Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Department of Veterinary Diagnostic and Production Animal Medicine, Iowa State University, Ames, IA 50011, USA.
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.
猪流行性腹泻病毒(PEDV)是一种α冠状病毒,可导致猪的高发病率和死亡率。作为病毒嗜性和进入的关键决定因素,PEDV 刺突蛋白是宿主抗体反应的关键靶标,也是基于蛋白质疫苗免疫原的良好候选物。我们使用电子显微镜评估了 PEDV 刺突结构以及猪多克隆抗体对病毒感染的反应。PEDV 刺突的结构揭示了类似于 HuCoV-NL63 的构象。PEDV 的几个蛋白-蛋白界面由非蛋白成分介导,包括 Asn264 上的聚糖和两个结合的棕榈油酸分子。对 PEDV 感染的多克隆抗体反应显示 S1 区域的表位占主导地位。这种结构和免疫特性为冠状病毒刺突稳定性决定因素提供了深入了解,并探索了病毒刺突蛋白的免疫景观。