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Updated: Jul 5, 2025

One-step Negative Chromatographic Purification of Helicobacter pylori Neutrophil-activating Protein Overexpressed in Escherichia coli in Batch Mode
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One-step Negative Chromatographic Purification of Helicobacter pylori Neutrophil-activating Protein Overexpressed in Escherichia coli in Batch Mode

Published on: June 18, 2016

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LOX-1 acts as an N6-methyladenosine-regulated receptor for Helicobacter pylori by binding to the bacterial catalase

Judeng Zeng1,2,3, Chuan Xie1,2,4, Ziheng Huang1,2,3

  • 1State Key Laboratory of Digestive Diseases, Li Ka Shing Institute of Health Sciences, The Chinese University of Hong Kong, Hong Kong Special Administrative Region, Hong Kong, China.

Nature Communications
|January 22, 2024
PubMed

Insights

N6-methyladenosine (m6A) RNA modification in host cells helps fight Helicobacter pylori infection. By reducing LOX-1 levels, m6A hinders bacterial adhesion and colonization.

Area of Science:

  • Molecular Biology
  • Microbiology
  • Immunology

Background:

  • The role of N6-methyladenosine (m6A) RNA modification in host responses to bacterial infections remains largely unknown.
  • Helicobacter pylori is a significant human pathogen that colonizes the gastric epithelium.

Purpose of the Study:

  • To investigate the role of m6A modification in host cells during Helicobacter pylori infection.
  • To identify key host targets regulated by m6A during H. pylori infection and elucidate their function.

Main Methods:

  • Analysis of m6A methylase expression and m6A levels in gastric epithelial cells upon H. pylori infection.
  • Utilizing Mettl3 hemizygous deletion mice and small interfering RNAs to modulate m6A methylase activity.
  • Identifying m6A-modified mRNA targets using sequencing techniques.
  • Assessing the impact of LOX-1 modulation on H. pylori adhesion and colonization.
  • Investigating the role of bacterial catalase in H. pylori adhesion.

Main Results:

  • H. pylori infection upregulates host m6A methylases and increases cellular m6A levels.
  • Reduced m6A methylase activity enhances H. pylori colonization, indicating a protective role for m6A.
  • LOX-1 mRNA was identified as a key m6A target, with m6A modification leading to its destabilization and reduced protein levels.
  • LOX-1 functions as a receptor for H. pylori catalase, facilitating bacterial adhesion.
  • Inhibition or genetic ablation of LOX-1, as well as deletion of bacterial catalase, significantly reduces H. pylori colonization and adhesion.

Conclusions:

  • Host m6A modification of LOX-1 mRNA is a critical defense mechanism against H. pylori infection.
  • Downregulation of LOX-1 via m6A modification reduces bacterial adhesion by limiting the interaction with H. pylori catalase.
  • These findings highlight the importance of epitranscriptomic modifications in host-pathogen interactions and suggest potential therapeutic targets.

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