Molecular Basis of Plasticity of Porcine Delta Coronavirus (PDCoV) & Development of Countermeasures Against Infection

Abstract

Porcine deltacoronavirus (PDCoV) is an enteric pathogen that infects a broad range of mammal and avian species. Viral entry is achieved through the transmembrane spike (S) glycoprotein, specifically the receptor binding domain (RBD), binding to host receptor aminopeptidase N (APN). The S glycoprotein plays a key role in modulating host and tissue tropism, zoonotic transmission, and pathogenesis. The mechanism by which the S glycoprotein binds to a broad range of host receptors is not understood. Given that the S glycoprotein is the main target of antibodies and that neutralizing antibody titers are a correlate of protection against coronaviruses, the development of vaccines and therapeutics focuses intensively on this glycoprotein target. This research describes the molecular basis of binding of the S glycoprotein to host receptors and identifies the neutralizing epitopes on the S glycoproteins providing the first line of protection for a possible future PDCoV epidemic.