Helicobacter pylori employs a general protein glycosylation system for the modification of outer membrane adhesins.

ABSTRACT: Helicobacter pylori infection is associated with the development of several gastric diseases including gastric cancer. To reach a long-term colonization in the host stomach, H. pylori employs multiple outer membrane adhesins for binding to the gastric mucosa. However, due to the redundancy of adhesins that complement the adhesive function of bacteria, targeting each individual adhesin alone usually achieves nonideal outcomes for preventing bacterial adhesion. Here, we report that key adhesins AlpA/B and BabA/B in H. pylori are modified by glycans and display a two-step molecular weight upshift pattern from the cytoplasm to the inner membrane and from the inner membrane to the outer membrane. Nevertheless, this upshift pattern is missing when the expression of some enzy

SUBMITTER: Teng KW 

PROVIDER: S-EPMC9553153 | biostudies-literature | 2022 Jan-Dec

REPOSITORIES: biostudies-literature