Localization of a Cardiolipin Synthase in <i>Helicobacter pylori</i> and Its Impact on the Flagellar Sheath Proteome
<i>Helicobacter pylori</i>, which colonizes the human gastric mucosa, uses a cluster of polar, sheathed flagella to swim across the mucous layer of the stomach. The function and biogenesis of the <i>H. pylori</i> flagellar sheath are poorly understood. Cardiolipin is a phosph...
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2025-07-01
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| author | Doreen Nguyen Nathan East Vincent J. Starai Timothy R. Hoover |
| author_facet | Doreen Nguyen Nathan East Vincent J. Starai Timothy R. Hoover |
| author_sort | Doreen Nguyen |
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| description | <i>Helicobacter pylori</i>, which colonizes the human gastric mucosa, uses a cluster of polar, sheathed flagella to swim across the mucous layer of the stomach. The function and biogenesis of the <i>H. pylori</i> flagellar sheath are poorly understood. Cardiolipin is a phospholipid that accumulates in regions of the membrane that have negative curvature, such as the cell pole, cell septum, and flagellar sheath. The final step in cardiolipin biosynthesis is catalyzed by cardiolipin synthase. <i>H. pylori</i> has at least two cardiolipin synthases, one of which is cardiolipin synthase C (ClsC). Bioinformatic analysis revealed that homologs of <i>H. pylori</i> ClsC are restricted to <i>Helicobacter</i> species that have sheathed flagella and the ClsC homologs are predicted lipoproteins. Fluorescence microscopy revealed that a ClsC super-folder green fluorescent protein localized to the cell pole and cell septum in <i>H. pylori</i> G27. Comparing the proteomes of isolated sheathed flagella from the <i>H. pylori</i> B128 wild type and a <i>clsC</i>::<i>cat</i> mutant, we identified five proteins that were absent in the mutant flagellum preparations. One of the proteins was FaaA, an autotransporter that localizes to the flagellar sheath. These findings suggest that the localization of FaaA and possibly other proteins to the flagellar sheath is dependent on ClsC. |
| format | Article |
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| institution | Kabale University |
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| language | English |
| publishDate | 2025-07-01 |
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| spelling | doaj-art-ce8193c0b0fd43bc8541a935e9f097622025-08-20T03:36:18ZengMDPI AGMicrobiology Research2036-74812025-07-0116715510.3390/microbiolres16070155Localization of a Cardiolipin Synthase in <i>Helicobacter pylori</i> and Its Impact on the Flagellar Sheath ProteomeDoreen Nguyen0Nathan East1Vincent J. Starai2Timothy R. Hoover3Department of Microbiology, University of Georgia, Athens, GA 30602, USADepartment of Microbiology, University of Georgia, Athens, GA 30602, USADepartment of Microbiology, University of Georgia, Athens, GA 30602, USADepartment of Microbiology, University of Georgia, Athens, GA 30602, USA<i>Helicobacter pylori</i>, which colonizes the human gastric mucosa, uses a cluster of polar, sheathed flagella to swim across the mucous layer of the stomach. The function and biogenesis of the <i>H. pylori</i> flagellar sheath are poorly understood. Cardiolipin is a phospholipid that accumulates in regions of the membrane that have negative curvature, such as the cell pole, cell septum, and flagellar sheath. The final step in cardiolipin biosynthesis is catalyzed by cardiolipin synthase. <i>H. pylori</i> has at least two cardiolipin synthases, one of which is cardiolipin synthase C (ClsC). Bioinformatic analysis revealed that homologs of <i>H. pylori</i> ClsC are restricted to <i>Helicobacter</i> species that have sheathed flagella and the ClsC homologs are predicted lipoproteins. Fluorescence microscopy revealed that a ClsC super-folder green fluorescent protein localized to the cell pole and cell septum in <i>H. pylori</i> G27. Comparing the proteomes of isolated sheathed flagella from the <i>H. pylori</i> B128 wild type and a <i>clsC</i>::<i>cat</i> mutant, we identified five proteins that were absent in the mutant flagellum preparations. One of the proteins was FaaA, an autotransporter that localizes to the flagellar sheath. These findings suggest that the localization of FaaA and possibly other proteins to the flagellar sheath is dependent on ClsC.https://www.mdpi.com/2036-7481/16/7/155<i>Helicobacter pylori</i>cardiolipin synthasecardiolipinflagellar sheath |
| spellingShingle | Doreen Nguyen Nathan East Vincent J. Starai Timothy R. Hoover Localization of a Cardiolipin Synthase in <i>Helicobacter pylori</i> and Its Impact on the Flagellar Sheath Proteome Microbiology Research <i>Helicobacter pylori</i> cardiolipin synthase cardiolipin flagellar sheath |
| title | Localization of a Cardiolipin Synthase in <i>Helicobacter pylori</i> and Its Impact on the Flagellar Sheath Proteome |
| title_full | Localization of a Cardiolipin Synthase in <i>Helicobacter pylori</i> and Its Impact on the Flagellar Sheath Proteome |
| title_fullStr | Localization of a Cardiolipin Synthase in <i>Helicobacter pylori</i> and Its Impact on the Flagellar Sheath Proteome |
| title_full_unstemmed | Localization of a Cardiolipin Synthase in <i>Helicobacter pylori</i> and Its Impact on the Flagellar Sheath Proteome |
| title_short | Localization of a Cardiolipin Synthase in <i>Helicobacter pylori</i> and Its Impact on the Flagellar Sheath Proteome |
| title_sort | localization of a cardiolipin synthase in i helicobacter pylori i and its impact on the flagellar sheath proteome |
| topic | <i>Helicobacter pylori</i> cardiolipin synthase cardiolipin flagellar sheath |
| url | https://www.mdpi.com/2036-7481/16/7/155 |
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