The HP0256 gene product is involved in motility and cell envelope architecture of Helicobacter pylori
- Equal contributors
1 Department of Microbiology & Alimentary Pharmabiotic Centre, University College Cork, Ireland
2 Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan, Canada
3 School of Biosciences, University of Birmingham, Edgbaston, Birmingham, UK
4 Bacterial Microarray Group, Division of Cellular and Molecular Medicine, St George's University of London, Cranmer Terrace, London, UK
BMC Microbiology 2010, 10:106 doi:10.1186/1471-2180-10-106Published: 8 April 2010
Helicobacter pylori is the causative agent for gastritis, and peptic and duodenal ulcers. The bacterium displays 5-6 polar sheathed flagella that are essential for colonisation and persistence in the gastric mucosa. The biochemistry and genetics of flagellar biogenesis in H. pylori has not been fully elucidated. Bioinformatics analysis suggested that the gene HP0256, annotated as hypothetical, was a FliJ homologue. In Salmonella, FliJ is a chaperone escort protein for FlgN and FliT, two proteins that themselves display chaperone activity for components of the hook, the rod and the filament.
Ablation of the HP0256 gene in H. pylori significantly reduced motility. However, flagellin and hook protein synthesis was not affected in the HP0256 mutant. Transmission electron transmission microscopy revealed that the HP0256 mutant cells displayed a normal flagellum configuration, suggesting that HP0256 was not essential for assembly and polar localisation of the flagella in the cell. Interestingly, whole genome microarrays of an HP0256 mutant revealed transcriptional changes in a number of genes associated with the flagellar regulon and the cell envelope, such as outer membrane proteins and adhesins. Consistent with the array data, lack of the HP0256 gene significantly reduced adhesion and the inflammatory response in host cells.
We conclude that HP0256 is not a functional counterpart of FliJ in H. pylori. However, it is required for full motility and it is involved, possibly indirectly, in expression of outer membrane proteins and adhesins involved in pathogenesis and adhesion.