Structure and immune recognition of the porcine epidemic diarrhea virus spike protein.
Structure and immune recognition of the porcine epidemic diarrhea virus spike protein.
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DOI:
10.1016/j.str.2020.12.003
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发表时间:
2021-04-01
期刊:
影响因子:
--
通讯作者:
Ward AB
中科院分区:
文献类型:
--
作者:
Kirchdoerfer RN;Bhandari M;Martini O;Sewall LM;Bangaru S;Yoon KJ;Ward AB
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. Kirchdoerfer et al. use cryoelectron microscopy of the porcine epidemic diarrhea virus spike ectodomain to identify glycans and fatty acids in protein-protein interfaces and delineate epitopes targeted by the pig immune response to infection.
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Bioinformatics (Oxford, England)
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