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Lipoprotein Processing and Sorting in Helicobacter pylori.

Mark S McClain1, Bradley J Voss2, Timothy L Cover1,2,3

  • 1Department of Medicine, Vanderbilt University School of Medicine, Nashville, Tennessee, USA mark.s.mcclain@vumc.org timothy.l.cover@vumc.org.

Mbio
|May 21, 2020
PubMed
Summary
This summary is machine-generated.

Helicobacter pylori lipoprotein processing differs from E. coli, with Lnt being dispensable. Lipidation of CagT is crucial for the Cag type IV secretion system and CagA delivery in H. pylori.

Keywords:
Helicobacter pyloriToll-like receptor 2lipoproteinsposttranslational protein modificationtype IV secretion systems

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Bacterial Pathogenesis

Background:

  • Gram-negative bacteria, exemplified by Escherichia coli, utilize specific enzymes (Lgt, LspA, Lnt) and the Lol system for lipoprotein synthesis, modification, and localization.
  • Existing models of lipoprotein processing, primarily derived from E. coli, may not universally apply across all proteobacteria classes.
  • Helicobacter pylori, an Epsilonproteobacteria species, colonizes the human stomach and is associated with stomach cancer pathogenesis.

Purpose of the Study:

  • To systematically analyze lipoprotein processing and localization pathways in Helicobacter pylori.
  • To investigate the essentiality of lipoprotein synthesis enzymes (Lgt, LspA, Lnt) and Lol system components in H. pylori.
  • To determine the role of lipoprotein modification, specifically lipidation, in the function of the H. pylori Cag type IV secretion system (Cag T4SS).

Main Methods:

  • Functional complementation assays using E. coli mutant strains with H. pylori homologs of lipoprotein processing genes.
  • Mutagenesis studies and analysis of conditionally lethal H. pylori mutant strains to assess gene essentiality.
  • Comparative analysis of CagT protein modification and Cag T4SS activity in wild-type and mutant H. pylori strains.

Main Results:

  • H. pylori Lgt and LspA homologs are essential for growth, while the Lnt homolog is dispensable.
  • H. pylori LolA and LolC/LolE homologs are essential for bacterial viability.
  • Lipidation of CagT, a Cag T4SS component, is essential for its stability and the overall function of the Cag T4SS, including CagA delivery.

Conclusions:

  • Lipoprotein synthesis and localization pathways in H. pylori significantly diverge from the canonical E. coli model.
  • The lipidation of CagT is a critical step for H. pylori Cag T4SS activity and pathogenesis.
  • This study provides the first comprehensive analysis of H. pylori lipoprotein production and localization, highlighting unique mechanisms in Epsilonproteobacteria.