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Rotavirus Outer Capsid Glycoprotein VP7 (G1 serotype) is a critical structural protein and major surface antigen of Group A Rotaviruses (RVA), the leading cause of severe, dehydrating gastroenteritis in infants and young children worldwide [2, 3]. As a calcium-dependent trimeric glycoprotein, VP7 forms the outermost shell of the virion and facilitates cell entry by interacting with host cell co-receptors, such as integrins, following initial attachment by the VP4 spike protein [1, 8]. It serves as a primary target for neutralizing antibodies, which stabilize the VP7 trimer and prevent the uncoating process required for viral replication [2, 12, 18]. Consequently, VP7 is a central component of global vaccination strategies, with major vaccines like Rotarix (monovalent G1P[8]) and RotaTeq (pentavalent) incorporating G1 antigens to elicit protective mucosal immunity [5, 14, 28]. However, the protein undergoes continuous evolution via antigenic drift and reassortment, necessitating ongoing surveillance for vaccine-escape mutants [9, 21, 26].
Vaccines containing G1 antigens induce the production of neutralizing antibodies (particularly mucosal IgA) that bind to the VP7 glycoprotein to stabilize the viral capsid and inhibit the uncoating and membrane penetration steps necessary for infection.
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