Antigenic relationships among type-1 fimbriae of Enterobacteriaceae revealed by immuno-electronmicroscopy

Adegbola, R. A.; OLD, D. C.

doi:10.1099/00222615-24-1-21

Cited by 11 publications

(5 citation statements)

References 14 publications

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“…Most of the antibodies evoked with the purified fimbrial preparation were directed primarily at the structural FimA subunit (which constitutes over 95% of the total fimbrial proteins), but none appeared to be directed at the minor FimH adhesive component. Furthermore, the FimA subunit was antigenically heterogeneous even among strains of the same species (57,58). Thus, the protection afforded by employing purified type 1 fimbriae as a vaccine was limited to relatively a few bacterial strains expressing homologous type 1 fimbriae.…”

Section: Discussionmentioning

confidence: 93%

Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection.

Thankavel

Madison²,

Ikeda³

et al. 1997

J. Clin. Invest.

136

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The FimH subunit of type 1-fimbriated Escherichia coli has been implicated as an important determinant of bacterial adherence and colonization of the urinary tract. Here, we sought to localize the functionally important domain(s) within the FimH molecule and to determine if antibodies against this domain would block adherence of type 1-fimbriated E. coli to the bladder mucosa in situ and in vivo in an established mouse model of cystitis. We generated translational fusion proteins of disparate regions of the FimH molecule with an affinity tag MalE, and tested each of the fusion products in vitro for functional activity. The minimum region responsible for binding mouse bladder epithelial cells and a soluble mannoprotein, horseradish peroxidase, was contained within residues 1-100 of the FimH molecule. We validated and extended these findings by demonstrating that antibodies directed at the putative binding region of

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Section: Discussionmentioning

confidence: 93%

Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection.

Thankavel

Madison²,

Ikeda³

et al. 1997

J. Clin. Invest.

136

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“…In each, the fim gene cluster is comprised of genes encoding structural components of the assembled appendages as well as genes necessary for the ordered assembly of the fimbriae. The genes and their products in E. coli and K. pneumoniae are closely related, and the fimbriae of the two species have been shown to be immunologically cross-reactive (1,10,34). However, strains of K. pneumoniae possess a gene, fimK, that is absent from the E. coli fim gene cluster and has been proposed to play a role in fim gene regulation (36).…”

Section: Discussionmentioning

confidence: 99%

FimA, FimF, and FimH Are Necessary for Assembly of Type 1 Fimbriae on Salmonella enterica Serovar Typhimurium

2012

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ABSTRACTSalmonella entericaserovar Typhimurium is a Gram-negative member of the familyEnterobacteriaceaeand is a common cause of bacterial food poisoning in humans. The fimbrial appendages are found on the surface of many enteric bacteria and enable the bacteria to bind to eukaryotic cells.S. Typhimurium type 1 fimbriae are characterized by mannose-sensitive hemagglutination and are assembled via the chaperone/usher pathway.S. Typhimurium type 1 fimbrial proteins are encoded by thefimgene cluster (fimAICDHFZYW), withfimAICDHFexpressed as a single transcriptional unit. The structural components of the fimbriae are FimA (major subunit), FimI, FimH (adhesin), and FimF (adaptor). In order to determine which components are required for fimbrial formation inS. Typhimurium, mutations infimA,fimI,fimH, andfimFwere constructed and examined for their ability to produce surface-assembled fimbriae.S. Typhimurium SL1344ΔfimA, -ΔfimH, and -ΔfimFmutants were unable to assemble fimbriae, indicating that these genes are necessary for fimbrial production inS. Typhimurium. However, SL1344ΔfimIwas able to assemble fimbriae. InEscherichia colitype 1 and Pap fimbriae, at least two adaptors are expressed in addition to the adhesins. However,E. colitype 1 and Pap fimbriae have been reported to be able to assemble fimbriae in the absence of these proteins. These results suggest differences between theS. Typhimurium type 1 fimbrial system and theE. colitype 1 and Pap fimbrial systems.

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“…level of homology (88%) in the primary structure between FimH proteins of E. coli and K pneumoniae examined so far (18), there are remarkable differences in the sizes and antigenic properties of FimA proteins among different species of enterobacteria (4,17). It is conceivable that the heterogeneity among the major components of the fimbrial shaft of each species results in the imposition of particular conformational constrains on its FimH proteins.…”

Section: Discussionmentioning

confidence: 98%

Type 1 fimbrial shafts of Escherichia coli and Klebsiella pneumoniae influence sugar-binding specificities of their FimH adhesins

et al. 1994

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The type 1 fimbriae of enterobacteria comprise FimA, which constitutes most of the fimbrial shaft, and a cassette of three minor ancillary subunits including FimH, the mannose-binding moiety. The sugar-binding specificities of Escherichia coli and KkebsieUla pneumoniae type 1 fimbriae were examined by determining the relative activities of two aromatic mannosides in inhibiting the yeast aggregation caused by the fimbriated bacteria. 4-Methylumbelliferyl a-mannoside (MeUmbatMan) was approximately 10-fold more effective than p-nitrophenyl oa-mannoside (p-NPaMan) in inhibiting the yeast aggregation caused by the recombinant

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Antigenic relationships among type-1 fimbriae of Enterobacteriaceae revealed by immuno-electronmicroscopy

Cited by 11 publications

References 14 publications

Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection.

Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection.

FimA, FimF, and FimH Are Necessary for Assembly of Type 1 Fimbriae on Salmonella enterica Serovar Typhimurium

Type 1 fimbrial shafts of Escherichia coli and Klebsiella pneumoniae influence sugar-binding specificities of their FimH adhesins

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