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研究揭示全长SARS-CoV-2突刺蛋白结构
作者:小柯机器人 发布时间:2020/10/22 15:07:45

美国斯克里普斯研究所Andrew B. Ward团队揭示全长SARS-CoV-2突刺蛋白结构。2020年10月20日,《科学》杂志在线发表了这项成果。

基于在聚山梨酯80(PS 80)去垢剂中形成的全长刺突蛋白,研究人员对来自Novavax的一种主要候选疫苗进行了冷冻电镜和位点特异性聚糖分析。研究表明,与已公布的突刺胞外域结构相比,突刺免疫原的稳定预融合构象与S1亚基略有不同。研究人员还观察到了突刺三聚体之间的新型相互作用,从而可以形成更高级的突刺复合物。这项研究证实了全长刺突蛋白免疫原的结构完整性,并为了解这一多价纳米颗粒免疫原的免疫反应提供了基础。
 
据悉,SARS-CoV-2疫苗的工作重点在于SARS-CoV-2突刺糖蛋白,这是中和抗体的主要靶标。
 
附:英文原文

Title: Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate

Author: Sandhya Bangaru, Gabriel Ozorowski, Hannah L. Turner, Aleksandar Antanasijevic, Deli Huang, Xiaoning Wang, Jonathan L. Torres, Jolene K. Diedrich, Jing-Hui Tian, Alyse D. Portnoff, Nita Patel, Michael J. Massare, John R. Yates, David Nemazee, James C. Paulson, Greg Glenn, Gale Smith, Andrew B. Ward

Issue&Volume: 2020/10/20

Abstract: AbstractVaccine efforts against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) responsible for the current COVID-19 pandemic are focused on SARS-CoV-2 spike glycoprotein, the primary target for neutralizing antibodies. We performed cryo-EM and site-specific glycan analysis of one of the leading subunit vaccine candidates from Novavax based on a full-length spike protein formulated in polysorbate 80 (PS 80) detergent. Our studies reveal a stable prefusion conformation of the spike immunogen with slight differences in the S1 subunit compared to published spike ectodomain structures. We also observed novel interactions between the spike trimers allowing formation of higher order spike complexes. This study confirms the structural integrity of the full-length spike protein immunogen and provides a basis for interpreting immune responses to this multivalent nanoparticle immunogen.

DOI: 10.1126/science.abe1502

Source: https://science.sciencemag.org/content/early/2020/10/19/science.abe1502

期刊信息
Science:《科学》,创刊于1880年。隶属于美国科学促进会,最新IF:41.037