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Helicobacter pylori adhesin BabA binds to blood group carbohydrates, influencing virulence and disease risk. Structural analysis reveals key binding site variations, offering insights into potential eradication therapies.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Immunology

Background:

  • The Helicobacter pylori adhesin BabA binds to ABO/Le(b) blood group carbohydrates, mediating bacterial attachment to gastric mucosa.
  • This interaction is a significant factor in H. pylori virulence, contributing to peptic ulcers and gastric cancer.
  • Functional diversity in BabA due to sequence variation is known, but its structural basis remains unclear.

Purpose of the Study:

  • To elucidate the structural-molecular determinants of BabA functional diversity.
  • To understand how BabA sequence variation affects binding affinity and specificity to blood group carbohydrates.
  • To explore potential therapeutic strategies targeting BabA-carbohydrate interactions.

Main Methods:

  • X-ray crystallography was used to determine the structures of representative BabA isoforms.
  • Structural analysis focused on the Le(b) binding site and associated diversity loops (DL1 and DL2).
  • In vivo studies in H. pylori-infected mice were conducted using N-acetylcysteine treatment.

Main Results:

  • X-ray structures revealed a polymorphic, three-pronged Le(b) binding site with two key diversity loops (DL1 and DL2) controlling binding affinity and ABO/O blood group preference.
  • Single amino acid substitutions in DL1 can alter H. pylori strain blood group preference.
  • The disulfide-clasped loop, crucial for binding ABO fucose, can be inactivated by reduction. N-acetylcysteine treatment reduced gastric mucosal neutrophil infiltration in infected mice.

Conclusions:

  • Structural insights into BabA polymorphism explain its functional diversity and variable binding preferences.
  • The disulfide-clasped loop's interaction with ABO fucose is a critical binding mechanism.
  • Redox modulation of BabA and N-acetylcysteine show promise for H. pylori eradication therapies.