Structure and immune recognition of the porcine epidemic diarrhea virus spike protein

Structure. 2021 Apr 1;29(4):385-392.e5. doi: 10.1016/j.str.2020.12.003. Epub 2020 Dec 29.


Porcine epidemic diarrhea virus (PEDV) is an alphacoronavirus responsible for significant morbidity and mortality in pigs. A key determinant of viral tropism and entry, the PEDV spike protein is a key target for the host antibody response and a good candidate for a protein-based vaccine immunogen. We used electron microscopy to evaluate the PEDV spike structure, as well as pig polyclonal antibody responses to viral infection. The structure of the PEDV spike reveals a configuration similar to that of HuCoV-NL63. Several PEDV protein-protein interfaces are mediated by non-protein components, including a glycan at Asn264 and two bound palmitoleic acid molecules. The polyclonal antibody response to PEDV infection shows a dominance of epitopes in the S1 region. This structural and immune characterization provides insights into coronavirus spike stability determinants and explores the immune landscape of viral spike proteins.

Keywords: cryoelectron microscopy; glycoprotein; palmitoleic acid; polyclonal antibody; porcine epidemic diarrhea virus.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Antibodies, Viral / metabolism*
  • Cell Line
  • Coronavirus Infections / immunology*
  • Cryoelectron Microscopy
  • Epitopes / immunology*
  • Fatty Acids, Monounsaturated / chemistry
  • Models, Molecular
  • Molecular Conformation
  • Polysaccharides / chemistry
  • Porcine epidemic diarrhea virus / chemistry
  • Porcine epidemic diarrhea virus / immunology*
  • Porcine epidemic diarrhea virus / metabolism
  • Protein Binding
  • Sf9 Cells
  • Spike Glycoprotein, Coronavirus / chemistry*
  • Spike Glycoprotein, Coronavirus / immunology
  • Swine


  • Antibodies, Viral
  • Epitopes
  • Fatty Acids, Monounsaturated
  • Polysaccharides
  • Spike Glycoprotein, Coronavirus
  • palmitoleic acid