Characterization and Fluctuations of an Ivermectin Binding Site at the Lipid Raft Interface of the N-Terminal Domain (NTD) of the Spike Protein of SARS-CoV-2 Variants DOI Creative Commons

Marine Lefebvre,

Henri Chahinian, Bernard La Scola

et al.

Viruses, Journal Year: 2024, Volume and Issue: 16(12), P. 1836 - 1836

Published: Nov. 27, 2024

Most studies on the docking of ivermectin spike protein SARS-CoV-2 concern receptor binding domain (RBD) and, more precisely, RBD interface recognized by ACE2 receptor. The N-terminal (NTD), which controls initial attachment virus to lipid raft gangliosides, has not received attention it deserves. In this study, we combined molecular modeling and physicochemical approaches analyze mode interaction with NTD-facing rafts host cell membrane. We characterize a area that presents point mutations deletions in successive variants from strain omicron KP.3 circulating many countries 2024. show exceptional flexibility, allowing drug bind all tested. energy is specific each variant, classification according their affinity for following ascending order: Omicron < Delta BA.5 Alpha Wuhan (B.1) BA.1. site subject important variations NTD, including Y144 deletion. It overlaps ganglioside as demonstrated studies. These results suggest new mechanism antiviral action based competitive inhibition rafts. current variant still ivermectin, although an slightly lower than strain.

Language: Английский

On the new SARS-CoV-2 variant KP.3.1.1: focus on its genetic potential DOI
Francesco Branda, Massimo Ciccozzi, Fabio Scarpa

et al.

Infectious Diseases, Journal Year: 2024, Volume and Issue: 56(10), P. 903 - 906

Published: Aug. 15, 2024

Language: Английский

Citations

3
Recent SARS-CoV-2 evolution trajectories indicate the emergence of Omicron’s several subvariants and the current rise of KP.3.1.1 and XEC DOI
Chiranjib Chakraborty, Manojit Bhattacharya, Ali S. Abdelhameed

et al.

Virology, Journal Year: 2025, Volume and Issue: unknown, P. 110508 - 110508

Published: March 1, 2025

Language: Английский

Citations

0
Genetic variability of the recombinant SARS-CoV-2 XEC: is it a new evolutionary dead-end lineage? DOI Creative Commons
Francesco Branda, Massimo Ciccozzi, Fabio Scarpa

et al.

New Microbes and New Infections, Journal Year: 2024, Volume and Issue: 62, P. 101520 - 101520

Published: Oct. 30, 2024

Language: Английский

Citations

2
Characterization and Fluctuations of an Ivermectin Binding Site at the Lipid Raft Interface of the N-Terminal Domain (NTD) of the Spike Protein of SARS-CoV-2 Variants DOI Creative Commons

Marine Lefebvre,

Henri Chahinian, Bernard La Scola

et al.

Viruses, Journal Year: 2024, Volume and Issue: 16(12), P. 1836 - 1836

Published: Nov. 27, 2024

Most studies on the docking of ivermectin spike protein SARS-CoV-2 concern receptor binding domain (RBD) and, more precisely, RBD interface recognized by ACE2 receptor. The N-terminal (NTD), which controls initial attachment virus to lipid raft gangliosides, has not received attention it deserves. In this study, we combined molecular modeling and physicochemical approaches analyze mode interaction with NTD-facing rafts host cell membrane. We characterize a area that presents point mutations deletions in successive variants from strain omicron KP.3 circulating many countries 2024. show exceptional flexibility, allowing drug bind all tested. energy is specific each variant, classification according their affinity for following ascending order: Omicron < Delta BA.5 Alpha Wuhan (B.1) BA.1. site subject important variations NTD, including Y144 deletion. It overlaps ganglioside as demonstrated studies. These results suggest new mechanism antiviral action based competitive inhibition rafts. current variant still ivermectin, although an slightly lower than strain.

Language: Английский

Citations

0