The SARS-CoV-2 spike protein: balancing stability and infectivity

被引:61
|
作者
Berger, Imre [1 ,2 ,3 ,4 ]
Schaffitzel, Christiane [1 ,2 ]
机构
[1] Univ Bristol, Sch Biochem, 1 Tankards Close, Bristol BS8 1TD, Avon, England
[2] Bristol Synthet Biol Ctr BrisSynBio, 24 Tyndall Ave, Bristol BS8 1TQ, Avon, England
[3] Max Planck Bristol Ctr Minimal Biol, Bristol BS8 1TS, Avon, England
[4] Univ Bristol, Sch Chem, Bristol BS8 1TS, Avon, England
基金
英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
D O I
10.1038/s41422-020-00430-4
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
引用
收藏
页码:1059 / 1060
页数:2
相关论文
共 50 条
  • [41] SARS-CoV-2 Spike Protein Destabilizes Microvascular Homeostasis
    Panigrahi, Soumya
    Goswami, Tamal
    Ferrari, Brian
    Antonelli, Christopher J.
    Bazdar, Douglas A.
    Gilmore, Hannah
    Freeman, Michael L.
    Lederman, Michael M.
    Sieg, Scott F.
    MICROBIOLOGY SPECTRUM, 2021, 9 (03):
  • [42] Evolution of the SARS-CoV-2 spike protein in the human host
    Wrobel, Antoni G.
    Benton, Donald J.
    Roustan, Chloe
    Borg, Annabel
    Hussain, Saira
    Martin, Stephen R.
    Rosenthal, Peter B.
    Skehel, John J.
    Gamblin, Steven J.
    NATURE COMMUNICATIONS, 2022, 13 (01)
  • [43] A thermostable, closed SARS-CoV-2 spike protein trimer
    Xiong, Xiaoli
    Qu, Kun
    Ciazynska, Katarzyna A.
    Hosmillo, Myra
    Carter, Andrew P.
    Ebrahimi, Soraya
    Ke, Zunlong
    Scheres, Sjors H. W.
    Bergamaschi, Laura
    Grice, Guinevere L.
    Zhang, Ying
    Nathan, James A.
    Baker, Stephen
    James, Leo C.
    Baxendale, Helen E.
    Goodfellow, Ian
    Doffinger, Rainer
    Briggs, John A. G.
    Bradley, John
    Lyons, Paul A.
    Smith, Kenneth G. C.
    Toshner, Mark
    Elmer, Anne
    Ribeiro, Carla
    Kourampa, Jenny
    Jose, Sherly
    Kennet, Jane
    Rowlands, Jane
    Meadows, Anne
    O'Brien, Criona
    Rastall, Rebecca
    Crucusio, Cherry
    Hewitt, Sarah
    Price, Jane
    Calder, Jo
    Canna, Laura
    Bucke, Ashlea
    Tordesillas, Hugo
    Harris, Julie
    Ruffolo, Valentina
    Domingo, Jason
    Graves, Barbara
    Butcher, Helen
    Caputo, Daniela
    Le Gresley, Emma
    Dunmore, Benjamin J.
    Martin, Jennifer
    Legchenko, Ekaterina
    Treacy, Carmen
    Huang, Christopher
    NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2020, 27 (10) : 934 - +
  • [44] Computational epitope map of SARS-CoV-2 spike protein
    Sikora, Mateusz
    von Bulow, Soren
    Blanc, Florian E. C.
    Gecht, Michael
    Covino, Roberto
    Hummer, Gerhard
    PLOS COMPUTATIONAL BIOLOGY, 2021, 17 (04)
  • [45] Computational biophysical characterization of the SARS-CoV-2 spike protein binding with the ACE2 receptor and implications for infectivity
    Chowdhury, Ratul
    Boorla, Veda Sheersh
    Maranas, Costas D.
    COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL, 2020, 18 (18): : 2573 - 2582
  • [46] Degradative Effect of Nattokinase on Spike Protein of SARS-CoV-2
    Tanikawa, Takashi
    Kiba, Yuka
    Yu, James
    Hsu, Kate
    Chen, Shinder
    Ishii, Ayako
    Yokogawa, Takami
    Suzuki, Ryuichiro
    Inoue, Yutaka
    Kitamura, Masashi
    MOLECULES, 2022, 27 (17):
  • [47] Characterization of a SARS-CoV-2 spike protein reference material
    Stocks, Bradley B.
    Thibeault, Marie-Pier
    Schrag, Joseph D.
    Melanson, Jeremy E.
    ANALYTICAL AND BIOANALYTICAL CHEMISTRY, 2022, 414 (12) : 3561 - 3569
  • [48] Distinct conformational states of SARS-CoV-2 spike protein
    Cai, Yongfei
    Zhang, Jun
    Xiao, Tianshu
    Peng, Hanqin
    Sterling, Sarah M.
    Walsh, Richard M., Jr.
    Rawson, Shaun
    Rits-Volloch, Sophia
    Chen, Bing
    SCIENCE, 2020, 369 (6511) : 1586 - +
  • [49] Conformational variability of loops in the SARS-CoV-2 spike protein
    Wong, Samuel W. K.
    Liu, Zongjun
    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2022, 90 (03) : 691 - 703
  • [50] A thermostable, closed SARS-CoV-2 spike protein trimer
    Xiaoli Xiong
    Kun Qu
    Katarzyna A. Ciazynska
    Myra Hosmillo
    Andrew P. Carter
    Soraya Ebrahimi
    Zunlong Ke
    Sjors H. W. Scheres
    Laura Bergamaschi
    Guinevere L. Grice
    Ying Zhang
    James A. Nathan
    Stephen Baker
    Leo C. James
    Helen E. Baxendale
    Ian Goodfellow
    Rainer Doffinger
    John A. G. Briggs
    Nature Structural & Molecular Biology, 2020, 27 : 934 - 941