Megha Vaidya, PV Virparia and Hetalkumar Panchal
Helicobacter pylori is gram-negative bacterial pathogen, associated with chronic gastritis and other severe gastro duodenal diseases such as peptic and gastric ulcers, gastric cancer, and mucosa-associated lymphoid tissue (MALT) lymphoma. One of the intriguing virulence factors of H. pylori is cag Pathogenicity Island (cagPAI) which codes for Type IV secreting system. Type IV secreting system is found in many strains of H. pylori. Present work focuses on protein interaction studies to clarify and confirm the interactions and assembly of proteins present in outer membrane and pilus structure of t4ss. During the interaction studies of t4ss we have focused on only CagC, Cag3 and CagM interactions based on steriochemical properties. It is found that the pattern of pilus formation follows the specific order of assembly and the order of assembly is CagC-C dimer formation followed by tetramer formation to form stable pilus assembly of t4ss. The order of interaction at the outer membrane is CagM interacts with CagC-C dimer and then with Cag3 to form sub-assembly of t4ss.This findings of structural interaction can be used to prevent onset of diseases caused by H. pylori by preventing the formation of t4ss, pilus assembly and ultimately the translocation of onco protein CagA in host organism.
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