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研究揭示新冠病毒和SARS病毒受体结合域中保守的抗原决定簇
作者:小柯机器人 发布时间:2020/4/10 14:58:34

美国斯克里普斯研究所Ian A. Wilson与中国香港大学Chris K. P. Mok等研究人员合作有了新发现。他们解析了新冠病毒(SARS-CoV-2)和SARS病毒(SARS-CoV)受体结合域中高度保守的抗原决定簇。相关论文于2020年4月3日在线发表在《科学》杂志上。

研究人员确定了CR3022(这是一个从恢复期SARS患者中分离出的中和抗体)与SARS-CoV-2刺突蛋白(S)的受体结合结构域(RBD)形成复合物的晶体结构,分辨率为3.1Å。CR3022靶向位于受体结合位点远端的高度保守的表位,可实现SARS-CoV-2和SARS-CoV之间的交叉反应结合。结构建模进一步证明,只有当三聚体S蛋白上的至少两个RBD呈“ up”构型并稍微旋转时,CR3022才能进入结合表位。总的来说,这项研究提供了对SARS-CoV-2抗体识别的分子见解。
 
据悉,由SARS-CoV-2病毒引起的COVID-19暴发现在已成为大流行病,但目前对该病毒的抗原性了解甚少。
 
附:英文原文

Title: A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV

Author: Meng Yuan, Nicholas C. Wu, Xueyong Zhu, Chang-Chun D. Lee, Ray T. Y. So, Huibin Lv, Chris K. P. Mok, Ian A. Wilson

Issue&Volume: 2020/04/03

Abstract: Abstract The outbreak of COVID-19 caused by SARS-CoV-2 virus has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein to 3.1 . CR3022 targets a highly conserved epitope, distal from the receptor-binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBD on the trimeric S protein are in the “up” conformation and slightly rotated. Overall, this study provides molecular insights into antibody recognition of SARS-CoV-2.

DOI: 10.1126/science.abb7269

Source: https://science.sciencemag.org/content/early/2020/04/02/science.abb7269

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