An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection.

ABSTRACT: Helicobacter pylori persistently colonizes about half the human population and contributes to the development of peptic ulcer disease and gastric cancer. This organism has evolved means to structurally alter its surface characteristics to evade innate and adaptive immune responses. H. pylori produces LPS O-antigen units that can be posttranslationally fucosylated to generate Lewis antigens, structures also found on human epithelial cells. We demonstrate an extensive diversity of Lewis x and Lewis y expression in LPS O-antigen units, occurring over time and in different regions of the human stomach. Lewis expression patterns were correlated with the on/off status of the three fucosyltransferases (FucT), FutA, FutB, and FutC, which are regulated via slipped-strand mispairing in intragenic po

SUBMITTER: Nilsson C 

PROVIDER: S-EPMC1413829 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature