Cav1.2 facilitates the binding and internalisation of porcine epidemic diarrhoea virus.

Abstract

Porcine epidemic diarrhoea virus (PEDV) has caused substantial economic losses to the global swine industry. The PEDV spike (S) protein mediates viral entry by interacting with host receptors. However, the molecular mechanisms underlying PEDV entry remain incompletely understood. In this study, we identified the L-type calcium channel Cav1.2 as a critical host factor for PEDV entry. Depletion of Cav1.2 significantly suppressed PEDV replication. Additionally, treatment with the FDA-approved Cav1.2 blocker diltiazem inhibited PEDV replication and disrupted early infection events. Mechanistically, we found that Cav1.2 interacts with the PEDV S1 subunit. Both Cav1.2 knockdown and diltiazem treatment substantially reduced the binding and internalisation of PEDV. These findings reveal that Cav1.2 is a key host factor for PEDV binding and internalisation via interaction with the viral S protein, and suggest that Cav1.2 may serve as a promising target for antiviral drug development against PEDV.