Rotavirus VP7 glycoprotein (VP7)

The **Rotavirus VP7 glycoprotein** is a highly conserved structural protein forming the outermost layer of the rotavirus capsid[4][8]. It is a trimeric, calcium ion–stabilized glycoprotein synthesized and processed in the endoplasmic reticulum, where it is essential for virion assembly and stability[1][4]. VP7 is the principal target of neutralizing antibodies, making it a primary determinant of rotavirus G serotypes and a critical antigen for vaccine development[3][5][6]. Removal of Ca2+ ions destabilizes the VP7 trimer and initiates viral entry by promoting uncoating[3][5]. VP7 contains multiple neutralizing epitopes and is subject to antigenic variation, with its gene (segment 9) used for molecular classification of rotavirus strains[4][6]. The protein's proper folding and function require glycosylation and correct disulfide bond formation[7]. VP7-directed immune responses are central to both natural immunity and vaccine-mediated protection against rotavirus infection[3][6].

Other names

Rotavirus VP7VP7 proteinRotavirus outer-layer protein VP7

Neutralization: Antibodies stabilize the VP7 trimer, inhibiting uncoating and viral entry[3][5]. Induction of protective immunity: Subunit or inactivated vaccines based on VP7 elicit neutralizing antibodies[3].