The human enterovirus D68 (EV-D68) is a causative agent of childhood respiratory infections, but despite its prevalence the exact mechanism mediating its cell entry have not been fully established. Investigators in the journal Nature Communications show how EV-D68 binds to sialic acid on the cell surface to initiate infection.
Human enterovirus D68 (EV-D68) is a causative agent of childhood respiratory diseases and has now emerged as a global public health threat. Nevertheless, knowledge of the tissue tropism and pathogenesis of EV-D68 has been hindered by a lack of studies on the receptor-mediated EV-D68 entry into host cells.
Investigators in the journal Nature Communications demonstrate that cell surface sialic acid is essential for EV-D68 to bind to and infect susceptible cells.
Crystal structures of EV-D68 in complex with sialylated glycan receptor analogues show that they bind into the ‘canyon’ on the virus surface.
The sialic acid receptor induces a cascade of conformational changes in the virus to eject a fatty-acid-like molecule that regulates the stability of the virus.
Thus, virus binding to a sialic acid receptor and to immunoglobulin-like receptors used by most other enteroviruses share a conserved mechanism for priming viral uncoating and facilitating cell entry.