Key Points
- To determine the kinetics and equilibrium parameters governing the binding interaction between poliovirus type 1 capsids and the soluble poliovirus receptor.
- Purified soluble poliovirus receptor from mammalian cells to confirm virus neutralization and receptor-induced structural alterations.
- Conducted surface plasmon resonance assays across temperatures from 5 °C to 20 °C to quantify the kinetic and equilibrium binding constants on poliovirus type 1 capsids.
- Identified two distinct binding sites for the receptor on poliovirus type 1 capsids, with affinity constants at 20 °C of KD(1) = 0.67 µM and KD(2) = 0.11 µM.
- Demonstrated that the relative abundance of the KD(2) site decreases with temperature, accounting for ~46% of total binding sites at 20 °C but only 12% at 5 °C, while KD(1) site levels remain constant.
Structured PICO
PPopulationPoliovirus and its cellular receptor (soluble form purified from mammalian cells)
IInterventionSurface plasmon resonance to examine interaction at different temperatures
OOutcomeKinetics and equilibrium of poliovirus binding to the poliovirus receptor (affinity constants)surrogate
Poliovirus type 1 capsid has two distinct binding sites for its cellular receptor, with temperature-dependent relative abundances.