Helicobacter pylori is a Gram-negative bacterium commonly found in human gut and has been associated with clinical conditions such as peptic ulcers and gastric cancers. It was found to be more prevalent in the developing countries with range of 85-95% and H. pylori infection rate is more than 50 % among worldwide population. Various vaccine and drug designing strategies are being explore by scientists in order to find an effective cure for the affected individuals. However, the drug resistance mechanism makes the objective seem difficult. The Lipopolysaccharide (LPS) of the bacteria plays an important role in the pathogenesis of Helicobacter as it harbors certain membrane bound proteins that are capable of inducing inflammation such as Th1 type immune responses in the host organism and also helps in its colonization in the human gut. Therefore, targeting the LPS synthesis pathway proteins might prove to be an effective strategy of dealing with H. pylori infection. Recently an enzyme, CDP-Diacylglycerol pyrophosphatase encoded by cdh gene has been identified in H. pylori strains that has been shown to be involved in the lipid X formation in the bacteria leading to mature LPS synthesis. Hence, investigating the structural and functional characteristics of the protein of interest along with identification of novel ligand molecules that may act as inhibitors might be an effective mechanism to treat H. pylori infections.
Keywords- Helicobacter pylori, Lipopolysaccharide (LPS), CDP-Diacylglycerol pyrophosphatase, structural biology.