Structural highlights
Function[FLID_HELPY] Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. Essential to colonize and establish infection in gastric mucosa as a result of its essential role in motility. Has effect on flaA gene transcription. Publication Abstract from PubMedHelicobacter pylori is a pathogenic flagellated bacterium that infects the gastroduodenal mucosa and causes peptic ulcers in humans. FliD caps the distal end of the flagellar filament and is essential in filament growth. Moreover, FliD has been studied to diagnose and prevent H. pylori infection. Here, we report structure-based molecular studies of H. pylori FliD (hpFliD). A crystal structure of hpFliD at 2.6A resolution presents a four-domain (D2-D5) structure, where the D3 domain forms a central platform surrounded by the other three domains (D2, D4, and D5). hpFliD domains D2 and D3 structurally resemble those of FliD orthologs, whereas the D4 and D5 domains are exclusive to hpFliD. Moreover, our ELISA analysis using anti-H. pylori antibodies demonstrated that the hpFliD-specific D4 and D5 domains are highly antigenic compared to the D2 and D3 domains. Collectively, our structural and serological analyses underscore the structural role of hpFliD domains and provide a molecular basis for vaccine and diagnosis development. Structural analysis of the flagellar capping protein FliD from Helicobacter pylori.,Cho SY, Song WS, Oh HB, Kim HU, Jung HS, Yoon SI Biochem Biophys Res Commun. 2019 Jun 18;514(1):98-104. doi:, 10.1016/j.bbrc.2019.04.065. Epub 2019 Apr 22. PMID:31023530[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 06:50, 23 May 2019.