Characterization of FimH Adhesins Expressed by
            <i>Salmonella enterica</i>
            Serovar Gallinarum Biovars Gallinarum and Pullorum: Reconstitution of Mannose-Binding Properties by Single Amino Acid Substitution

Kisiela, Dagmara I.; Sapeta, Anna; Kuczkowski, Maciej; Stefaniak, Tadeusz; Wieliczko, Alina; Ugorski, Maciej

doi:10.1128/iai.73.9.6187-6190.2005

Cited by 42 publications

(41 citation statements)

References 20 publications

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“…Our previous study of FimH sequences from different avian and human isolates of S. Enteritidis revealed that all the analysed isolates express the same allelic variant of FimH (Kisiela et al, 2005b), which was first found in the S. Typhimurium SL1344 strain by Boddicker et al (2002). This strain of S. Typhimurium bound weakly to HEp-2 cells, in contrast to the high-adhesive strain LB5010, which attached strongly to those cells.…”

Section: Discussionmentioning

confidence: 87%

“…They were identified by Western blotting using primary antimyc mAb 9E10 (ATCC, no. CRL-1729) and alkaline phosphataseconjugated goat anti-mouse immunoglobulins (Dako) or rabbit polyclonal antibodies directed against FimH (Kisiela et al, 2005b) and horseradish peroxidase (HRP)-conjugated goat anti-rabbit immunoglobulins (Sigma). The binding of the scFimH proteins to RNase B (Sigma), HRP (Sigma) and mannan-BSA was analysed by far-Western blotting.…”

Section: Methodsmentioning

confidence: 99%

“…Sequencing of the fimH genes from different avian and human S. Enteritidis isolates (Kisiela et al, 2005b) shows that all the analysed strains represent the low-adhesive variant of S. Typhimurium described by Boddicker et al (2002). The functional characterization of low-adhesive variants of FimH proteins from S. Enteritidis and S. Typhimurium reveals that FimH adhesins bind equally to human colon carcinoma and bladder cancer cells (Kisiela et al, 2006).…”

Section: Introductionmentioning

confidence: 94%

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The high-adhesive properties of the FimH adhesin of Salmonella enterica serovar Enteritidis are determined by a single F118S substitution

et al. 2010

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The binding properties of low-and high-adhesive forms of FimH adhesins from Salmonella enterica serovars Enteritidis and Typhimurium (S. Enteritidis and S. Typhimurium) were studied using chimeric proteins containing an additional peptide that represents an N-terminal extension of the FimF protein. This modification, by taking advantage of a donor strand exchange mechanism, closes the hydrophobic groove in the fimbrial domain of the FimH adhesin. Such selfcomplemented adhesins (scFimH) did not form aggregates and were more stable (resistant to proteolytic cleavage) than native FimH. High-adhesive variants of scFimH proteins, with alanine at position 61 and serine at position 118, were obtained by site-directed mutagenesis of fimH genes from low-adhesive variants of S. Enteritidis and S. Typhimurium, with glycine at position 61 and phenylalanine at position 118. Direct kinetic analysis using surface plasmon resonance (SPR) and glycoproteins carrying high-mannose carbohydrate chains (RNase B, horseradish peroxidase and mannan-BSA) revealed the existence of high-and low-adhesive allelic variants, not only in S. Typhimurium but also in S. Enteritidis. Using two additional mutants of low-adhesive FimH protein from S. Enteritidis (Gly61Ala and Phe118Ser), SPR analysis pointed to Ser118 as the major determinant of the high-adhesive phenotype of type 1 fimbriae from S. Enteritidis. These studies demonstrated for the first time that the functional differences observed with whole fimbriated bacteria could be reproduced at the level of purified adhesin. They strongly suggest that the adhesive properties of type 1 fimbriae are determined only by structural differences in the FimH proteins and are not influenced by the fimbrial shaft on which the adhesin is located.

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Section: Discussionmentioning

confidence: 87%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 94%

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The high-adhesive properties of the FimH adhesin of Salmonella enterica serovar Enteritidis are determined by a single F118S substitution

et al. 2010

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“…General suitability of the models is supported by the fact that the threonine residue (Thr-56) that is critical for mannose binding in Salmonella FimH (35) mapped to the top loops of the N-terminal domain exactly where the mannose-binding pocket is predicted to be located. Additional support for the model comes from the similarity of the distribution pattern of binding-enhancing mutations along the tertiary structure of Salmonella FimH with the pattern shown for E. coli FimH.…”

Section: Discussionmentioning

confidence: 99%

Allosteric Catch Bond Properties of the FimH Adhesin from Salmonella enterica Serovar Typhimurium

