Key result
At temperatures below 37°C, the antiviral compound WIN51711 prevents wild-type poliovirus from binding to its cellular receptor, indicating that the viral capsid must undergo structural changes to bind.
Why the study?
Does WIN51711 prevent poliovirus receptor binding at low temperatures?
Does WIN51711 prevent poliovirus receptor binding at low temperatures?
The poliovirus capsid must undergo structural changes to bind to its cellular receptor, a process that can be blocked by WIN51711 at low temperatures.
Answers are grounded in this paper and cite their sources.
WIN51711 may target poliovirus capsid transitions; leaves open whether this mechanism translates to in vivo antiviral efficacy.
Drugs such as WIN51711 that inhibit picornavirus replication are thought to block poliovirus infectivity by binding to the capsid and preventing structural transitions required for uncoating. We examined the activity of WIN51711 at temperatures where capsid flexibility is thought to be decreased. Below 37 degrees C, WIN51711 inhibits the binding of wild-type poliovirus to cells but does not affect the binding of a poliovirus mutant which is believed to undergo structural transitions more readily. These results suggest that the poliovirus capsid must undergo structural changes to bind to its cellular receptor.
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Dove et al. (2000) studied Poliovirus infection. WIN51711 vs. Vehicle (DMSO) was evaluated on Percentage of radioactive methionine-labeled virus bound to cells. At temperatures below 37°C, the antiviral compound WIN51711 prevents wild-type poliovirus from binding to its cellular receptor, indicating that the viral capsid must undergo structural changes to bind.
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