Abstract
Although flagellar motility is essential for the colonisation of the stomach by Helicobacter pylori, little is known about the regulation of flagellar biosynthesis in this organism. We have identified a gene in H. pylori, designated fliI, whose deduced amino acid sequence revealed extensive homology with the FliI/LcrB/InvC family of proteins which energise the export of flagellar and other virulence factors in several bacterial species. An isogenic mutant of fliI was non-motile and synthesised reduced amounts of flagellin and hook protein subunits. The majority (> 99%) of mutant cells were completely aflagellate. These results suggest that FliI is a novel ATPase involved in flagellar export in H. pylori.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / physiology*
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Amino Acid Sequence
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Bacterial Proteins / analysis
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Bacterial Proteins / genetics
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Bacterial Proteins / physiology*
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Flagella / metabolism*
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Flagellin / analysis
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Genes, Bacterial / genetics
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Helicobacter pylori / enzymology*
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Helicobacter pylori / genetics
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Helicobacter pylori / ultrastructure
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Molecular Sequence Data
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Mutation
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Proteins / genetics
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Proteins / physiology*
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Proton-Translocating ATPases*
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
Substances
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Bacterial Proteins
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FlgE protein, Bacteria
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Proteins
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Flagellin
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flaA protein, bacteria
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fliI protein, bacteria
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flaB flagellin
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Adenosine Triphosphatases
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Proton-Translocating ATPases