Rotavirus outer capsid protein VP4 and Rotavirus outer capsid protein VP7 (VP4, VP7)

Rotavirus outer capsid proteins VP4 and VP7 form the external structural layer of the virion and are essential for viral infectivity, cell attachment, entry, and immune recognition. VP4 assembles into spike-like projections responsible for binding to host cell receptors and mediating membrane penetration upon proteolytic cleavage. VP7 is a glycosylated, trimeric protein that forms a smooth outer lattice, stabilizing the virion and determining G serotype specificity. Both proteins are primary targets for host neutralizing antibodies, dictate immune protection and host specificity, and are the immunogens in all currently licensed rotavirus vaccines[1][3][5][6][8]. VP4 and VP7 are the key antigenic and structural molecules of the rotavirus outer capsid. They determine serotype-specific immunity, host range, and the infectivity of rotavirus. Both are considered therapeutic and diagnostic targets due to their roles in immune response and as neutralization antigens. The canonical names and structure (VP4 as spike protein, VP7 as glycoprotein layer) are standardized and directly supported by structural, immunological, and functional data[1][2][3][5][6][8].

Other names

VP4 protein (spike protein)VP7 protein (glycoprotein)Rotavirus spike protein (VP4)Rotavirus outer capsid glycoprotein (VP7)

Vaccines/antibodies binding VP7 or VP4 block conformational changes or receptor binding necessary for cell entry, neutralizing infectivity. Antibody-mediated neutralization (direct inhibition of membrane penetration or virus uncoating).