Structural basis for SARS-CoV-2 Delta variant recognition of ACE2 receptor and broadly neutralizing antibodies
Published 2022 View Full Article
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Title
Structural basis for SARS-CoV-2 Delta variant recognition of ACE2 receptor and broadly neutralizing antibodies
Authors
Keywords
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Journal
Nature Communications
Volume 13, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2022-02-15
DOI
10.1038/s41467-022-28528-w
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Note: Only part of the references are listed.- Development and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections
- (2021) Chao Zhang et al. Nature Communications
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- (2021) Piyada Supasa et al. CELL
- Genomic characterization of a novel SARS-CoV-2 lineage from Rio de Janeiro, Brazil
- (2021) Carolina M. Voloch et al. JOURNAL OF VIROLOGY
- Emergence of a SARS-CoV-2 variant of concern with mutations in spike glycoprotein
- (2021) Houriiyah Tegally et al. NATURE
- Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England
- (2021) Nicholas G. Davies et al. SCIENCE
- Antibody evasion by the P.1 strain of SARS-CoV-2
- (2021) Wanwisa Dejnirattisai et al. CELL
- Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization
- (2021) Pengfei Wang et al. Cell Host & Microbe
- Structural basis for the different states of the spike protein of SARS-CoV-2 in complex with ACE2
- (2021) Renhong Yan et al. CELL RESEARCH
- Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice
- (2021) Phillip Pymm et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structural impact on SARS-CoV-2 spike protein by D614G substitution
- (2021) Jun Zhang et al. SCIENCE
- Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies
- (2021) Xing Zhu et al. PLOS BIOLOGY
- Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum
- (2021) Chang Liu et al. CELL
- Increased transmissibility and global spread of SARS-CoV-2 variants of concern as at June 2021
- (2021) Finlay Campbell et al. Eurosurveillance
- Reduced sensitivity of SARS-CoV-2 variant Delta to antibody neutralization
- (2021) Delphine Planas et al. NATURE
- Daily briefing: Why the Delta variant spreads so fast
- (2021) Flora Graham NATURE
- SARS-CoV-2 variants of concern are emerging in India
- (2021) Jasdeep Singh et al. NATURE MEDICINE
- Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
- (2021) Meng Yuan et al. SCIENCE
- SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
- (2021) Matthew McCallum et al. SCIENCE
- Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity
- (2021) Sophie M.-C. Gobeil et al. SCIENCE
- Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
- (2021) Yongfei Cai et al. SCIENCE
- Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies
- (2021) Gabriele Cerutti et al. STRUCTURE
- The Spike of Concern—The Novel Variants of SARS-CoV-2
- (2021) Anna Winger et al. Viruses-Basel
- Molecular Level Dissection of Critical Spike Mutations in SARS‐CoV‐2 Variants of Concern (VOCs): A Simplified Review
- (2021) Nilesh Joshi et al. ChemistrySelect
- Conformational dynamics of the Beta and Kappa SARS-CoV-2 spike proteins and their complexes with ACE2 receptor revealed by cryo-EM
- (2021) Yifan Wang et al. Nature Communications
- Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2
- (2020) Renhong Yan et al. SCIENCE
- Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
- (2020) Daniel Wrapp et al. SCIENCE
- Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
- (2020) Qihui Wang et al. CELL
- Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
- (2020) Alexandra C. Walls et al. CELL
- Identification of Human Single-Domain Antibodies against SARS-CoV-2
- (2020) Yanling Wu et al. Cell Host & Microbe
- A human neutralizing antibody targets the receptor binding site of SARS-CoV-2
- (2020) Rui Shi et al. NATURE
- Human neutralizing antibodies elicited by SARS-CoV-2 infection
- (2020) Bin Ju et al. NATURE
- Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
- (2020) Dora Pinto et al. NATURE
- Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
- (2020) Jun Lan et al. NATURE
- Structural basis of receptor recognition by SARS-CoV-2
- (2020) Jian Shang et al. NATURE
- A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2
- (2020) Yan Wu et al. SCIENCE
- Coronavirus membrane fusion mechanism offers a potential target for antiviral development
- (2020) Tiffany Tang et al. ANTIVIRAL RESEARCH
- Potently neutralizing and protective human antibodies against SARS-CoV-2
- (2020) Seth J. Zost et al. NATURE
- SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects
- (2020) Antoni G. Wrobel et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies
- (2020) Alina Baum et al. SCIENCE
- Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail
- (2020) Johanna Hansen et al. SCIENCE
- Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody
- (2020) Zhe Lv et al. SCIENCE
- Distinct conformational states of SARS-CoV-2 spike protein
- (2020) Yongfei Cai et al. SCIENCE
- Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant
- (2020) Leonid Yurkovetskiy et al. CELL
- Structurally Resolved SARS-CoV-2 Antibody Shows High Efficacy in Severely Infected Hamsters and Provides a Potent Cocktail Pairing Strategy
- (2020) Shuo Du et al. CELL
- Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
- (2020) Donald J. Benton et al. NATURE
- Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein
- (2020) Christine Toelzer et al. SCIENCE
- Cryo-EM Structures of SARS-CoV-2 Spike without and with ACE2 Reveal a pH-Dependent Switch to Mediate Endosomal Positioning of Receptor-Binding Domains
- (2020) Tongqing Zhou et al. Cell Host & Microbe
- Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM
- (2020) Cong Xu et al. Science Advances
- MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
- (2017) Shawn Q Zheng et al. NATURE METHODS
- cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
- (2017) Ali Punjani et al. NATURE METHODS
- UCSF ChimeraX: Meeting modern challenges in visualization and analysis
- (2017) Thomas D. Goddard et al. PROTEIN SCIENCE
- A pipeline approach to single-particle processing inRELION
- (2017) Rafael Fernandez-Leiro et al. Acta Crystallographica Section D-Structural Biology
- G196 epitope tag system: a novel monoclonal antibody, G196, recognizes the small, soluble peptide DLVPR with high affinity
- (2017) Kasumi Tatsumi et al. Scientific Reports
- CTFFIND4: Fast and accurate defocus estimation from electron micrographs
- (2015) Alexis Rohou et al. JOURNAL OF STRUCTURAL BIOLOGY
- Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement
- (2015) Frank DiMaio et al. NATURE METHODS
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
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