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The Helicobacter pylori UreB-HspA fusion protein is a recombinant antigen designed for prophylactic vaccination against H. pylori infection. It consists of the UreB subunit of the urease enzyme, which is essential for the bacterium to neutralize gastric acid via urea hydrolysis, and the HspA protein, a GroES-like chaperone involved in nickel metabolism and protein folding [2][3]. By combining these two highly immunogenic and conserved proteins, the fusion antigen aims to elicit a synergistic immune response that prevents bacterial adhesion and survival within the stomach [1]. Clinical development has primarily focused on oral delivery systems to stimulate mucosal immunity in the gut-associated lymphoid tissue. This target is significant in the effort to reduce the global burden of gastric cancer and peptic ulcers by preventing the initial H. pylori colonization in high-risk populations [1][4]. Sources: [1] Guo, M., et al. (2015). Efficacy, safety, and immunogenicity of an oral recombinant Helicobacter pylori vaccine in children in China: a randomised, double-blind, placebo-controlled, phase 3 trial. The Lancet. [2] Liu, K. Y., et al. (2011). Immunogenicity and protective efficacy of a Vibrio cholerae-derived DNA vaccine encoding Helicobacter pylori UreB and HspA. World Journal of Gastroenterology. [3] UniProt Consortium. Urease subunit beta (P14916) and Heat shock protein A (P0A0V4). [4] Malfertheiner, P. (2015). Helicobacter pylori: an oral vaccine on the horizon. The Lancet.
The fusion protein acts as a vaccine antigen that induces mucosal and systemic immune responses, specifically producing anti-UreB and anti-HspA antibodies (IgA and IgG) to neutralize urease activity and inhibit H. pylori colonization of the gastric mucosa [1][2].
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