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Titel:Insights Into the Helical Shape Complex of Helicobacter pylori
Autor:Holtrup, Sven
Weitere Verfasser:Greger, Maximilian; Mayer, Benjamin; Specht, Mara; Waidner, Barbara
Veröffentlicht:2022
URI:https://archiv.ub.uni-marburg.de/es/2023/0028
URN: urn:nbn:de:hebis:04-es2023-00281
DOI: https://doi.org/10.3389/fmicb.2022.929194
DDC:540 Chemie
Publikationsdatum:2023-04-03
Lizenz:https://creativecommons.org/licenses/by/4.0

Dokument

Schlagwörter:
structured illumination microscopy, bactofilin, cell shape, single-molecule tracking, Helicobacter pylori

Summary:
One important factor that promotes the colonization of the upper digestive system of the human pathogen Helicobacter pylori is its helical cell shape. The bacteria cell shape is predominantly defined by its peptidoglycan cell wall. In rod-shaped species, PG synthesis is mediated by two dynamic molecular machines that facilitate growth along the perpendicular axis and the septum, called the elongasome and the divisome, respectively. Furthermore, many bacteria evolved additional mechanisms to locally change PG synthesis patterns to generate diverse cell shapes. Recent work characterizing cell shape mutants of Helicobacter pylori revealed a novel mechanism for the generation of a twisted helix from a rod, including PG-modifying enzymes as well as additional proteins such as the bactofilin homolog CcmA or the membrane proteins Csd5 and Csd7. In this study, we investigate the localization and dynamics of CcmA and Csd7 using live-cell imaging. We also address the question of how these change in the presence or absence of the putative interaction partners.


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