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PubMed1983

The production of F41 fimbriae by piglet strains of enterotoxigenic Escherichia coli that lack K88, K99 and 987P fimbriae.

The enterotoxigenic Escherichia coli strains 1676, 1706, 1751 and KEC96a, which do not produce fimbrial adhesive antigens of the K88, K99 or 987P antigen type reacted both in vitro and in vivo with antiserum to F41 fimbriae in an indirect immunofluorescent antibody technique. Antiserum used to demonstrate material B, an adhesive antigen thought to mediate the adhesive and mannose-resistant (MR) haemagglutinating properties of E. coli strains 1676, 1706 and 1751, reacted in vitro with an F41+ strain. The antiserum also inhibited the MR haemagglutinating activity of F41 antigen and gave an anionic precipitation line in immunoelectrophoresis experiments with an extract containing F41 antigen. The MR haemagglutinating properties of an antigen extract containing material B from E. coli strain 1706 was neutralized by antiserum to F41 fimbriae and by OK antisera to E. coli strains that produce both F41 and K99 fimbriae. These sera also gave an anionic precipitation line with the MR haemagglutinin from E. coli strain 1706 and the MR haemagglutinin gave a line of identity with F41 in gel diffusion experiments with antiserum to F41 fimbriae. OK antisera to K99+ F41- bacteria and OK antisera to K88+ bacteria and 987P+ bacteria did not react with this haemagglutinin. Transmission electron microscopy on the ileum of newborn gnotobiotic piglets infected with E. coli strain 1706 showed irregular, poorly defined filamentous material surrounding some,though not all, bacteria but regular fimbrial structures were not visible.(ABSTRACT TRUNCATED AT 250 WORDS)

Adhesiveness↗
PubMed1980

A possible association between CFA (I) fimbriae and K99 fimbriae on Escherichia coli and bacterial adherence to human lymphocytes.

We have explored a possible association between Escherichia coli binding to human lymphocytes and plasmid coded fimbriae on the bacterial surface. E. coli with or without the plasmid coded membrane CFA(I), K99 and K88 were mixed with freshly-drawn human peripheral blood lymphocytes. When the lymphocytes were mixed with E. coli possessing the CFA(I) fimbriae, 59% of the lymphocytes bound bacteria onto the surface, whereas only 22% of the lymphocytes bound the CFA(I)- derivative. The lymphocytes bound 53% and 56% of two K9+ strains, whereas 22% and 8% of the lymphocytes adhered the same strains without the K99 fimbriae. Twelve per cent and 7% of lymphocytes bound bacteria when the strain was K88+ or K88-, respectively. Likewise a low (8%) adherence to lymphocytes was found when the E. coli did not possess fimbriae or flagella.

Antigens, Bacterial↗
PubMed1997

Synthesis and function of Actinomyces naeslundii T14V type 1 fimbriae require the expression of additional fimbria-associated genes.

The nucleotide sequence of the chromosomal DNA flanking the Actinomyces naeslundii (formerly A. viscosus) T14V type 1 fimbrial structural subunit gene (fimP) was determined. Six open reading frames (ORFs), in the order 5' ORF3, ORF2, ORF1,fimP, ORF4, ORF5, ORF6 3', were identified. ORF1 encoded a protein of 408 amino acid residues (Mr = 39,270) and had significant sequence homology with the A. naeslundii T14V type 1 and A. naeslundii WVU45 type 2 fimbrial structural subunits. An in-frame fusion of ORF1 to the malE gene of the expression vector, pMAL-c2, yielded a protein that was immunostained with antibodies raised against the maltose binding protein and A. naeslundii T14V whole bacteria. Digestion of the fusion protein with factor Xa released a protein (apparent molecular mass of 34 kDa) that was immunostained only with the antibody directed against A. naeslundii T14V whole bacterial cells. Integration plasmids carrying a kanamycin resistance gene (kan) that was used to substitute for ORF1 or for DNA fragments internal to the coding region of the other five ORFs were used to transform A. naeslundii T14V. Neither type 1 fimbriae nor the 65-kDa fimbrial structural subunit was detected in mutants obtained by allelic replacement of ORF1 or ORF2. Mutants obtained by allelic replacement of ORF3 or ORF4 expressed only the 65-kDa fimbrial structural subunit. These mutants did not bind, in vitro, to proline-rich proteins that serve as the receptors for Actinomyces type 1 fimbriae. In contrast, a mutant in which the integration plasmid DNA had been inserted at a site close to the carboxyl terminus of ORF6 expressed type 1 fimbriae and had adherence properties similar to those observed in the wild-type strain. These results demonstrate the existence of additional genes near fimP that are likely to be involved in the synthesis and function of cell surface fimbriae of A. naeslundii T14V.

