Flagellar Glycosylation: Current Advances

Hayakawa, Jumpei; Ishizuka, Morio

doi:10.5772/48352

Cited by 7 publications

(5 citation statements)

References 110 publications

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“…PAS-staining showed that both the FliC1 and FliC2 flagellins were glycosylated. This posttranscriptional modification was previously reported in other bacteria and archaea [ 13 , 14 ]. In those studies, glycosylation of flagellins was reported to be involved in stability, assembly, virulence, or motility of flagella or the flagellated microbes, albeit the functions are not fully understood.…”

Section: Discussionsupporting

confidence: 85%

Characterization of flagellins isolated from a highly motile strain of Lactobacillus agilis

et al. 2016

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Background: Most lactic acid bacteria are non-motile but some of them are flagellated and exhibit motility. So far, motile lactobacilli have rarely been studied, and characteristics of their flagellins are poorly understood. In this study, a highly motile strain of Lactobacillus agilis was recruited for transcriptional analysis and characterization of its flagellins. Results: Unlike another motile lactic acid bacteria of intestinal isolate, Lactobacillus ruminis, flagellar filaments of the L. agilis strain probably consist of two homologous but distinct flagellins. Glycosylation of the flagellar filaments and their resistance to heat, acid and SDS were also observed. The immunological activity of the flagellins was evaluated through the stimulation of Caco-2 cells. The results show that TLR5-stimulating activity of the protein is attenuated, likely due to an incomplete TLR5-recognition site.

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Section: Discussionsupporting

confidence: 85%

Characterization of flagellins isolated from a highly motile strain of Lactobacillus agilis

et al. 2016

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“…Flagellins are composed of highly conserved N and C regions (domains D0 and D1) that are positioned within the filament core of the flagellum, whereas the middle hypervariable region (domains D2 and D3) are exposed on the surface of the flagellum (Fig. 7D) (43). An alignment of flagellins from different bacterial species to which rSp0032 binds (S. typhimurium and V. diazotrophicus) and does not bind (B. subtilis) shows that the basis of this binding difference may be domain D2 that is mostly missing from B. subtilis flagellin (Fig.…”

Section: Discussionmentioning

confidence: 99%

A recombinant Sp185/333 protein from the purple sea urchin has multitasking binding activities towards certain microbes and PAMPs

et al. 2016

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The purple sea urchin, Strongylocentrotus purpuratus, possesses a sophisticated innate immune system that responds to microbes effectively by swift expression of the highly diverse Sp185/333 gene family. The Sp185/333 proteins are predicted to have anti-pathogen functions based on inducible gene expression and their significant sequence diversity. Sp185/333 proteins are all predicted to be intrinsically disordered and do not exhibit sequence similarities to other known proteins. To test the anti-pathogen hypothesis, a recombinant Sp185/333 protein, rSp0032, was evaluated and found to exhibit specific binding to marine Vibrio diazotrophicus and to Saccharomyces cerevisiae, but not to two Bacillus species. rSp0032 also binds to LPS, β-1,3-glucan and flagellin but not to peptidoglycan. rSp0032 binding to LPS can be competed by LPS, β-1,3-glucan and flagellin but not by peptidoglycan. We speculate that the predicted intrinsically disordered structure of rSp0032 may adapt to different conformations in binding to a limited number of PAMPs and pathogens. Given that rSp0032 binds to a range of targets, and that up to 260 different Sp185/333 proteins can be expressed per individual sea urchin, this family of immune response proteins may facilitate effective host protection against a broad array of potential pathogens encountered in the marine environment.

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“…Following the first description about 30 years ago, an increasing number of reports on flagella post-translational modifications from archaea and bacteria has been published and reviewed (9)(10)(11). In most bacterial flagellins described to date, the glycans are attached to the protein via an O-glycosidic linkage.…”

Section: Introductionmentioning

confidence: 99%

Flagellin Glycoproteomics of the Periodontitis Associated Pathogen Selenomonas sputigena Reveals Previously Not Described O-glycans and Rhamnose Fragment Rearrangement Occurring on the Glycopeptides

Rath

Schirmeister

Figl

et al. 2018

Molecular & Cellular Proteomics

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Flagellar Glycosylation: Current Advances

Cited by 7 publications

References 110 publications

Characterization of flagellins isolated from a highly motile strain of Lactobacillus agilis

Characterization of flagellins isolated from a highly motile strain of Lactobacillus agilis

A recombinant Sp185/333 protein from the purple sea urchin has multitasking binding activities towards certain microbes and PAMPs

Flagellin Glycoproteomics of the Periodontitis Associated Pathogen Selenomonas sputigena Reveals Previously Not Described O-glycans and Rhamnose Fragment Rearrangement Occurring on the Glycopeptides

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