Structure, receptor recognition, and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein.
Structure, receptor recognition, and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein.
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DOI：
10.1016/j.cell.2022.05.019
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发表时间：
2022-06-23
期刊：
影响因子：
64.5
通讯作者：
Veesler, David
中科院分区：
文献类型：
--
作者：
Tortorici, M. Alejandra;Walls, Alexandra C.;Joshi, Anshu;Park, Young-Jun;Eguia, Rachel T.;Miranda, Marcos C.;Kepl, Elizabeth;Dosey, Annie;Stevens-Ayers, Terry;Boeckh, Michael J.;Telenti, Amalio;Lanzavecchia, Antonio;King, Neil P.;Corti, Davide;Bloom, Jesse D.;Veesler, David
从儿童呼吸道拭子中分离出CCoV-HuPn-2018表明，更多的冠状病毒正在向人类传播，而不是以前所认识到的。我们确定了CCoV-HuPn-2018刺突糖蛋白三聚体在两种不同构象状态下的结构，并表明其结构域0识别唾液酸苷。我们鉴定了CCoV-HuPn-2018刺突结合犬、猫和猪氨肽酶N（APN）直系同源物，其作为进入受体，并确定了与犬APN复合的受体结合B结构域的结构。在人APN的N739位引入寡糖使细胞对CCoV-HuPn-2018刺突介导的进入敏感，这表明单核苷酸多态性可能是某些个体中病毒检测的原因。由HCoV-229 E感染引起的人多克隆血浆抗体和猪冠状病毒单克隆抗体抑制CCoV-HuPn-2018刺突介导的进入，强调了冠状病毒之间的交叉中和活性。这些数据为针对这种代表第八种人类感染冠状病毒的人畜共患病病原体的疫苗和治疗开发铺平了道路。冠状病毒CCoV-HuPn-2018 S的Cryo-EM结构揭示了结构域0的两种构象，其识别唾液酸苷。犬、猫和猪APN以及人N739聚糖敲入APN是进入受体，表明SNP可能是患者中检测到CCoV-HuPn-2018的原因。由冠状病毒229 E感染引发的人类抗体抑制CCoV-HuPn-2018，突出了CCoV-coronavirus交叉中和活性。
The isolation of CCoV-HuPn-2018 from a child respiratory swab indicates that more coronaviruses are spilling over to humans than previously appreciated. We determined the structures of the CCoV-HuPn-2018 spike glycoprotein trimer in two distinct conformational states and showed that its domain 0 recognizes sialosides. We identified that the CCoV-HuPn-2018 spike binds canine, feline, and porcine aminopeptidase N (APN) orthologs, which serve as entry receptors, and determined the structure of the receptor-binding B domain in complex with canine APN. The introduction of an oligosaccharide at position N739 of human APN renders cells susceptible to CCoV-HuPn-2018 spike-mediated entry, suggesting that single-nucleotide polymorphisms might account for viral detection in some individuals. Human polyclonal plasma antibodies elicited by HCoV-229E infection and a porcine coronavirus monoclonal antibody inhibit CCoV-HuPn-2018 spike-mediated entry, underscoring the cross-neutralizing activity among ɑ-coronaviruses. These data pave the way for vaccine and therapeutic development targeting this zoonotic pathogen representing the eighth human-infecting coronavirus. Cryo-EM structures of the coronavirus CCoV-HuPn-2018 S reveal two conformations of domain 0, which recognize sialosides. Canine, feline, and porcine APNs and human N739 glycan knockin APN are entry receptors, suggesting that SNPs might account for CCoV-HuPn-2018 detection in patients. Human antibodies elicited by coronavirus 229E infection inhibit CCoV-HuPn-2018, highlighting ɑ-coronavirus cross-neutralizing activity.
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