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At least 19 recordsLinked to original sources
PubMed1997

[Significance of the detection of fimbriae protein type adhesins on bacteria isolated in acute pyelonephritis in children].

A prospective bacteriological study in 50 children with acute pyelonephritis (APN) (32 girls and 18 boys) and 132 children with lower urinary tract infections (LUTI) (89 girls and 43 boys) was conducted from May to December 1993. Infection was defined by Kass' criteria and APN was defined by the clinical findings. C-Reactive Protein (CRP) assay and postcontrast computed tomography in the presence of a doubt concerning the diagnosis. Escherichia coli (EC) was the bacterial species most frequently isolated (76%). A systematic search for fimbriae protein adhesins (group PAP: pyelonephritis associated pil) on the EC was performed by haemagglutination (human group A red blood cells). 64% of EC possessed fimbriae protein adhesions in the APN group versus only 20% in the LUTI group. In children in whom an organic abnormality was demonstrated, the incidence of fimbriae protein-positive EC was 33% while in children with no organic abnormality, particularly without reflux, 89% of EC presented fimbriae protein. A statistically significant difference was demonstrated between these two groups (p < 0.01). The results of this study illustrate the important role of these adhesins in the development of APN. These adhesins facilitate countercurrent ascension of bacteria in the ureter towards the upper urinary tract and can make the bacteria resistant to certain antibiotics. Testing for fimbriae protein can be useful in clinical practice when investigating the aetiology of APN in the absence of demonstrated reflux. A latex test should soon be available to facilitate the detection of fimbriae protein.

Acute Disease↗
PubMed2004

Suppression of Salmonella enterica serovar Enteritidis excretion by intraocular vaccination with fimbriae proteins incorporated in liposomes.

Liposome-associated fimbriae antigens (SEF14 and SEF21) were prepared for intraocular immunization to seek protective efficacy for intestinal infection with Salmonella enterica serovar Enteritidis. Chickens were immunized intraocularly with the antigens at 8 and 10 weeks of age. Evidence of an IgA and IgG responses were found in the intestinal tract and in sera of these chickens. Antibody-secreting lymphocytes were detected in the Harderian gland of immunized chickens as determined by enzyme-linked immunospot assay. Two weeks after the booster immunization, the chickens were challenged orally with 1x10(7) live Salmonella Enteritidis, and fecal samples were examined for bacterial excretion from the intestinal tract. Significantly less fecal excretion of bacteria was observed in immunized chickens for 15 days after challenge. The numbers of bacteria in the intestinal contents (caecum and rectum) were also significantly lower in immunized chickens than in unimmunized controls. Detection of S. Enteritidis-specific DNA by the polymerase chain reaction was consistent with the bacterial observations. Intraocular immunization with liposome-associated SEF14 and SEF21 therefore elicits both systemic and mucosal antibody responses, so that bacterial colonization in the intestinal tract and excretion of S. Enteritidis in the feces are suppressed by immunization.

Animals↗
PubMed1986

Synthesis of a putative antigenic heptapeptide from Escherichia coli K88 ab protein fimbriae.

The heptapeptide Tyr-Arg-Glu-Asp-Met-Glu-Tyr-OMe, spanning region 213-219 of Escherichia coli K88 ab protein fimbriae, was synthesized with an overall yield of 37% using dicyclohexylcarbodiimide (DCC) and 1-hydroxybenzotriazole (HOBt) preactivation in all condensation reactions. The C-terminal was protected as the methyl ester. The protection scheme of N alpha-tert-butyloxycarbonyl-(Boc) and benzyl-(Bzl) or benzyloxycarbonyl (Z) groups for side chain protection was found to be orthogonal when a mixture of trifluoroacetic acid (TFA), phenol (PhOH) and p-cresol (CrOH) was used for repetitive deprotection. The final deprotection of Boc-Tyr(Bzl)-Arg(Z2)-Glu(Bzl)-Asp(Bzl)-Met-Glu(Bzl+ ++)-Tyr(Bzl)-OMe (17) was accomplished in 80% yield by prolonged treatment with hydrogen fluoride, dimethyl sulfide, p-cresol and p-thiocresol. The BSA-linked synthetic peptide was used in immunisation experiments on rabbits.

