Lastly, we investigated the relationship between receptor binding and viral stability. We show that receptor preference does not influence capsid stability. Also we show that the requirement for acidic pH during viral entry varies among isolates and is also independent of their receptor preference.

As expected, we found that EV-D68 binds to α2,6-linked N-glycans, but some strains were particularly fond of specific disialylated gangliosides GD3, GD1c, GT1a, and GQ1b. We confirmed a functional relevance for viral entry using enzymatic inhibition and by using glycolipid mimetics as inhibitors.

Previous work found two EV-D68 viruses using HS to enter cells. Utilising a HS array, we confirmed this and found a third! The secret? They all share a special change at position 271 in their VP1 protein - switching from a negatively/neutrally charged amino acid to a positive charge.