Rotavirus VP7 G1 glycoprotein (VP7)

Rotavirus VP7 G1 glycoprotein is a 37-kDa structural protein that forms the outer layer of the Group A rotavirus capsid, organized as 260 trimers (Source: UniProt). It is a major neutralizing antigen and the primary determinant of the G1 serotype, which is the most prevalent cause of severe gastroenteritis in humans worldwide (Source: NIH). VP7 plays a critical role in the viral life cycle by facilitating attachment to host cell receptors and acting as a calcium-dependent regulator of the uncoating process (Source: PubMed). Upon entry into the host cell endosome, a decrease in calcium concentration triggers the dissociation of the VP7 shell, which is necessary for the conformational changes in the VP4 spike protein that lead to membrane penetration (Source: NIH). Due to its essential role in infectivity and its high immunogenicity, VP7 G1 is a central component of live-attenuated vaccines such as Rotarix and RotaTeq (Source: Drugs.com). These vaccines work by eliciting neutralizing antibodies that stabilize the VP7 trimer, thereby blocking the uncoating trigger and preventing viral replication (Source: PubMed).

Other names

G1 antigenG1 glycoproteinOuter capsid protein VP7G-type proteinVP7 glycoprotein

Vaccines targeting the Rotavirus VP7 G1 glycoprotein induce the production of serotype-specific neutralizing antibodies. These antibodies bind to the outward-facing surface of the VP7 trimer, stabilizing the calcium-dependent intersubunit contacts. This stabilization prevents the dissociation of the VP7 shell in the low-calcium environment of the endosome, thereby inhibiting the uncoating process and the subsequent membrane-penetrating conformational changes of the VP4 spike protein (Source: NIH, 2010; PubMed, 2020).