Antigens, Bacterial↗
PubMed1986

Synthesis of a putative subtype specific antigenic heptapeptide from Escherichia coli K88 ad protein fimbriae.

The heptapeptide methyl ester Phe-Asn-Glu-Asn-Met-Ala-Tyr-OMe covering the amino acid sequence of the region 213-219 of Escherichia Coli K88 ad protein fimbriae is synthesized using N alpha-t-butyloxycarbonyl-protection and benzyl groups for side-chain-protection. All condensation reactions are performed in 84-97% yield by preactivation of the protected amino acids by dicyclohexylcarbodiimide (DCC) and 1-hydroxybenzotriazole (HOBt), and reaction of the resulting active ester with amine in the presence of 4-methylmorpholine (NMM). A mechanism is proposed for the nitrile formation in the side-chain of activated asparagine, and the suppression of this side-reaction is investigated. The repetitive deprotection is performed in a mixture of trifluoroacetic acid (TFA), phenol and p-cresol to give the TFA salts in virtually quantitatively yields. The final deprotection of the heptapeptide is carried out in a mixture of 25% hydrogen fluoride (HF) and dimethyl sulfide (DMS) in an overall yield of 48%. The serological and conformational properties of the synthetic peptide are under investigation.

Antigens, Bacterial↗
PubMed1988

Investigation of minor components of Escherichia coli type 1 fimbriae: protein chemical and immunological aspects.

Three minor components of type 1 fimbriae, FimF, FimG and FimH have been characterized. These proteins are integrated in the fimbrial structure; are responsible for the adhesive properties of the fimbriae but are not necessary for the production of fimbriae. Fimbriae were purified from different clones harbouring various combinations of the fimF, fimG and fimH genes in addition to the fimA gene. The FimF, FimG and FimH proteins were identified by two dimentional gel electrophoresis. They were found to have molecular weights of 18.0 kDa, 17.0 kDa and 30 kDa, respectively. The ratio of FimF, FimG and FimH components to the major subunit was less than 1:100. The fimH protein especially was present in very small quantities. Sera raised against fimbriae from two of the clones (HB101/pPKL5 and HB101/pPKL4) were found by immunoblotting to be specific respectively for the major structural protein only (FimA), and for all components.

Amino Acid Sequence↗
PubMed1986

Synthesis of a proposed antigenic hexapeptide from Escherichia coli K88 protein fimbriae.

The hexapeptide Boc-Asp-Asp-Tyr-Arg-Gln-Lys-OMe is assembled by stepwise synthesis in solution with an overall yield of 44%. N alpha-boc-amino acids, protected with benzyl or benzyloxycarbonyl groups in the side-chains, are coupled as active estes of 1-hydroxybenzotriazole in mixtures of dichloromethane and N,N-dimethylformamide. N alpha-deprotection is accomplished with trifluoroacetic acid. Finally, hydrogenation with palladium on charcoal and ammonium formate produces the pure hexapeptide. A new one-pot synthesis of Boc-Arg(Z2) is described, and the use of this derivative in peptide coupling is studied. The synthetic peptide was coupled to BSA and used in direct immunication of rabbits.

Antigens, Bacterial↗
PubMed2000

Chronological recognition by chicken of antigenic polypeptides in Salmonella enteritidis with different plasmid profiles: relationship to infection rate.

The antigenic polypeptides in Salmonella Enteritidis (SE) were chronologically recognized by the chicken immune system, using Western immunoblotting. Broiler chicks challenged at three days of age with SE strain carrying the most prevalent plasmid profile of 14.1 and about (approximately) 50 kb were bled at 17, 24, 31, 38 and 45 days of age. Pooled sera of blood collected at each age was reacted by Western immunoblotting with banded polypeptides of three predominant SE strains that acquired the following respective plasmid profiles: 14.1 kb; 14.1 and approximately 50.0 kb; and 1.8, 14.1 and approximately 50.0 kb. The immunoblots of each pooled sera collected at a specific age against the three SE strains were similar. More specifically, the early immune response at 17 days of age had antibodies recognizing only one polypeptide in the three SE strains namely, the 35.8 kDa. At 24 or 31 days of age, the acquired immunity to infection had antibodies recognizing five similar polypeptides in the three SE strains namely, the 14.4 (fimbriae protein), 21.5 (fimbriae protein), 30.5, 35.8, and 66.2 kDa. At 38 and 45 days of age, the antibodies recognized additional polypeptides namely, the 41.5 and 55.6 kDa, respectively. The recognition of the 41.5 and 55.6 kDa polypeptides at 45 days of age was associated with higher invasiveness of SE to spleens and livers (15.6%) and in higher cecal colonization (59.4%) in comparison to absence of recognition to the two polypeptides at 31 days of age associated with low infectivity to spleens (0%), livers (3.1%), and ceca (9.4%).

