk of the homopolymeric rod [3] and PapE forms the bulk of the tip ¢brillum [4]. The PapG adhesin is joined to the distal end of the tip ¢brillum via an adaptor protein PapF and the tip ¢brillum is connected to the pilus rod via PapK [4].…”

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confidence: 99%

Role of intestinal surfactant-like particles as a potential reservoir of uropathogenic Escherichia coli

Mahmood

Engle

Hultgren

et al. 2000

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…1A) (25,31). The order of the remaining pilus subunits has been delineated through a combination of biochemical studies and electron microscopy (2,6,7,13,21,23,25). The tip fibrillum is thought to be composed of PapG, PapF, and PapE ( Fig.…”

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confidence: 99%

“…1A). The thick rod contains PapA subunits arranged to form a right-handed helical cylinder with 3.28 subunits per turn (2,7,13). Finally, the PapH subunit is thought to terminate assembly and anchor the entire composite structure to the outer membrane (1) (Fig.…”

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confidence: 99%

Adaptor Function of PapF Depends on Donor Strand Exchange in P-Pilus Biogenesis of Escherichia coli

2007

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P-pilus biogenesis occurs via the highly conserved chaperone-usher pathway and involves the strict coordination of multiple subunit proteins. All nonadhesin structural P-pilus subunits possess the same topology, consisting of two domains: an incomplete immunoglobulin-like fold (pilin body) and an N-terminal extension. Pilus subunits form interactions with one another through donor strand exchange, occurring at the usher, in which the N-terminal extension of an incoming subunit completes the pilin body of the preceding subunit, allowing the incorporation of the subunit into the pilus fiber. In this study, pilus subunits in which the N-terminal extension was either deleted or swapped with that of another subunit were used to examine the role of each domain of PapF in functions involving donor strand exchange and hierarchical assembly. We found that the N-terminal extension of PapF is required to adapt the PapG adhesin to the tip of the fiber. The pilin body of PapF is required to efficiently initiate assembly of the remainder of the pilus, with the assistance of the N-terminal extension. Thus, distinct functions were assigned to each region of the PapF subunit. In conclusion, all pilin subunits possess the same overall architectural topology; however, each N-terminal extension and pilin body has specific functions in pilus biogenesis.P pili are adhesive organelles that are critical virulence factors in the establishment of pyelonephritis by uropathogenic Escherichia coli (23,(36)(37)(38). These adhesive organelles are macromolecular, fibrous structures on the surface of the bacteria that mediate the recognition of and attachment to tissues of the kidney by the pathogen (5,17,23,29,31,34,(36)(37)(38)42). This attachment is a key step in the pathogenic cascade of uropathogenic E. coli, leading to the establishment of infection (36,38

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Helical structure of P pili from Escherichia coli

Cited by 89 publications

References 15 publications

Salmonella enteritidis agfBAC operon encoding thin, aggregative fimbriae

Salmonella enteritidis agfBAC operon encoding thin, aggregative fimbriae

Role of intestinal surfactant-like particles as a potential reservoir of uropathogenic Escherichia coli

Adaptor Function of PapF Depends on Donor Strand Exchange in P-Pilus Biogenesis of Escherichia coli

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