Structural Immunology of SARS‐CoV‐2

Immunological Reviews, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 27, 2024

The SARS-CoV-2 spike (S) protein has undergone significant evolution, enhancing both receptor binding and immune evasion. In this review, we summarize ongoing efforts to develop antibodies targeting various epitopes of the S protein, focusing on their neutralization potency, breadth, escape mechanisms. Antibodies receptor-binding site (RBS) typically exhibit high neutralizing potency but are frequently evaded by mutations in variants. contrast, conserved regions, such as S2 stem helix fusion peptide, broader reactivity generally lower potency. However, several broadly have demonstrated exceptional efficacy against emerging variants, including latest omicron subvariants, underscoring potential vulnerable sites RBS-A RBS-D/CR3022. We also highlight public classes different protein. targeted present opportunities for germline-targeting vaccine strategies. Overall, developing escape-resistant, potent effective vaccines remains crucial combating future This review emphasizes importance identifying key utilizing antibody affinity maturation inform therapeutic design.

Language: Английский

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The biophysical landscape of viral evolution

Proceedings of the National Academy of Sciences, Journal Year: 2024, Volume and Issue: 121(27)

Published: June 24, 2024

Language: Английский

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Epitope mapping via in vitro deep mutational scanning methods and its applications

Journal of Biological Chemistry, Journal Year: 2024, Volume and Issue: unknown, P. 108072 - 108072

Published: Dec. 1, 2024

Language: Английский

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Decoding the SARS-CoV-2 Infection Process: Insights into Origin, Spread, and Therapeutic Approaches

Microbial Pathogenesis, Journal Year: 2025, Volume and Issue: unknown, P. 107328 - 107328

Published: Jan. 1, 2025

Language: Английский

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The fusion peptide of the spike protein S2 domain may be a mimetic analog of β-coronaviruses and serve as a novel virus-host membrane fusion inhibitor

Antiviral Research, Journal Year: 2025, Volume and Issue: unknown, P. 106144 - 106144

Published: March 1, 2025

Language: Английский

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A quantitative comparison of the deleteriousness of missense and nonsense mutations using the structurally resolved human protein interactome

Protein Science, Journal Year: 2025, Volume and Issue: 34(6)

Published: May 19, 2025

Abstract The complex genotype‐to‐phenotype relationships in Mendelian diseases can be elucidated by mutation‐induced disturbances to the networks of molecular interactions (interactomes) human cells. Missense and nonsense mutations cause distinct perturbations within protein interactome, leading functional phenotypic effects with varying degrees severity. Here, we structurally resolve interactome at atomic‐level resolutions perform structural thermodynamic calculations assess biophysical implications these mutations. We focus on a specific type missense mutation, known as “quasi‐null” mutations, which destabilize proteins similar consequences (node removal) propose “fold difference” quantification deleteriousness, measures ratio between fractions node‐removal datasets disease‐causing non‐pathogenic estimate fold differences range from 3 (for quasi‐null folding ΔΔG ≥2 kcal/mol) 20 mutations). observe strong positive correlation destabilization demonstrating that deleteriousness spans continuous spectrum, extreme (highly deleterious) end. Our findings substantiate disparity severity suggest is indicative outcomes analyses allow for potential identification whose removal or lead harmful phenotypes, enabling development targeted therapeutic approaches, enhancing comprehension intricate mechanisms governing clinically relevant diseases.

Language: Английский

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ROC-guided virtual screening, molecular dynamics simulation, and bioactivity validation assessment Z195914464 as a 3CL Mpro inhibitor

Biophysical Chemistry, Journal Year: 2024, Volume and Issue: 317, P. 107357 - 107357

Published: Nov. 23, 2024

Language: Английский

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