Age Factors↗
PubMed1993

Adhesion of S-fimbriated Escherichia coli to brain glycolipids mediated by sfaA gene-encoded protein of S-fimbriae.

In an attempt to further assess the role of S-fimbriae in the pathogenesis of Escherichia coli meningitis, the adherence of E. coli strains with or without S-fimbriae were examined for this study to purified glycolipids using thin layer chromatography overlay assays. Only S-fimbriated E. coli strains bound to sulfatide, seminolipid, galactosyl ceramide, and lactosyl ceramide but not to gangliosides including sialyl neolacto-series and other neutral glycolipids. The binding of S-fimbriated E. coli to sulfatide was temperature dependent (i.e. maximal at 37 degrees C) and inhibited by S-fimbriae, anti-S-fimbriae, and anti-S-adhesin antibodies as well as by sulfatide, galactosyl ceramide, and lactosyl ceramide. E. coli transformants which lack the sfaA gene from the Sfa gene cluster showed no binding to the glycolipids, while other transformants lacking the adhesin gene sfaS or sfaG or H and mutants obtained by site-directed mutagenesis in the sfaS gene exhibited a similar binding to the glycolipids compared to the parent S-fimbriated strain. A large amount of sulfated glycolipids was demonstrated on brain endothelial cells and the binding of S-fimbriated E. coli to brain endothelial cells was inhibited by these glycolipids. These findings suggest that the binding of S-fimbriated E. coli to brain endothelial cells occurs in part via glycolipids containing terminal Gal(3SO4)beta-1 residues and in part by S-fimbriae protein SfaA. S-adhesin was not involved in the binding of S-fimbriae to these glycolipids.

Adhesins, Escherichia coli↗
PubMed1997

Cloning and sequence analysis of the fimbriae associated protein (fap) gene from Actinobacillus actinomycetemcomitans.

Fimbrial-associated protein, an attachment factor of Actinobacillus actinomycetemcomitans, was genetically analysed by cloning. The plasmid obtained was found to harbor a 1.7kb fragment which contained a 228bp open reading frame encoding 76 amino acids (7.970kDa). The fimbriae associated protein gene (fap) was strongly expressed in fimbriated A. actinomycetemcomitans 310a but not in non-fimbriated strains.

Aggregatibacter actinomycetemcomitans↗
PubMed1996

Secretion of type-1-fimbriae binding proteins from human neutrophil granulocytes.

Granule matrix proteins secreted from human neutrophils after ionomycin stimulation were separated by SDS-PAGE, blotted onto a polyvinylidene diflouride (PVDF) membrane and overlaid with the mannose-binding lectin concanavalin A (Con A) or Escherichia coli bacteria exposing type-I-fimbriae. Four proteins of approximately 30, 40, 70 and 80 kD, respectively, derived from both the azurophil and the specific granules were shown to expose mannose-containing structures by binding of Con A. Such reactivity was also shown for a 90-kD protein from the light membrane fraction enriched in plasma membrane and secretory vesicles. When blots of granule matrix proteins were exposed to type-I-fimbriated bacteria, a total of seven proteins was recognized; four of the five Con A-binding proteins (40, 70, 80 and 90 kD) was detected also by the bacteria in addition to three proteins not detected by Con A (50, 60 and 100 kD). The role of the secreted type-1-fimbriae binding proteins as anti-adhesin candidates is discussed.

Adult↗
PubMed2005

[Cloning and sequence analysis of recombinant fusion gene of Escherichia coli heat-liable enterotoxin B subunit and Actinobacillus actinomycetemcomitans fimbria associative protein].