Actinomyces viscosus↗
PubMed1995

Cloning of determinants encoding F165(2) fimbriae from porcine septicaemic Escherichia coli confirms their identity as F1C fimbriae.

Cloning of the f165(2) operon that encodes F1C-like fimbriae in Escherichia coli indicates that this operon is a member of the S/Foc family. The genetic determinant coding for the F165(2) fimbriae was cloned from the chromosome of the porcine E. coli wild-type strain 4787 (O115:K-1:H51:F165). The cloned F165(2) and the wild-type operon expressed a major fimbrial protein subunit of molecular mass 17.2 kDa that was detected by anti-F165 and anti-F1C polyclonal sera. The sequences of the f165(2)A and f165(2)FGH genes are reported. Major subunit gene f165(2)A encodes a mature protein of 156 amino acids. Minor subunit genes F, G and H encode mature proteins of 148, 145 and 276 amino acids, respectively. The amino acid sequences of the four proteins share similarities with those of the known S and F1C fimbrial antigens that are produced by extraintestinal E. coli which is associated with sepsis, urinary tract infections and newborn meningitis. The F165(2)A protein was identical to the major subunit protein of F1C, with a difference only at the first position. It was also similar, to a lesser extent, to the major subunit proteins of SfaI and SfaII fimbriae. F165(2)F was identical to FocF and SfaG/SfaIIS, and F165(2)H was more closely related to FocG than to SfaIS/SfaIIS, and F165(2)H was more closely related to FocH than to SfaIH/SfaIIH.

Amino Acid Sequence↗
PubMed1996

P-fimbriae-producing septicaemic Escherichia coli from poultry possess fel-related gene clusters whereas pap-hybridizing P-fimbriae-negative strains have partial or divergent P fimbrial gene clusters.

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. The absence of P fimbrial expression was associated with lack of PCR amplification of one or more of these genes, most commonly the I gene. Restriction endonuclease EcoRI, BamHI or PstI digests of genomic DNA from all strains hybridized with each of the gene probes and demonstrated polymorphisms between P-positive and P-negative strains. PstI digests of DNA from 12 of the 13 strains, when hybridized with the A gene probe, demonstrated a 0.1 kb fragment specific to the felA gene which encodes the major structural protein of F11 fimbriae. Hence, only the P-positive strains contained complete copies of fel-related gene clusters. In contrast, most of the pap-hybridizing P-negative strains contained partial or divergent P fimbrial gene clusters, which explains the lack of P fimbrial expression by these strains.

Animals↗
PubMed2006

Demonstration of regulatory cross-talk between P fimbriae and type 1 fimbriae in uropathogenic Escherichia coli.

The majority of Escherichia coli strains isolated from urinary tract infections have the potential to express multiple fimbriae. Two of the most common fimbrial adhesins are type 1 fimbriae and pyelonephritis-associated pili (Pap). Previous research has shown that induced, plasmid-based expression of a Pap regulator, papB, and its close homologues can prevent inversion of the fim switch controlling the expression of type 1 fimbriae. The aim of the present study was to determine if this cross-regulation occurs when PapB is expressed from its native promoter in the chromosome of E. coli K-12 and clinical isolates. The regulation was examined in three ways: (1) mutated alleles of the pap regulatory region, including papB and papI, that maintain the pap promoter in either the off or the on phase were exchanged into the chromosome of both E. coli K-12 and the clinical isolate E. coli CFT073, and the effect on type 1 fimbrial expression was measured; (2) type 1 fimbrial expression was determined using a novel fimS : : gfp(+) reporter system in mutants of the clinical isolate E. coli 536 in which combinations of complete fimbrial clusters had been deleted; (3) type 1 fimbrial expression was determined in a range of clinical isolates and compared with both the number of P clusters and their expression. All three approaches demonstrated that P expression represses type 1 fimbrial expression. Using a number of novel genetic approaches, this work extends the initial finding that PapB inhibits FimB recombination to the impact of this regulation in clinical isolates.

