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The Helicobacter pylori cell shape promoting protein Csd5 interacts with the cell wall, MurF, and the bacterial

Kris M Blair1,2, Kevin S Mears1, Jennifer A Taylor1,3

  • 1Division of Human Biology, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave, Seattle, WA, 98109, USA.

Molecular Microbiology
|July 25, 2018
PubMed

Insights

Helicobacter pylori

Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Helicobacter pylori infection is linked to gastric ulcers and stomach cancers.
  • The helical shape of H. pylori is crucial for colonizing the stomach.
  • The precise mechanism coordinating peptidoglycan hydrolases for shape maintenance is unknown.

Purpose of the Study:

  • To investigate the role of Csd5 in maintaining the helical shape of H. pylori.
  • To identify proteins interacting with Csd5 and elucidate their function in cell shape.
  • To understand how Csd5 integrates periplasmic and cytosolic components for shape regulation.

Main Methods:

  • Immunoprecipitation and mass spectrometry to identify Csd5 interacting partners.
  • Domain deletions, point mutations, and transmembrane domain chimeras of Csd5.
  • Analysis of Csd5 interactions with cytosolic proteins (CcmA, MurF) and ATP synthase.

Main Results:

  • Csd5 interacts with CcmA (bactofilin), MurF (peptidoglycan precursor synthase), and ATP synthase.
  • The N-terminal transmembrane domain of Csd5 mediates interactions with MurF, CcmA, and ATP synthase.
  • The C-terminal SH3 domain of Csd5 is responsible for binding to peptidoglycan.

Conclusions:

  • Csd5 is a scaffolding protein essential for maintaining the helical shape of H. pylori.
  • Csd5 functions within a membrane-associated multi-protein complex.
  • This complex links periplasmic peptidoglycan, peptidoglycan synthesis, the bacterial cytoskeleton, and ATP synthase to regulate cell shape.

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