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Structural analysis of receptor binding domain mutations in SARS-CoV-2 variants of concern that modulate ACE2 and antibody binding.
<div class='caption-title'>The global prevalence of SARS-CoV-2 VoC/VoI RBD mutations and their locations within the S protein</div>
<div class='caption-title'>Complete sets of VoC/VoI RBD mutations increase S protein trimer-ACE2 binding affinity</div>
Mannar D, Saville JW, Zhu X, Srivastava SS, Berezuk AM, Zhou S, Tuttle KS, Kim A, Li W, Dimitrov DS, Subramaniam S
OpenAccess logo Cell Rep 37 110156 (2021)
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Cited: 45 times
EuropePMC logo PMID: 34914928

Abstract

The recently emerged severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) Beta (B.1.351) and Gamma (P.1) variants of concern (VoCs) include a key mutation (N501Y) found in the Alpha (B.1.1.7) variant that enhances affinity of the spike protein for its receptor, angiotensin-converting enzyme 2 (ACE2). Additional mutations are found in these variants at residues 417 and 484 that appear to promote antibody evasion. In contrast, the Epsilon variants (B.1.427/429) lack the N501Y mutation yet exhibit antibody evasion. We have engineered spike proteins to express these receptor binding domain (RBD) VoC mutations either in isolation or in different combinations and analyze the effects using biochemical assays and cryoelectron microscopy (cryo-EM) structural analyses. Overall, our findings suggest that the emergence of new SARS-CoV-2 variant spikes can be rationalized as the result of mutations that confer increased ACE2 affinity, increased antibody evasion, or both, providing a framework to dissect the molecular factors that drive VoC evolution.

Articles - 7sxv mentioned but not cited (1)

  1. Structural analysis of receptor binding domain mutations in SARS-CoV-2 variants of concern that modulate ACE2 and antibody binding. Mannar D, Saville JW, Zhu X, Srivastava SS, Berezuk AM, Zhou S, Tuttle KS, Kim A, Li W, Dimitrov DS, Subramaniam S. Cell Rep 37 110156 (2021)


Reviews citing this publication (7)

  1. Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants. Ghimire D, Han Y, Lu M. Viruses 14 1255 (2022)
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  6. Exploring the Structural Variability of Dynamic Biological Complexes by Single-Particle Cryo-Electron Microscopy. DiIorio MC, Kulczyk AW. Micromachines (Basel) 14 118 (2022)
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Articles citing this publication (37)

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  19. Conformational Flexibility and Local Frustration in the Functional States of the SARS-CoV-2 Spike B.1.1.7 and B.1.351 Variants: Mutation-Induced Allosteric Modulation Mechanism of Functional Dynamics and Protein Stability. Verkhivker G. Int J Mol Sci 23 1646 (2022)
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