TheDrHemagglutinin, Afimbrial Adhesins AFA-IandAFA-III, and F1845Fimbriae ofUropathogenic andDiarrhea-Associated Escherichia coli Belong toaFamily ofHemagglutinins withDrReceptor Recognition (original) (raw)
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A hemagglutinin of uropathogenic Escherichia coli recognizes the Dr blood group antigen
Infection and immunity, 1988
A receptor moiety and blood group substance recognized by the O75X adhesin was studied. Well-defined erythrocytes representing different blood group systems and bacterial derivatives carrying plasmid pBJN406 encoding the adhesin were used in a direct hemagglutination assay. We showed that Dr blood group antigen, a component of the IFC blood group complex, is the receptor for the O75X fimbrialike adhesin (Dr hemagglutinin) of uropathogenic Escherichia coli. The molecule recognized by the Dr hemagglutinin on Dr blood group substance is a chloramphenicol-like structure. The inhibitory effect of the active compounds indicates that a tyrosine-containing molecule could be a natural receptor for the Dr hemagglutinin. Dr blood group substance was found in tubular basement membrane and Bowman's capsule of the human kidney. Specific attachment of a Dr hemagglutinin-positive bacterial strain to the kidney substructures was inhibited by chloramphenicol.
Infection and immunity, 1995
Uropathogenic Escherichia coli strains express a variety of adhesins, including members of the Dr adhesin family such as the Dr hemagglutinin, AFAI, and AFAIII. Certain E. coli adhesins (e.g., type 1 and S fimbriae) are known to mediate adherence to human polymorphonuclear leukocytes (PMNs). The receptor on erythrocytes for Dr family adhesins, decay accelerating factor, is also present on PMNs. To determine whether Dr family adhesins mediate adherence to PMNs and to characterize the specificity and consequences of such adherence, we studied agglutination of PMNs and adherence to PMNs by recombinant E. coli strains expressing various mannose-resistant or mannose-sensitive adhesins, in the presence or absence of inhibitors of adherence. Dr family adhesins, like type 1 fimbriae, mediated concentration-dependent adherence to PMNs. Adherence to PMNs was mannose sensitive for type 1 fimbriae but mannose resistant for Dr family adhesins. Chloramphenicol inhibited PMN adherence for the Dr h...
Molecular analysis and epidemiology of the Dr hemagglutinin of uropathogenic Escherichia coli
Infection and immunity, 1989
The genetic organization and epidemiology of Dr hemagglutinin was studied. Plasmids derived from pBJN406 and carrying transposon inserts were analyzed for their abilities to confer the mannose-resistant hemagglutination phenotype and expression of plasmid-encoded proteins. The 6.6-kilobase DNA fragment expressed five polypeptides with molecular masses of 15.5, 5, 18, 90, and 32 kilodaltons encoded by the draA, draB, draC, draD, and draE genes, respectively. Four genes, draA, draC, draD, and draE, were required for full mannose-resistant hemagglutination expression. Mutation in the draA gene, previously identified as encoding fimbrillin, resulted in loss of the adherence phenotype. We screened 658 strains isolated from patients with urinary tract infections (UTI) or from fecal samples for the presence of DNA sequences homologous to the draD gene. A significantly higher frequency of draD-related sequences was found among Escherichia coli strains from patients with cystitis than among ...
FEMS Microbiology Letters, 1994
We have recently demonstrated that cultured human intestinal HT-29 and Caco-2 cell lines express receptors for the F1845 fimbrial adhesin harbored by the diarrheagenic C1845 Escherichia coli (Kernéis et al., Infect. Immun. 59 (1991) 4013-4018). This adhesin belongs to a family of adhesins including the Dr hemagglutinin and the afimbrial adhesin AFA-I harbored by uropathogenic E. coli. Here we investigated the cell association of laboratory E. coli strains expressing the Dr hemagglutinin and the afimbrial adhesin AFA-I with human cultured enterocyte-like or mucosecreting cells. We observed that the E. coli strains bearing these adhesins adhere both to human intestinal undifferentiated and differentiated fluid-transporting cells, and to mucus-secreting cells. This result strongly suggests a high capacity of intestinal colonization for the uropathogenic E. coli harboring adhesive factors belonging to the Dr adhesin family. These results further corroborate the intestinal colonization by uropathogenic E. coli of the Dr family related to the fecal-perineal-urethral hypothesis of urinary tract infection pathogenesis.
Microbial Pathogenesis, 1986
Hoekstra and H. Bergmans. The role of fimbriae of uropathogenic Escherichia coli as carriers of the adhesin involved in mannose-resistant hemagglutination. Microbial Pathogenesis 1986 ; 1 : 51-56. The gene clusters encoding various P-fimbriae (F7 1 , F7 2, F9 and F11) were compared. Deletion plasmids that lack the gene encoding the fimbrillin were derived from these gene clusters. Introduction of these deletion plasmids into an E. coli K1 2 strain resulted in non-fimbriated cells that still showed mannose-resistant hemagglutination (MRHA). However when introduced into wild type E. coli strains no MRHA was observed. Derivatives of the wild type E, coli strains with reduced amounts of 0-antigen on the other hand showed MRHA when harbouring these plasmids. These results indicate that adhesion and presence of fimbriae are not necessarily linked. P-fimbriae could function as a carrier for the adhesin and thus endow adhesive capacity to cells with a complete O-antigen .
Journal of Clinical Microbiology, 2001
The recently demonstrated heterogeneity of these operons (L. Lalioui, M. Jouve, P. Gounon, and C. Le Bouguénec, Infect. Immun. 67:5048-5059, 1999) was used to develop a new PCR assay for detecting all the operons of the afa family with a single genetic tool. This PCR approach was validated by investigating three collections of human E. coli isolates originating from the stools of infants with diarrhea (88 strains), the urine of patients with pyelonephritis (97 strains), and the blood of cancer patients (115 strains). The results obtained with this single test and those previously obtained with several PCR assays were closely correlated. The AfaE adhesins encoded by the afa operons are variable, particularly with respect to the primary sequence encoded by the afaE gene. The receptor binding specificities have not been determined for all of these adhesins; some recognize the Dr blood group antigen (Afa/Dr ؉ adhesins) on the human decay-accelerating factor (DAF) as a receptor, and others (Afa/Dr ؊ adhesins) do not. Thus, the afa operons detected in this study were characterized by subtyping the afaE gene using specific PCRs. In addition, the DAF-binding capacities of as-yet-uncharacterized AfaE adhesins were tested by various cellular approaches. The afaE8 subtype (Afa/Dr ؊ adhesin) was found to predominate in afa-positive isolates from sepsis patients (75%); it was frequent in afa-positive pyelonephritis E. coli (55.5%) and absent from diarrhea-associated strains. In contrast, Afa/Dr ؉ strains (regardless of the afaE subtype) were associated with both diarrhea (100%) and extraintestinal infections (44 and 25% in afa-positive pyelonephritis and sepsis strains, respectively). These data suggest that there is an association between the subtype of AfaE adhesin and the physiological site of the infection caused by afa-positive strains.