Adherence properties of Helicobacter pylori: Impact on pathogenesis and adaptation to the host

The adherence of the human gastric pathogen Helicobacter pylori to the gastric mucosa is widely assumed to play a substantial role in initial colonization and long-term persistence in the human stomach. In the past, a couple of putative adhesins were identified, most of which were members of the lar...

Full description

Saved in:
Bibliographic Details
Published in:International journal of medical microbiology 2005-09, Vol.295 (5), p.317-324
Main Author: Odenbreit, Stefan
Format: Article
Language:English
Subjects:
Adaptation, Physiological
Adherence
Adhesins, Bacterial - physiology
Animals
Bacterial Adhesion - physiology
Bacterial Outer Membrane Proteins - physiology
Colonization
Gastric Mucosa - microbiology
Helicobacter Infections - microbiology
Helicobacter pylori
Helicobacter pylori - pathogenicity
Helicobacter pylori - physiology
Helicobacter pylori - ultrastructure
Humans
Lewis blood group antigens
Outer membrane proteins
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The adherence of the human gastric pathogen Helicobacter pylori to the gastric mucosa is widely assumed to play a substantial role in initial colonization and long-term persistence in the human stomach. In the past, a couple of putative adhesins were identified, most of which were members of the large outer membrane protein (OMP) family of H. pylori. Among these, the BabA protein was shown to recognize the Le b antigen, which is presented as a dominant surface structure in the gastric mucosa. The SabA adhesin binds to sialylated antigens, which are up-regulated in inflamed gastric tissue. Other OMPs, such as AlpAB or HopZ were also shown to be involved in binding to gastric epithelial cells, but the corresponding receptors are unknown. The aim of this review is to summarize recent data giving new insights in binding specificities of H. pylori adhesins and their role in pathogenesis and adaptation to the host.
ISSN:1438-4221
1618-0607
DOI:10.1016/j.ijmm.2005.06.003