英国剑桥大学John A. G. Briggs课题组解析出完整病毒颗粒上SARS-CoV-2突刺蛋白的结构与分布。相关论文于2020年8月17日在线发表在《自然》杂志上。
Title: Structures and distributions of SARS-CoV-2 spike proteins on intact virions
Author: Zunlong Ke, Joaquin Oton, Kun Qu, Mirko Cortese, Vojtech Zila, Lesley McKeane, Takanori Nakane, Jasenko Zivanov, Christopher J. Neufeldt, Berati Cerikan, John M. Lu, Julia Peukes, Xiaoli Xiong, Hans-Georg Krusslich, Sjors H. W. Scheres, Ralf Bartenschlager, John A. G. Briggs
Issue&Volume: 2020-08-17
Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells2–6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9–12. The structure and distribution of S on the virion surface, however, has not been characterized. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S present on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination.
DOI: 10.1038/s41586-020-2665-2
Source: https://www.nature.com/articles/s41586-020-2665-2
Nature:《自然》,创刊于1869年。隶属于施普林格·自然出版集团,最新IF:69.504
官方网址:http://www.nature.com/
投稿链接:http://www.nature.com/authors/submit_manuscript.html
本期文章:《自然》:Online/在线发表