We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
The Helicobacter pylori cell shape promoting protein Csd5 interacts with the cell wall, MurF, and the bacterial cytoskeleton.
- Authors
Blair, Kris M.; Mears, Kevin S.; Taylor, Jennifer A.; Fero, Jutta; Jones, Lisa A.; Gafken, Philip R.; Whitney, John C.; Salama, Nina R.
- Abstract
Summary: Chronic infection with Helicobacter pylori can lead to the development of gastric ulcers and stomach cancers. The helical cell shape of H. pylori promotes stomach colonization. Screens for loss of helical shape have identified several periplasmic peptidoglycan (PG) hydrolases and non‐enzymatic putative scaffolding proteins, including Csd5. Both over and under expression of the PG hydrolases perturb helical shape, but the mechanism used to coordinate and localize their enzymatic activities is not known. Using immunoprecipitation and mass spectrometry we identified Csd5 interactions with cytosolic proteins CcmA, a bactofilin required for helical shape, and MurF, a PG precursor synthase, as well as the inner membrane spanning ATP synthase. A combination of Csd5 domain deletions, point mutations, and transmembrane domain chimeras revealed that the N‐terminal transmembrane domain promotes MurF, CcmA, and ATP synthase interactions, while the C‐terminal SH3 domain mediates PG binding. We conclude that Csd5 promotes helical shape as part of a membrane associated, multi‐protein shape complex that includes interactions with the periplasmic cell wall, a PG precursor synthesis enzyme, the bacterial cytoskeleton, and ATP synthase. Csd5 is a non‐enzymatic protein that promotes helical cell shape and thus efficient colonization of the human host. We performed a structure–function analysis coupled to immunoprecipitation and mass spectrometry with identify Csd5 interaction partners and interaction domains. Here, we show that Csd5 is part of multi‐protein 'shapeosome' complex that spans the cytoplasmic membrane and mediates interactions with the periplasmic peptidoglycan (PG) cell wall, a cytoplasmic peptidoglycan precursor synthase, a putative bactofilin, and membrane embedded ATP synthase.
- Subjects
HELICOBACTER pylori; BACTERIAL cell walls; PEPTIDOGLYCAN hydrolase; IMMUNOPRECIPITATION; ADENOSINE triphosphatase
- Publication
Molecular Microbiology, 2018, Vol 110, Issue 1, p114
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/mmi.14087