Published online Jun 21, 2017. doi: 10.3748/wjg.v23.i23.4158
Peer-review started: February 7, 2017
First decision: March 16, 2017
Revised: April 12, 2017
Accepted: June 1, 2017
Article in press: June 1, 2017
Published online: June 21, 2017
Processing time: 142 Days and 22.1 Hours
Helicobacter pylori (H. pylori) as a causative agent of gastric complications, is well adapted for the colonization of gastric mucosa. Although the infectious process depends on several factors, the adhesion to the gastric mucosa is the first and important step. Among several outer membrane proteins, BabA is one of the significant protein involving in many inflammatory processes in addition to its role in the attachment for the persistent colonization. We performed a PubMed search using the key words: “babA”, “pylori”, “gastric complications”, “homologous recombination”, “slipped strand mispairing”; a total of 249 articles were displayed. Of these we mainly focused on articles with the full text in English and published between 2005 and 2016. H. pylori BabA is involved in binding with receptors; however, its synthesis is regulated by phase variation. In this review we confirm that H. pylori babA can be modulated at the molecular and functional levels to adapt to the stress within the gastro-intestinal tract.
Core tip:Helicobacter pylori are well adapted to colonize the gastric mucosa. Although the infectious process depends on several factors, adhesion to the gastric mucosa is the first and critical step. Among outer membrane proteins, BabA is an important protein involved in many inflammatory processes in addition to playing a role in the aforementioned attachment process. In this review, we have summarized the current, published knowledge regarding its functional and molecular aspects by which the pathogen can attach to the host cell receptors.