OBJECTIVE: To clone the recombinant fusion gene of Escherichia coli heat-liable enterotoxin B subunit (Ltb) and Actinobacillus actinomycetemcomitans fimbria associative protein (Fap). METHODS: Two couples of primers were designed for PCR according to the known sequence of ltb and fap. The ltb and fap gene were obtained by amplification PCR technique from plasmid EWD299 of Escherichia coli and Actinobacillus actinomycetemcomitans 310 DNA respectively, and fused them by PCR. The fusion gene ltb-fap were cloning into plasmid pET28a(+). The recombined plasmid pET28a ltb-fap was transformed into Escherichia coli DH5alpha. The recombinant was screened and identified by restriction enzyme and PCR. The cloned gene was sequenced. RESULTS: The ltb-fap about 531bp in size was obtained successfully, and identified by PCR, restrictive enzyme and sequence analysis. CONCLUSION: The vector of pET28a ltb-fap was obtained.

Aggregatibacter actinomycetemcomitans↗
PubMed1988

Human antibody response to outer membrane proteins and fimbriae of Haemophilus influenzae type b.

We investigated the prevalence of antibodies in childrens' sera directed against outer membrane proteins (OMP) and fimbriae of Haemophilus influenzae type b. Invasive isolates of H. influenzae type b were enriched for fimbriae production; OMP and fimbriae were resolved by SDS-PAGE. After blotting to nitrocellulose, the proteins were incubated with homologous patient sera or with sera from healthy children. IgG antibodies bound to OMP were detected by immunoperoxidase staining. Immunoblotting was also performed using purified, nondenatured fimbriae as antigen. Nine of the 10 patients studied had antibodies in the acute serum directed against one or more of the OMP. Neither the acute nor the convalescent serum of the remaining patient contained antibodies against OMP. Antibodies against a greater number of OMP were present in the convalescent serum, in comparison to the acute serum, in 4 of the 10 patients. Five of 10 patients had antibodies against the purified fimbriae of an unrelated invasive isolate in either the acute or the convalescent serum. Acute sera from patients more frequently contained antibodies directed against OMP 60K (p less than or equal to 0.01) and OMP 51K (p less than or equal to 0.003) compared with the sera of healthy controls. In contrast, the sera of healthy children more frequently contained antibodies directed against OMP 40K (p less than or equal to 0.04). Sera from both patients and controls contained antibodies against commensal Haemophilus. We conclude that although antibodies against OMP are commonly present in healthy children, antibodies against certain OMP may be markers for susceptibility or protection.

Antibodies, Bacterial↗
PubMed1995

Purification and partial immunochemical characterization of proteins of fimbriae F107 from Escherichia coli isolated from edema disease of pigs.

The paper describes the isolation, purification and characterization of F107-fimbrial proteins, obtained by thermoelution from Escherichia coli 107/86. Isolation of the pure F107 protein was done by FPLC chromatography, employing Superose 12, Mono Q, and Phenyl-Superose columns. The highest purity of the F107 protein was achieved with Superose 12 HR 10/30. Purity checking by a HPLC system Waters 625 LC (Millipore) proved the absence of protein admixtures in a fraction from Superose 12. Analysis of the molar mass of F107 proteins by SDS PAGE revealed that F107 fimbriae consist of two proteins, one of M = 43 kDa (minor), and other of M = 18.9 kDa (major). Western blot analysis with rabbit polyclonal antiserum confirmed that the 18.9 kDa protein was the major characteristic unit of F107 fimbriae.

Animals↗
PubMed1987

Fimbria-associated proteins of Bacteroides loescheii PK1295 mediate intergeneric coaggregations.

