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The Helicobacter pylori CagA-VacA-UreB fusion protein antigen is a recombinant trivalent construct designed as a primary vaccine candidate to prevent and treat H. pylori infections (Zhu et al., 2014). This fusion protein incorporates three major virulence factors: Cytotoxin-associated gene A (CagA), which disrupts host cell signaling and promotes oncogenesis; Vacuolating cytotoxin A (VacA), which induces pore formation and apoptosis in gastric epithelial cells; and Urease subunit beta (UreB), an essential component of the enzyme that allows the bacterium to survive the stomach's acidic environment (Cover & Blanke, 2005; Eaton et al., 1991). By combining these antigens into a single molecule, the construct aims to elicit a robust, multi-pronged immune response involving both neutralizing antibodies and cellular immunity (Guo et al., 2017). This multi-antigen approach is intended to provide broader protection against various H. pylori strains compared to monovalent vaccines. Clinical and preclinical studies have evaluated its efficacy in reducing bacterial load and preventing the development of associated gastric diseases, such as chronic gastritis, peptic ulcers, and gastric adenocarcinoma (Ming et al., 2015). As a therapeutic target, it represents a critical focus for the development of prophylactic and potentially therapeutic immunization strategies against one of the most common bacterial infections worldwide.
The fusion protein acts as a vaccine antigen to stimulate the host immune system, inducing the production of specific serum IgG and secretory IgA antibodies, as well as activating T-cell mediated immunity to neutralize H. pylori virulence factors and inhibit bacterial colonization (Guo et al., 2017).
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