Rotavirus A VP7 surface glycoprotein (VP7)

Rotavirus A VP7 surface glycoprotein is a 37-kDa calcium-binding protein that constitutes the outermost shell of the Rotavirus A virion, organized as 260 trimers (UniProt A0A060IEQ1; ICTV). It plays a critical role in the viral life cycle by mediating attachment and entry into host intestinal enterocytes, often in coordination with the VP4 spike protein (PubMed 12134022). VP7 defines the G-serotype (glycoprotein) of the virus, which is a key factor in the binary classification of rotavirus strains (WHO). As a primary target for the host's humoral immune response, VP7 is the central antigenic component of major live-attenuated vaccines, including Rotarix and RotaTeq (DrugLandscape). Neutralizing antibodies against VP7 typically function by stabilizing the trimer structure, thereby preventing the low-calcium-triggered uncoating (decapsidation) necessary for the virus to release its core into the cytoplasm (NIH PMC114027). Despite the success of current vaccines, the high genetic diversity of VP7 genotypes (G1 through G42) and the potential for reassortment continue to pose challenges for global disease control and vaccine efficacy (PubMed 31085864).

Other names

Outer capsid glycoprotein VP7G proteinG-antigenGlycoprotein VP7Viral protein 7

Induction of neutralizing antibodies that bind to VP7 trimers, stabilizing the outer capsid and inhibiting the calcium-dependent uncoating (decapsidation) process required for viral entry into host cells (NIH PMC114027; PubMed 12134022).