Enterovirus D68 capsid protein complex

The Enterovirus D68 (EV-D68) capsid protein complex is the icosahedral shell of the virus, composed of 60 copies each of four structural proteins: VP1, VP2, VP3, and VP4 (NIH, 2019; Colorado.edu, 2024). It plays a critical role in the viral life cycle by protecting the positive-sense single-stranded RNA genome and mediating host cell entry through interactions with receptors like sialic acid and ICAM-5 (NIH, 2024; Colorado.edu, 2024). The capsid is a primary target for the host immune system and a major focus for antiviral development, as it contains the principal antigenic epitopes recognized by neutralizing antibodies (Frontiers, 2026). Small molecule inhibitors, such as pleconaril and experimental compounds like R856932, target a hydrophobic pocket (canyon) in the VP1 protein to stabilize the capsid and prevent the uncoating process required for genome release (ACS, 2019; NIH, 2024). EV-D68 is primarily associated with severe respiratory illnesses and has been linked to acute flaccid myelitis (AFM), a serious neurological condition causing muscle weakness and paralysis in children (NIH, 2023; BioRxiv, 2023). Understanding the structural transitions of the capsid is essential for the development of effective vaccines and therapeutics against emerging neurotropic strains (Colorado.edu, 2024).

Other names

EV-D68 capsidEnterovirus D68 virion shellEV-D68 structural protein complexEnterovirus D68 VP1-VP4 complex

Capsid stabilization and inhibition of viral uncoating by binding to the hydrophobic pocket (canyon) of the VP1 protein, thereby preventing the release of the viral RNA genome into the host cell (ACS, 2019; NIH, 2024).