Kisiela

Kramer

Tchesnokova

et al. 2011

Journal of Biological Chemistry

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Despite sharing the name and the ability to mediate mannosesensitive adhesion, the type 1 fimbrial FimH adhesins of Salmonella Typhimurium and Escherichia coli share only 15% sequence identity. In the present study, we demonstrate that even with this limited identity in primary sequence, these two proteins share remarkable similarity of complex receptor binding and structural properties. In silico simulations suggest that, like E. coli FimH, Salmonella FimH has a two-domain tertiary structure topology, with a mannose-binding pocket located on the apex of a lectin domain. Structural analysis of mutations that enhance S. Typhimurium FimH binding to eukaryotic cells and mannose-BSA demonstrated that they are not located proximal to the predicted mannose-binding pocket but rather occur in the vicinity of the predicted interface between the lectin and pilin domains of the adhesin. This implies that the functional effect of such mutations is indirect and probably allosteric in nature. By analogy with E. coli FimH, we suggest that Salmonella FimH functions as an allosteric catch bond adhesin, where shear-induced separation of the lectin and pilin domains results in a shift from a low affinity to a high affinity binding conformation of the lectin domain. Indeed, we observed shear-enhanced binding of whole bacteria expressing S. Typhimurium type 1 fimbriae. In addition, we observed that anti-FimH antibodies activate rather than inhibit S. Typhimurium FimH mannose binding, consistent with the allosteric catch bond properties of this adhesin.Terminal mannosyl residues are among the most common components of oligosaccharides in cell membrane glycoproteins of eukaryotic organisms, including humans. In particular, terminally exposed mannose is ubiquitous in high mannose and hybrid types of N-linked oligosaccharides. Thus, it is not surprising that a great number of bacterial commensals and pathogens have evolved a variety of adhesive organelles that specifically recognize terminal mannose, allowing them to attach to a wide spectrum of mammalian cells (1-5). For example, among different species of the Enterobacteriaceae, mannose-specific adhesion is mediated by type 1 fimbriae, relatively rigid fibrillar appendages of 0.5-2 m in length with the mannose-binding protein (adhesin) positioned on the fimbrial tip. However, despite the general topological similarities, type 1 fimbriae in some bacterial species (e.g. Escherichia coli, Salmonella enterica, and Serratia marcescens) are not closely related genetically (6 -9) and probably have evolved independently from each other as a result of convergent evolution driven toward the ability to bind terminal mannose, highlighting the physiological importance of mannose-specific bacterial adhesion.

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“…This designation can be confusing, since naturally occurring mutations resulting in a single-amino-acid substitution in the S. enterica FimH tip adhesin can result in a loss of mannose-sensitive hemagglutination (175). Furthermore, gene clusters encoding type 1 fimbriae of S. enterica and E. coli are both referred to as fim operons, although these are not orthologous gene clusters.…”

Section: The ␥-Fimbriaementioning

confidence: 99%

Evolution of the Chaperone/Usher Assembly Pathway: Fimbrial Classification Goes Greek

Nuccio

Bäumler

2007

Microbiol Mol Biol Rev

298

456

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SUMMARY Many Proteobacteria use the chaperone/usher pathway to assemble proteinaceous filaments on the bacterial surface. These filaments can curl into fimbrial or nonfimbrial surface structures (e.g., a capsule or spore coat). This article reviews the phylogeny of operons belonging to the chaperone/usher assembly class to explore the utility of establishing a scheme for subdividing them into clades of phylogenetically related gene clusters. Based on usher amino acid sequence comparisons, our analysis shows that the chaperone/usher assembly class is subdivided into six major phylogenetic clades, which we have termed α-, β-, γ-, κ-, π-, and σ-fimbriae. Members of each clade share related operon structures and encode fimbrial subunits with similar protein domains. The proposed classification system offers a simple and convenient method for assigning newly discovered chaperone/usher systems to one of the six major phylogenetic groups.

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Characterization of FimH Adhesins Expressed by Salmonella enterica Serovar Gallinarum Biovars Gallinarum and Pullorum: Reconstitution of Mannose-Binding Properties by Single Amino Acid Substitution

Cited by 42 publications

References 20 publications

The high-adhesive properties of the FimH adhesin of Salmonella enterica serovar Enteritidis are determined by a single F118S substitution

The high-adhesive properties of the FimH adhesin of Salmonella enterica serovar Enteritidis are determined by a single F118S substitution

Allosteric Catch Bond Properties of the FimH Adhesin from Salmonella enterica Serovar Typhimurium

Evolution of the Chaperone/Usher Assembly Pathway: Fimbrial Classification Goes Greek

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