<i>Helicobacter pylori</i> SabA Adhesin in Persistent Infection and Chronic Inflammation

TLDR

Helicobacter pylori adheres to the gastric mucosa via specific bacterial adhesins and host receptors. The study aims to identify sialyl-dimeric-Lewis x glycosphingolipid as a receptor for H. pylori and demonstrate its binding. The sialic acid–binding adhesin SabA was isolated using a retagging method and its sabA gene (JHP662/HP0725) was identified.

Abstract

Helicobacter pylori adherence in the human gastric mucosa involves specific bacterial adhesins and cognate host receptors. Here, we identify sialyl-dimeric-Lewis x glycosphingolipid as a receptor for H . pylori and show that H . pylori infection induced formation of sialyl-Lewis x antigens in gastric epithelium in humans and in a Rhesus monkey. The corresponding sialic acid–binding adhesin (SabA) was isolated with the “retagging” method, and the underlying sabA gene (JHP662/HP0725) was identified. The ability of many H . pylori strains to adhere to sialylated glycoconjugates expressed during chronic inflammation might thus contribute to virulence and the extraordinary chronicity of H . pylori infection.