Host integrins and Heat shock cognate 71 kDa protein (Hsc70) as rotavirus co-receptors

Rotavirus entry into host cells is a complex, multi-step process involving several cell surface molecules that act as receptors or co-receptors. The "Host integrins and Hsc70" group refers to a functional complex of proteins, primarily located in cholesterol-enriched lipid rafts, that facilitate the internalization of the virus after initial attachment (nih.gov, 2021). Key integrins involved include alpha-2/beta-1, alpha-v/beta-3, and alpha-x/beta-2, which interact with the viral outer capsid proteins VP4 (specifically the VP5* subunit) and VP7 (nih.gov, 2003). The heat shock cognate protein 70 (Hsc70) acts as a post-attachment co-receptor, interacting with a specific domain on VP5* (frontiersin.org, 2020). These molecules are critical for the transition from viral attachment to penetration and the release of double-layered particles into the cytoplasm (nih.gov, 2012). Research into these co-receptors has identified potential therapeutic strategies, such as using monoclonal antibodies, synthetic peptides, or small molecules like genistein to block viral entry and reduce infectivity (nih.gov, 2021). However, because these proteins are essential for normal cellular functions like adhesion and protein folding, targeting them presents significant safety challenges (nih.gov, 2021). This target is considered "incorrect" as a single therapeutic target because it encompasses multiple distinct proteins rather than a single molecular entity.

Other names

Rotavirus functional receptor complexRotavirus entry receptorsIntegrin-Hsc70 complexRotavirus co-receptor complex

Entry inhibition, Attachment inhibition, Post-attachment blocking, Disruption of lipid rafts