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A full-length, membrane-associated model supports a role for NS3 as a candidate membrane-spanning RNA translocase that may couple ATP hydrolysis to genome movement and establishes a basis for mechanistic studies and structure-guided antiviral design.
It is demonstrated that cell surface sialic acid is essential for EV-D68 to bind to and infect susceptible cells and that 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.
It is shown that spikes from both serotypes of HKU1 preferentially bind 9-O-acetylated α2,8-linked disialosides, and molecular dynamics simulations indicated that membrane-embedded GT3, but not GD3, presents its glycan chain in a geometry compatible with S1A-mediated engagement.
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