ArticleeLife2023
Lys417 acts as a molecular switch that regulates the conformation of SARS-CoV-2 spike protein.
Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 11 citations in OpenAlex.
- Update and reuse: Structure-guided nanobody evolution against SARS-CoV-2 escape.PLoS pathogens · 2026Article
- Structural basis for bat receptor recognition by SARS-CoV-2 and bat SARS2-like coronaviruses.Communications biology · 2026Article
- Using Machine Learning to Analyze Molecular Dynamics Simulations of Biomolecules.The journal of physical chemistry. B · 2025Article
- Structural and Energetic Insights into SARS-CoV-2 Evolution: Analysis of hACE2-RBD Binding in Wild-Type, Delta, and Omicron Subvariants.International journal of molecular sciences · 2025Article
- Biophysics of SARS-CoV-2 spike protein's receptor-binding domain interaction with ACE2 and neutralizing antibodies: from computation to functional insights.Biophysical reviews · 2025Review
- Adaptive evolution of SARS-CoV-2 during a persistent infection for 521 days in an immunocompromised patient.NPJ genomic medicine · 2025Article
- Discovery of Nanosota-9 as anti-Omicron nanobody therapeutic candidate.PLoS pathogens · 2024Article
- Dual-role epitope on SARS-CoV-2 spike enhances and neutralizes viral entry across different variants.PLoS pathogens · 2024Article
- Structure-guided in vitro evolution of nanobodies targeting new viral variants.PLoS pathogens · 2024Article
- Structural basis for mouse receptor recognition by bat SARS2-like coronaviruses.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural basis for raccoon dog receptor recognition by SARS-CoV-2.PLoS pathogens · 2024Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
SARS-CoV-2 spike protein plays a key role in mediating viral entry and inducing host immune responses. It can adopt either an open or closed conformation based on the position of its receptor-binding domain (RBD). It is yet unclear what causes these conformational changes or how they influence the spike's functions. Here, we show that Lys417 in the RBD plays dual roles in the spike's structure: it stabilizes the closed conformation of the trimeric spike by mediating inter-spike-subunit interactions; it also directly interacts with ACE2 receptor. Hence, a K417V mutation has opposing effects on the spike's function: it opens up the spike for better ACE2 binding while weakening the RBD's direct binding to ACE2. The net outcomes of this mutation are to allow the spike to bind ACE2 with higher probability and mediate viral entry more efficiently, but become more exposed to neutralizing antibodies. Given that residue 417 has been a viral mutational hotspot, SARS-CoV-2 may have been evolving to strike a balance between infection potency and immune evasion, contributing to its pandemic spread.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.