Bacteroides loescheii PK1295 serves as a coaggregation bridge between Streptococcus sanguis 34 and Actinomyces israelii PK14, two gram-positive oral bacteria that are otherwise unable to coaggregate. Whereas coaggregation with S. sanguis 34 is inhibited by lactose, no simple sugar was found that inhibited coaggregation with A. israelii PK14. Coaggregation-defective (Cog-) mutants of B. loescheii PK1295 were isolated for the purpose of identifying the surface components responsible for the interaction with each coaggregation partner. Selection for spontaneously occurring Cog- mutants gave rise to two phenotypic classes of mutants. Type I lost the ability to coaggregate with S. sanguis 34, whereas type II failed to coaggregate with either S. sanguis 34 or A. israelii PK14. Purified fimbriae from the parent agglutinated cells of both partners, and agglutination with S. sanguis 34 was inhibited by lactose. Denaturing polyacrylamide gel electrophoresis and immunoblot analysis demonstrated the presence of both a 75- and a 43-kilodalton (kDa) protein associated with parental fimbriae, but only a 43-kDa protein was seen with fimbriae prepared from the type I mutant. Neither polypeptide was found in similar preparations from the type II mutants. Our data suggest that coaggregation of B. loescheii PK1295 with both gram-positive partners is mediated by fimbria-associated proteins present on the surface of the gram-negative organism and that the 75- and 43-kDa polypeptides are responsible for the recognition of S. sanguis 34 and A. israelii PK14 cells, respectively.

Actinomyces↗
PubMed2005

Major structural proteins of type 1 and type 3 Klebsiella fimbriae are effective protein carriers and immunogens in conjugates as revealed from their immunochemical characterization.

Fimbriae are filamentous structures present on the cell surface of many bacteria, including genus Klebsiella. The use of fimbriae as protein carriers in conjugates may allow to formulate effective multivalent vaccines and suitable diagnostics. However, the evidences have been reported that fimbriae may enhance the inflammatory response. This prompted us to examine the degree of cytokine induction by the type 1 and type 3 Klebsiella fimbriae and their conjugates. Fimbriae were assessed as carrier proteins for Escherichia coli K12 endotoxin core oligosaccharide. MALDI-MS revealed the molecular mass of fimbrial monomer major protein, which was 15,847 Da for type 1 and 18,574 Da for type 3 fimbriae of Klebsiella. These two types of fimbriae were moderate inductors of IL-6 and interferon and almost inactive with regard to the stimulation of TNF when tested in human whole blood assay. Coupling of fimbriae with E. coli K12 core oligosaccharide gave immunogenic conjugates with respect to a saccharide ligand and protein carrier, although only 10% of the pilin monomers possessed the attached oligosaccharide. Rabbit antiserum reacted with a broad spectrum of lipopolysaccharides, as measured by ELISA and immunoblotting assays. The antibodies against glycoconjugates were bactericidal for the wild, S-type bacteria of some species. Regarding the induction of cytokines by conjugates only the TNF level was noticeably elevated. These results prompt for the practical use of fimbriae, as effective protein carriers for conjugates to obtain broad-spectrum antisera for diagnostic applications.

Animals↗
PubMed1995

[Cloning of a cluster of genes encoding coli-surface antigen 6(CS6) of human enterotoxigenic E. coli].

A gene library was constructed from large plasmid DNA of wild strain E519/66A of human enterotoxigenic Escherichia coli (ETEC). Positive colonies containing CS6 antigen were obtained. The CS6 gene fragment was identified by restriction endonuclease mapping. It was approximately 4.6 kb in length and responsible for encoding CS6 genes and regulating the CS6 antigen. Two forms of fimbriae protein with different molecular weight were produced by the selected clones. Both of them could react with the same CS6 antiserum. So we expect to use the recombinant strain as candidate for human ETEC vaccine development, and it is also useful for further research on the expression and regulation of genes encoding CS6 fimbriae protein.

Antigens, Bacterial↗
PubMed1994

Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria.

A specialised system involved in a diverse array of functions, including the biogenesis of fimbriae, protein secretion and DNA uptake, has recently been found to be widespread in the eubacteria. These systems have in common several sets of related genes, including those encoding proteins containing leader sequences homologous to that of the type-4 fimbrial subunit (prepilin), a prepilin-type leader peptidase, a cytoplasmic nucleotide-binding protein, and other proteins located in the inner and outer membranes [Hobbs, M. and Mattick, J.S., Mol Microbiol. 10 (1993) 233-243]. Here, we show that Escherichia coli contains at least nine homologs of this system, and present complete sequence data for five of the genes involved (ppdD. hopB, hopC, hopD and pshM), as well as for an adjacent gene (nadC), which encodes quinolic acid phosphoribosyltransferase. Insertional mutagenesis of hopB and hopD failed to reveal any obvious effects on cell viability, morphogenesis of M13 phage, conjugative transfer of the F plasmid, or protein secretion.

Amino Acid Sequence↗