Disease relevance of papC

• Identification of a major cluster including 96.4% of the strains carrying the cnf1, papC, and hlyC genes and ECOR subgroup B2 strains suggested that the virulent E. coli strains causing bacteremia in cancer patients are closely related to ECOR B2 strains [1].
• The organization of P fimbrial gene clusters of 13 papC-hybridizing Escherichia coli strains isolated from poultry with colisepticaemia, five P-fimbriae-expressing (P-positive) and eight P-fimbriae-non-expressing (P-negative), were examined by PCR and by Southern blot hybridization using primers or gene probes specific to the I, B, A, C or G genes [2].
• Common accessory genes for the Bordetella pertussis filamentous hemagglutinin and fimbriae share sequence similarities with the papC and papD gene families [3].
• Four pap genes (papA, papB, papC, papM) were found by sequencing near to snbA, a Streptomyces pristinaespiralis gene which was previously shown to encode one of the pristinamycin I (PI) synthetases [4].
• Genes encoding aerobactin and PapC occurred significantly less frequently in isolates causing cystitis than in those causing prostatitis (P < 0.01 and P < 0.0001, respectively) and pyelonephritis (P < 0.01 and P < 0.0001, respectively) [5].

High impact information on papC

• The nucleotide sequence of this area contains the open reading frames fhaD and fhaA, whose products share sequence similarities with the papD and papC gene products, respectively [3].
• The PapC usher forms an oligomeric channel: implications for pilus biogenesis across the outer membrane [6].
• Following the arrival of PapC, the formation of pili seemed to proceed spontaneously and was not sensitive to a pH shift or an inhibitor of the electrochemical gradient across the cytoplasmic membrane [7].
• The kinetics of assembly and the energy requirements of the "secretion" events at the outer membrane were investigated using a pulse-chase analysis in which preformed labeled periplasmic chaperone-subunit complexes were assembled into pili in synchrony by the induction of PapC [7].
• Removal of the C-terminal domain did not change the basic shape of the PapC molecule, but altered the dimeric association of the usher, suggesting that the C terminus forms part of the dimerization interface [8].

Biological context of papC

• The presence on various pathogenicity islands (PAIs) of a combination of the cnf1, papC, and hlyC genes on the chromosome was strongly suggested by Southern blotting of pulsed-field gel electrophoresis (PFGE) patterns with specific DNA probes [1].
• This outer membrane protein had extensive amino acid sequence homology with PapC and FaeD, two E. coli outer membrane proteins involved in the export and assembly of pilus and fimbria subunits on the cell surface [9].

Anatomical context of papC

• In this study we investigated the effect of human milk on production of mRNA for fimA (type 1 fimbriae) and papC (P fimbriae) in E. coli [10].
• Six uropathogenic Escherichia coli strains (all expressing type 1 pili; three positive for the gene marker for P-fimbriae papC and three negative for papC), previously isolated from patients with symptomatic urinary tract infections, were grown in urine samples and tested for their ability to adhere to the T24 bladder cell line in vitro [11].

Other interactions of papC

• Of the blood isolates, 24, 37, and 26% were positive for cnf1, papC, and hlyC, respectively, versus only 6, 17, and 6% of the fecal isolates (P < 0.05 in all instances) [1].

Analytical, diagnostic and therapeutic context of papC

• We studied the structure and oligomeric state of PapC by gel filtration, dynamic light scattering, and electron microscopy and image analysis [8].

References