Porcine epidemic diarrhea virus spike protein (PEDV S protein)

The Porcine epidemic diarrhea virus spike protein (PEDV S protein) is a large, trimeric glycoprotein that protrudes from the viral surface as club-shaped spikes, mediating attachment to host cells and subsequent membrane fusion for viral entry. It consists of S1 and S2 subunits, where S1 handles receptor binding—primarily to porcine aminopeptidase N (pAPN)—and potentially sialic acids via its N-terminal domain, while S2 drives fusion through characteristic α-helices following proteolytic cleavage at S1/S2 and S2' sites. The prefusion structure, resolved by cryo-EM at ~3.1 Å, reveals a densely glycosylated architecture with domains including N-terminal domain (NTD), receptor-binding domain (RBD), and fusion machinery, showing conformational flexibility akin to other alphacoronaviruses like NL63. PEDV S remains uncleaved during virion packaging but activates in host lysosomes, enabling infection of intestinal enterocytes and causing severe diarrhea in pigs. As the primary immunogen, it elicits neutralizing antibodies targeting S1 epitopes, informing vaccine design to block entry and mitigate agricultural losses from PEDV outbreaks.

Other names

PEDV spike glycoproteinPEDV S glycoprotein