Rotavirus VP4 and VP7 structural proteins (VP4, VP7)

The rotavirus VP4 and VP7 structural proteins are the two outermost capsid components of rotavirus particles. VP4 forms spike-like projections on the virion surface and is essential for mediating the virus's initial binding to host cell receptors and subsequent penetration of the endosomal membrane, enabling genome release into the cytoplasm[1][2][6][8]. VP7 is a calcium-stabilized glycoprotein that forms a protective outer layer and is critical for virion assembly and stability; it interacts directly with VP4 to lock the spikes in place and must be removed (uncoated) for successful membrane penetration to occur during infection[1][3][5]. Both proteins are the primary targets of broadly neutralizing antibodies and constitute the immunodominant antigens included in rotavirus vaccines[4][6]. Antigenic diversity in these proteins underlies the different rotavirus serotypes and poses both an immunological and therapeutic challenge. Together, VP4 and VP7 are central to viral infectivity, tropism, and immune recognition[1][2][3][4][6][7][8].

Other names

VP4 (rotavirus spike protein)VP7 (rotavirus outer layer protein)Rotavirus outer capsid proteins

Virus neutralization via antibody binding to VP4 or VP7, blocking cellular attachment or membrane penetration Prevention of viral entry by inhibiting conformational changes in VP4 Inhibition of uncoating or capsid assembly by interfering with VP7 stability