Structural and Functional Insights into the Evolution of SARS-CoV-2 KP.3.1.1 Spike Protein DOI Creative Commons
Zi‐Qi Feng, Jiachen Huang, Sabyasachi Baboo

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 10, 2024

Summary The JN.1-sublineage KP.3.1.1 recently emerged as the globally prevalent SARS-CoV-2 variant, demonstrating increased infectivity and antibody escape. We investigated how mutations a deletion in spike protein (S) affect ACE2 binding Mass spectrometry revealed new glycan site at residue N30 altered glycoforms neighboring N61. Cryo-EM structures showed that rearrangement of adjacent residues did not significantly change overall structure, up-down ratio receptor-binding domains (RBDs), or binding. Furthermore, S structure with hACE2 further confirmed an epistatic effect between F456L Q493E on Our analysis shows variants after late 2023 are now incorporating reversions to found other sarbecoviruses, including glycan, Q493E, others. Overall, these results inform structural functional consequences mutations, current evolutionary trajectory, immune evasion.

Language: Английский

The JN.1 variant of COVID-19: immune evasion, transmissibility, and implications for global health DOI Creative Commons
A. Siddiqui,

Imshaal Musharaf,

Bashar Haruna Gulumbe

et al.

Therapeutic Advances in Infectious Disease, Journal Year: 2025, Volume and Issue: 12

Published: Jan. 1, 2025

The emergence of the COVID-19 JN.1 variant has raised global health concerns as it gains prevalence in several regions worldwide. First identified August 2023, evolved from Omicron lineage's BA.2.86 subvariant. Patients infected with commonly exhibit symptoms such sore throat, fever, dry cough, nausea, and vomiting. While World Health Organization labeled a Variant Interest, currently presents low risk. However, its increased transmissibility, particularly cold, climates, is concerning. This review provides comprehensive overview JN.1's biological characteristics, epidemiology, immune evasion, efficacy existing antiviral treatments vaccination strategies. A literature search across key databases targeted studies January 2023 to 2024, emphasizing recent insights into spread clinical impact. Findings reveal that exhibits higher infectivity evasion than previous variants, largely due L4555 mutation. From November March showed an increasing trend transmission. Previously approved antivirals, including Paxlovid, Veklury, Lagevrio, demonstrate effectiveness against JN.1, current vaccines still protect severe illness this variant. rates remain low. Monitoring efforts include genomic assessments, wastewater surveillance, digital tracking contain variant's spread. It essential encourage public maintain preventive measures reduce Continued research critical for understanding managing evolving landscape emerging variants.

Language: Английский

Citations

0
The Omicron variant BA.2.86.1 of SARS- CoV-2 demonstrates an altered interaction network and dynamic features to enhance the interaction with the hACE2 DOI Creative Commons
Taimur Khan, Muhammad Shahab, Ahmad M. Alharbi

et al.

Scientific Reports, Journal Year: 2025, Volume and Issue: 15(1)

Published: Feb. 22, 2025

Language: Английский

Citations

0
Regional Dynamics and Mechanisms Behind SARS-CoV-2 XDV.1 Prevalence in Chongqing via Genomic Surveillance and Molecular Insights DOI Creative Commons
Yan Jin, Fangyuan Liu,

Sihan Hu

et al.

Virus Research, Journal Year: 2025, Volume and Issue: unknown, P. 199562 - 199562

Published: March 1, 2025

Language: Английский

Citations

0
Structural and Functional Insights into the Evolution of SARS-CoV-2 KP.3.1.1 Spike Protein DOI Creative Commons
Zi‐Qi Feng, Jiachen Huang, Sabyasachi Baboo

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 10, 2024

Summary The JN.1-sublineage KP.3.1.1 recently emerged as the globally prevalent SARS-CoV-2 variant, demonstrating increased infectivity and antibody escape. We investigated how mutations a deletion in spike protein (S) affect ACE2 binding Mass spectrometry revealed new glycan site at residue N30 altered glycoforms neighboring N61. Cryo-EM structures showed that rearrangement of adjacent residues did not significantly change overall structure, up-down ratio receptor-binding domains (RBDs), or binding. Furthermore, S structure with hACE2 further confirmed an epistatic effect between F456L Q493E on Our analysis shows variants after late 2023 are now incorporating reversions to found other sarbecoviruses, including glycan, Q493E, others. Overall, these results inform structural functional consequences mutations, current evolutionary trajectory, immune evasion.

Language: Английский

Citations

2