Adhesins, Bacterial↗
PubMed1994

Sequences related to the major subunit gene fedA of F107 fimbriae in porcine Escherichia coli strains that express adhesive fimbriae.

Porcine Escherichia coli strains isolated from cases of postweaning diarrhea or edema disease were analysed for the presence of fedA, the major subunit gene of F107 fimbriae. The E. coli isolates were known to contain colonisation factor '8813', or to express F107, 2134P or other fimbriae, different from F4, F5, F6, and F41. PCR with fedA-specific primers, restriction enzyme digestion of the PCR product, and nucleotide sequence analysis demonstrated that 2134P pili, colonisation factor '8813' and fimbriae identified on Australian strains of the O141 serotype belong to one family of F107 fimbrial antigens.

Amino Acid Sequence↗
PubMed1997

Porphyromonas gingivalis fimbria-stimulated bone resorption is inhibited through binding of the fimbriae to fibronectin.

Our most recent study demonstrated that fibronectin is one of the Porphyromonas gingivalis fimbria-binding proteins. In this present study, we demonstrate with mouse embryonic calvarial cells that P. gingivalis fimbria-stimulated bone resorption is inhibited by human fibronectin. The fibronectin inhibition was dose and culture time dependent and was completely neutralized by antifibronectin antibody. The inhibitory action of fibronectin depended on fimbrial interaction with the heparin-binding and cell-attachment domains in the fibronectin structure.

Animals↗
PubMed1983

Regeneration of rat hippocampal fimbria fibers after fimbria transection and peripheral nerve or fetal hippocampal implantation.

After a unilateral hippocampal fornix-fimbria transection in adult rats, either autologous peripheral nerve or fetal hippocampus was implanted into the transection site. After 2 to 4 weeks, 2 to 3 months, and 6 to 8 months fimbria fiber regeneration was analyzed by acetylcholinesterase (AChE) histochemistry and retrograde transport of horseradish peroxidase after injection into the denervated host hippocampus. Prominent innervation of both types of implant by central AChE-staining axons occurred by 2 to 3 weeks postimplantation and was sustained to at least 8 months. Reinnervation of the adjacent host hippocampal terminal zone was also apparent, but was sparse compared with innervation of implants.

Acetylcholinesterase↗
PubMed1988

Mutations in cloned Escherichia coli P fimbriae genes that makes fimbriae-production resistant to suppression by trimethoprim.

The effect of sublethal concentrations of trimethoprim on the expression of P fimbriae was tested in Escherichia coli HB101 recombinant strains. Fimbriation was inhibited at trimethoprim concentrations down to at least 1/64 of the minimal inhibitory concentration. However, the expression of the P fimbrillin by recombinant plasmids containing deletions in front of the fimbrillin gene did not respond to the inhibitory effect of trimethoprim indicating that trimethoprim may act at the level of gene regulation.

Agglutination Tests↗
PubMed2004

Characterization of the second long polar (LP) fimbriae of Escherichia coli O157:H7 and distribution of LP fimbriae in other pathogenic E. coli strains.

A second region containing five genes homologous to the long polar fimbrial operon of Salmonella enterica serovar Typhimurium is located in the chromosome of enterohemorrhagic Escherichia coli (EHEC) O157:H7. A non-fimbriated E. coli K-12 strain carrying the cloned EHEC lpf (lpf2) genes expressed thin fibrillae-like structures on its surface and displayed reduced adherence to tissue culture cells. Neither mutation in the lpfA2 gene in either the parent or lpfA1 mutant strains showed an effect in adherence or in the formation of A/E lesions on HeLa cells. lpfA2 isogenic mutant strains adhere to Caco-2 cells almost as well as the wild-type at 5 h, but they were deficient in adherence at early time points. A collection of diarrheagenic E. coli strains were investigated for the presence of lpfA1 and lpfA2 and results showed that these genes are present in specific serogroups which are phylogenetically related. Our results suggest that LP fimbriae 2 may contribute to the early stages of EHEC adhesion and that genes encoding the major LP fimbrial subunits are present in a small group of EHEC and EPEC serotypes.

Bacterial Adhesion↗
PubMed2002

Role of type 1 fimbria- and P fimbria-specific adherence in colonization of the neurogenic human bladder by Escherichia coli.

