A new study, published in the journal Scientific Advances by researchers at the University of Nottingham and AstraZeneca, has revealed that H. Pylori uses a molecular mechanism to attach to stomach sugars. Helicobacter pylori (H. pylori) is the ulcer causing bacteria. It is estimated that 50% of the population is a carrier of the bacterium and it is considered one of the most common bacterial infections and a leading cause of ulcers and gastric cancer.
The exact molecular interaction pathway of H. Pylori with its host has eluded researchers for years. The interactions between the H. pylori adhesion protein BabA and Lewisb sugars of the gastric mucosa revealed that BabA possesses a specific groove at the tip pf the protein that enables it to securely attach to Lewisb using a network of hydrogen bonds (the same kind of interactions that keep water molecules together).
If the hydrogen bonds are disrupted the network does not function properly and binding of the adhesion sugar proteins do not occur. “Because BabA is unique to H. pylori, we can specifically target, and hopefully eradicate, this bacterium without affecting the other good bacteria in our normal flora. If successful, this therapeutic strategy will also be extremely useful for treating H. pylori infections that are already resistant to antibiotics,” said Naim Hage, the post graduate researcher who worked on the project as part of a doctoral thesis.
“While this study answers long-standing questions about how H. pylori colonises the stomach, it represents the very first step in the development of novel therapies. The next few years of laboratory-based research will be crucial to determine if an anti-BabA adhesion approach is viable and can progress to clinical development. A similar approach is already showing promising results for the treatment of urinary tract infections in preclinical models. Looking forward, we are excited to continue working closely with AstraZeneca who have provided a tremendous amount of support to achieve this discovery”, said Dr Franco Falcone.
Franco H. Falcone et al. Structural basis of Lewisb antigen binding by the Helicobacter pylori adhesin BabA. Science Advances, August 2015 DOI: 10.1126/sciadv.1500315