Structural Basis for Stabilization of the Hypervariable D3 Domain of Salmonella Flagellin upon Filament Formation

Muskotál, Adél; Seregélyes, Csaba; Sebestyén, Á.; Vonderviszt, Ferenc

doi:10.1016/j.jmb.2010.09.024

Cited by 23 publications

(48 citation statements)

References 23 publications

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“…Although no specific function has been assigned to the central region, its deletion leads to a reduction in filament stability (25), and previous studies demonstrated that the central region of flagellin is the surface-exposed antigenic portion of flagellar filaments (24,26). KEGG pathway analysis results also indicated that antigen processing-and presentation-related proteins were uniquely enriched with mFliC3, and similar results were observed uniquely for lysosome-related proteins with rFliC3 (Table 3).…”

Section: Discussionmentioning

confidence: 56%

Host Specificity of Flagellins from Segmented Filamentous Bacteria Affects Their Patterns of Interaction with Mouse Ileal Mucosal Proteins

Chen

Yin

Wang

et al. 2017

Appl Environ Microbiol

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Segmented filamentous bacteria (SFB) are known modulators of the mammalian immune system. Currently, the technology for investigating SFB culture in vitro is immature, and as a result, the mechanisms of SFB colonization and immune regulation are not yet fully elucidated. In this study, we investigated the gene diversity and host specificity of SFB flagellin genes. The fliC1 and fliC2 genes are relatively conserved, while the fliC3 and fliC4 genes are more variable, especially at the central and C-terminal regions. Host specificity analysis demonstrated that the fliC1 genes do not cluster together based on the host organism, whereas the fliC3 and fliC4 genes were host specific at the nucleotide and deduced amino acid levels. SFB flagellin protein expression in the ileum mucosa and cecal contents was detected by using fluorescence in situ hybridization (FISH) combined with immunohistochemical (IHC) analysis, immunoblotting, and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Although the purified SFB FliC3 protein originating from both mouse and rat was able to activate Toll-like receptor 5 (TLR5)-linked NF-B signaling, no host specificity was observed. Interestingly, the patterns of interaction with mouse ileum mucosal proteins were different for mouse FliC3 (mFliC3) and rat FliC3 (rFliC3). Gene Ontology (GO) and KEGG analyses indicated that more adherence-related proteins interacted with mFliC3, while more lysosome-and proteolysis-related proteins interacted with rFliC3. In vitro degradation experiments indicated that the stability of rFliC3 was lower than that of mFliC3 when they were incubated with mouse ileum mucosal proteins. In summary, the gene diversity and host specificity of SFB flagellin genes were investigated, and SFB flagellin expression was detected in gut samples.IMPORTANCE Since SFB genomes contain only one copy of each FliC gene, the diversity of FliC is representative of SFB strain diversity. Currently, little is known regarding the diversity and specificity of members of the group of SFB. The work presented herein demonstrates that select SFB strains, exhibiting unique FliC patterns, are present in a variety of mammalian hosts. SFB fliC genes were found to interact with a number of unique targets, providing further evidence for SFB host selection. Together, this work represents a major advancement in identifying SFB and delineating how members of the group of SFB interact with the host. Future examination of FliC genes will likely enhance our knowledge of intestinal colonization by the gut microbiota.KEYWORDS segmented filamentous bacteria, flagellin, host specificity, gene diversity, ileum mucosal proteins

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Section: Discussionmentioning

confidence: 56%

Host Specificity of Flagellins from Segmented Filamentous Bacteria Affects Their Patterns of Interaction with Mouse Ileal Mucosal Proteins

Chen

Yin

Wang

et al. 2017

Appl Environ Microbiol

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“…In the ∆D3_FliC two constituent fragments are connected by the short GLNSA linker upon removal of D3, resulting the continuous D2 domain [19]. In this work the GLNSA segment was replaced by oligopeptides containing the GRGDS pentapeptide.…”

Section: Design and Production Of Flagellin-rgd Fusionsmentioning

confidence: 99%

“…Natural deletion mutants or deletion variants constructed by genetic engineering in the central hypervariable region of flagellin are typically mechanically unstable and show altered polymorphic properties. Our previous results demonstrated that removal of the highly variable D3 domain of flagellin does not significantly influence filament stability, if the other domains remain undisturbed [19]. Thus, replacement of D3 may offer a promising approach for insertion of heterologous sequences, while preserving the ability to form stable filaments.…”

Section: Introductionmentioning

confidence: 98%

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Flagellin based biomimetic coatings: From cell-repellent surfaces to highly adhesive coatings

et al. 2016

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“…It was demonstrated that the variable central portion of flagellin, forming the surface-exposed D3 domain in the polymeric state, is not involved in filament formation and can be replaced by other proteins without destroying self-assembling ability [13,14]. The prototype of polymerizable flagellin-based enzymes (flagzymes) had been created by introducing the xylanase A (XynA) enzyme from Bacillus subtilis into the middle part of flagellin replacing D3 ( Fig.…”

Section: Introductionmentioning

confidence: 99%

Xylan-Degrading Catalytic Flagellar Nanorods

et al. 2015

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Flagellin, the main component of flagellar filaments, is a protein possessing polymerization ability. In this work a novel fusion construct of xylanase A from B. subtilis and Salmonella flagellin was created which is applicable to build xylan-degrading catalytic nanorods of high stability. The FliC-XynA chimera when overexpressed in a flagellin deficient Salmonella host strain was secreted into the culture medium by the flagellum-specific export machinery allowing easy purification. Filamentous assemblies displaying high surface density of catalytic sites were produced by ammonium-sulfate-induced polymerization. FliC-XynA nanorods were resistant to proteolytic degradation and preserved their enzymatic activity for a long period of time. Furnishing enzymes with self-assembling ability to build catalytic nanorods offers a promising alternative approach to enzyme immobilization onto nanostructured synthetic scaffolds.

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Structural Basis for Stabilization of the Hypervariable D3 Domain of Salmonella Flagellin upon Filament Formation

Cited by 23 publications

References 23 publications

Host Specificity of Flagellins from Segmented Filamentous Bacteria Affects Their Patterns of Interaction with Mouse Ileal Mucosal Proteins

Host Specificity of Flagellins from Segmented Filamentous Bacteria Affects Their Patterns of Interaction with Mouse Ileal Mucosal Proteins

Flagellin based biomimetic coatings: From cell-repellent surfaces to highly adhesive coatings

Xylan-Degrading Catalytic Flagellar Nanorods

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