Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant.
Leonid Yurkovetskiy,Xue Wang,Kristen E. Pascal,Christopher Tomkins-Tinch,Thomas Nyalile,Yetao Wang,Alina Baum,William E. Diehl,Ann Dauphin,Claudia Carbone,Kristen Veinotte,Shawn B. Egri,Stephen F. Schaffner,Stephen F. Schaffner,Jacob E. Lemieux,James B. Munro,Ashique Rafique,Abhi Barve,Pardis C. Sabeti,Christos A. Kyratsous,Natalya Dudkina,Kuang Shen,Jeremy Luban +22 more
TLDR
It is shown that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin.About:
This article is published in Cell.The article was published on 2020-10-29 and is currently open access. It has received 840 citations till now. The article focuses on the topics: Virion membrane & Protein structure.read more
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Cryo-EM structure of the SARS-CoV-2 Omicron spike
Gabriele Cerutti,Yicheng Guo,Lihong Liu,Liyuan Liu,Zhening Zhang,Yang Luo,Yiming Huang,Harris H. Wang,David D. Ho,Zizhang Sheng,Lawrence Shapiro +10 more
TL;DR: In this paper , a 3.1 Å-resolution cryoelectron microscopy (cryo-EM) structure of the Omicron spike protein ectodomain was presented, showing a spike that is exclusively in the 1-RBD-up conformation with high mobility of RBD.
Journal ArticleDOI
Antibody and B cell responses to SARS-CoV-2 infection and vaccination.
Katharina Röltgen,Scott D. Boyd +1 more
TL;DR: In this paper, the authors review findings addressing the nature of antibody responses against SARS-CoV-2 and their role in protecting from infection or modulating COVID-19 disease severity.
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Impact of South African 501.V2 Variant on SARS-CoV-2 Spike Infectivity and Neutralization: A Structure-based Computational Assessment
TL;DR: In this paper, the effects of amino acid substitutions in the spike (S) receptor-binding domain (RBD) of the SARS-CoV-2 variants on the interactions with the human ACE2 receptor and monoclonal antibodies (mAbs) reported earlier to neutralize the spike were analyzed.
Journal ArticleDOI
Evaluation of cell-based and surrogate SARS-CoV-2 neutralization assays.
Anton M Sholukh,Andrew Fiore-Gartland,Emily S Ford,Maurine D. Miner,Yixuan J. Hou,Longping V. Tse,Hannah Kaiser,Haiying Zhu,Joyce Y C Lu,Bhanupriya Madarampalli,Arnold Park,Florian A. Lempp,Russell St Germain,Emily L Bossard,Jia Jin Kee,Kurt Diem,Andrew B. Stuart,Peter B. Rupert,Chance Brock,Matthew Buerger,Margaret K. Doll,April K. Randhawa,Leonidas Stamatatos,Roland K. Strong,Colleen McLaughlin,Meei-Li Huang,Keith R. Jerome,Keith R. Jerome,Ralph S. Baric,David C. Montefiori,Lawrence Corey,Lawrence Corey +31 more
TL;DR: Head-to-head evaluation of different SARS-CoV-2 neutralization platforms could facilitate comparisons across studies and laboratories, and high concordance between the outcomes of cell-based assays with live and pseudotyped virions enables valid cross-study comparison using these platforms.
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Variant SARS-CoV-2 mRNA vaccines confer broad neutralization as primary or booster series in mice
Kai Wu,Angela Choi,Matthew A. Koch,Sayda Elbashir,LingZhi Ma,Diana Lee,Angela Woods,Carole Henry,Charis Palandjian,Anna Hill,Julian Quinones,Naveen Nunna,Sarah O’Connell,Adrian B. McDermott,Samantha Falcone,Elisabeth Narayanan,Tonya M. Colpitts,Hamilton Bennett,Kizzmekia S. Corbett,Robert A. Seder,Barney S. Graham,Guillaume Stewart-Jones,Andrea Carfi,Darin K. Edwards +23 more
TL;DR: In this paper, the authors evaluated two updated COVID-19 mRNA vaccines designed to target emerging SARS-CoV-2 variants: (1) monovalent mRNA-1273.351 encodes for the S protein found in the B.1.351 lineage and (2) mRNA- 1273.211 was most effective at providing broad cross-variant neutralization in mice.
References
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