Recent clinical studies suggest that the deliberate colonization of the human bladder with a prototypic asymptomatic bacteriuria-associated bacterium, Escherichia coli 83972, may reduce the frequency of urinary tract infection in individuals with spinal cord injuries. However, the mechanism by which E. coli 83972 colonizes the bladder is unknown. We examined the role in bladder colonization of the E. coli 83972 genes papG and fimH, which respectively encode P and type 1 receptor-specific fimbrial adhesins. E. coli 83972 and isogenic papGDelta and papGDelta fimHDelta mutants of E. coli 83972 were compared for their capacities to colonize the neurogenic human bladder. Both strains were capable of stable colonization of the bladder. The results indicated that type 1 class-specific adherence and P class-specific adherence, while implicated as significant colonization factors in experiments that employed various animal model systems, were not required for colonization of the neurogenic bladder in human beings. The implications of these results with regard to the selection of potential vaccine antigens for the prevention of urinary tract infection are discussed.

Adhesins, Escherichia coli↗
PubMed1982

P-antigen-recognizing fimbriae from human uropathogenic Escherichia coli strains.

P-antigen-recognizing fimbriae (P fimbriae) from four pyelonephritogenic Escherichia coli strains and type 1 fimbriae from an E. coli strain and a Salmonella typhimurium strain were purified. The P fimbriae were morphologically similar to type 1 fimbriae. The purified P fimbriae agglutinated neuraminidase-treated human P1 and P2k erythrocytes but not p erythrocytes, which lack all P-blood group-specific glycosphingolipids. However, coating of neuraminidase-treated p erythrocytes with globoside rendered such erythrocytes agglutinable by the P fimbriae. The hemagglutinations were in all instances fully inhibited by the synthetic alpha-D-Galp-(1-4)-beta-D-Galp-1-O-Me glycoside. The binding specificity of the P fimbriae could also be demonstrated by using fimbriae coated onto latex particles and nontreated erythrocytes. It was thus concluded that the P fimbriae recognize and bind to the alpha-D-Galp-(1-4)-beta-D-Galp carbohydrate sequence occurring in the series of P-blood group antigen-specific glycosphingolipids. In contrast to both type 1 fimbriae, all four P fimbriae preparations showed multiple bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Antisera were raised in rabbits against the various E. coli fimbriae. In enzyme-linked immunosorbent assays each one of the antisera to the P fimbriae reacted to titers of log 4 to 7 with both the homologous and the heterologous P fimbriae, but not with the type 1 fimbriae of E. coli. In a reciprocal fashion, the antiserum to the type 1 fimbriae of one E. coli strain reacted only with the homologous type 1 but not with any of the P fimbriae preparations.

Blood Group Antigens↗
PubMed1998

Binding of Porphyromonas gingivalis fimbriae to proline-rich glycoproteins in parotid saliva via a domain shared by major salivary components.

Porphyromonas gingivalis, a putative periodontopathogen, can bind to human saliva through its fimbriae. We previously found that salivary components from the submandibular and sublingual glands bind to P. gingivalis fimbriae and that acidic proline-rich protein (PRP) and statherin function as receptor molecules for fimbriae. In this study, we investigated the fimbria-binding components in parotid saliva. Fractionated human parotid saliva by gel-filtration chromatography was immobilized onto nitrocellulose membranes for the overlay assay following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The salivary components on the membrane were allowed to interact with fimbriae purified from P. gingivalis ATCC 33277, and the interacted fimbriae were probed with anti-fimbria antibodies. The fimbriae were shown to bind to two forms of proline-rich glycoproteins (PRGs) as well as to acidic PRPs and statherin. Moreover, fimbriae bound to several components of smaller molecular size which appeared to be acidic PRP variants and basic PRPs. Fimbriae bound strongly to the purified PRGs adsorbed onto hydroxyapatite (HAP) beads. In contrast, PRGs in solution failed to inhibit the fimbrial binding to the immobilized PRGs on the HAP beads. These findings suggest that the appearance of binding site(s) of PRGs can be ascribed to their conformational changes. We previously identified the distinct segments within PRP and statherin molecules that are involved in fimbrial binding. The peptides analogous to the binding regions of PRP and statherin (i.e., PRP-C and STN-C) markedly inhibit the binding of fimbriae to PRP and statherin immobilized on the HAP beads, respectively. The PRP-C significantly inhibited the binding of fimbriae to PRG-coated HAP beads as well as to PRP on HAP beads. The peptide did not affect the binding of fimbriae to statherin, whereas the STN-C showed no effect on the fimbrial binding to PRPs or PRGs. In the overlay assay, the PRP-C clearly diminished the interactions between the fimbriae and the various salivary components, including PRPs, the PRGs, and the components with smaller molecular sizes but not statherin. These results strongly suggest that fimbriae bind to salivary components (except statherin) via common peptide segments. It is also suggested that fimbriae bind to saliva through the two distinct binding domains of receptory salivary components: (i) PRGs and PRPs and (ii) statherin.

