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Spike protein of the SARS-CoV-2 omicron variant interacts with actin
Ai Fujimoto
Haruki Kawai
Rintaro Kawamura
Akira Kitamura
Acceso Abierto
Atribución-NoComercial-SinDerivadas
https://doi.org/10.1101/2024.05.16.594608
https://www.biorxiv.org/content/10.1101/2024.05.16.594608v1
Abstract The omicron variant of SARS-CoV-2 is responsible for the COVID-19 pandemic, serving as a significant origin for the variants still being detected today. It affects the spike protein that most vaccines used to target when the Omicron strain was discovered. Here, we demonstrate that the receptor binding domain (RBD) of the Omicron variant of SARS-CoV-2 exhibits an increased affinity for human angiotensin-converting enzyme type 2 (hACE2) as a viral cell receptor compared to the prototype RBD. We also identified that β- and γ-actin are Omicron-specific binding partners of RBD. Protein complex predictions suggested that many of the Omicron-specific amino acid substitutions might be involved in the affinity of RBD and actin. Accordingly, we highlight the intriguing observation that proteins expected to localize to different cellular compartments exhibit strong binding.
bioRxiv
17-05-2024
Preimpreso
Inglés
Público en general
VIRUS RESPIRATORIOS
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