Adult↗
PubMed1996

Prevotella intermedia fimbriae mediate hemagglutination.

Our earlier studies demonstrated that clinical strains of Prevotella intermedia, isolated from human periodontal pockets, possess various types of fimbria (surface appendages) as determined ultrastructurally. These bacteria have the ability to agglutinate selected mammalian erythrocytes. Hemagglutinating activity exhibited by these cells may be attributable to these surface structures. Strain 17, which possess fimbriae of 8 nm in diameter and readily agglutinates human, monkey, sheep, rabbit, and mouse erythrocytes was selected to determine whether these fimbriae possessed the hemagglutinating activity. Fimbriae were mechanically sheared, concentrated by ammonium sulfate precipitation, solubilized in 10 mM Tris-HCl buffer containing 0.5% deoxycholate and partly purified by ultracentrifugation in a 10-50% linear sucrose gradient. Isolated fimbriae banded at a density of 1.20-1.15 g/ml, appeared fairly uniform ultrastructurally, and possessed hemagglutinating activity. The hemagglutinating activity of P. intermedia whole cells and isolated fimbriae was reduced by treatment with proteases and eliminated by treatment with heat at 80 degrees C for 10 min. The optimal pH for the hemagglutination was 7.0. In the process of hemagglutination, P. intermedia whole cells and isolated fimbriae bound to rabbit erythrocytes as observed by: (a) decrease in the hemagglutinating activity of bacterial whole cells and isolated fimbriae after incubation with rabbit erythrocytes, (b) increase in hemagglutinating activity of the red cells used for absorption, and (c) the presence of P. intermedia whole cells and fimbriae on red cells after absorption as revealed by immunoelectron microscopy. Both the immune immunoglobulin G of the rabbit polyclonal anti-fimbriae antibody and the immune immunoglobulin G and its Fab fragments of the murine monoclonal anti-fimbriae antibody were effective inhibitors of hemagglutination mediated by isolated fimbriae. Immunogold labeling showed that the monoclonal antibody bound specifically to P. intermedia fimbriae. These results collectively suggest that the hemagglutination exhibited by P. intermedia may be attributable to the fimbriae or the fimbrial-associated components.

Animals↗
PubMed1985

Three-dimensional structure of fimbriae determines specificity of immune response.

We recently described how a fraction of isolated fimbriae from a multifimbriated strain of Escherichia coli O7:K1:H6 (WF96) could be subdivided by sequential disaggregation in disrupting agents into individual subunits with different molecular weights. In this study, antibodies were raised in rabbits against these isolated fimbrial subunits and against purified intact WF96 fimbriae. These sera were tested by Western blot analysis or by enzyme-linked immunosorbent assays for reactivity against the following antigens: intact WF96 fimbriae, dissociated WF96 fimbriae, dissociated and reaggregated WF96 fimbriae, the WF96 21K fimbrial subunit, reaggregated WF96 21K subunits, the WF96 16K subunits, reaggregated WF96 16K subunits, intact fimbriae from four other E. coli strains, and deaggregated fimbriae from these strains. We found that antibody against intact WF96 fimbriae only reacted strongly with intact WF96 fimbriae, depolymerized and reaggregated WF96 fimbriae, or reaggregated fimbrial subunits; no reactions were evident with intact fimbriae from four other E. coli strains. Conversely, antisera prepared against the WF96 16K subunit and against the WF96 21K subunit did not react with intact WF96 fimbriae or with depolymerized and reaggregated WF96 fimbriae, but did react with homologous isolated subunits. One cross-reaction between fimbrial subunits was apparent: anti-WF96 16K subunit bound to a 21K subunit of deaggregated fimbriae, from another E. coli strain. Taken together, the findings indicate that the three-dimensional structure of the fimbrial preparation used to immunize animals determines the specificity of the immune response.

Electrophoresis, Polyacrylamide Gel↗