tetano
Editor, Senior Moderator
Cells
. 2024 Aug 7;13(16):1318.
doi: 10.3390/cells13161318. Interaction of Receptor-Binding Domain of the SARS-CoV-2 Omicron Variant with hACE2 and Actin
Ai Fujimoto[SUP] 1 [/SUP], Haruki Kawai[SUP] 1 [/SUP], Rintaro Kawamura[SUP] 1 [/SUP], Akira Kitamura[SUP] 2 3 [/SUP]
Affiliations
The omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was identified in 2021 as a variant with heavy amino acid mutations in the spike protein, which is targeted by most vaccines, compared to previous variants. Amino acid substitutions in the spike proteins may alter their affinity for host viral receptors and the host interactome. Here, we found that the receptor-binding domain (RBD) of the omicron variant of SARS-CoV-2 exhibited an increased affinity for human angiotensin-converting enzyme 2, a viral cell receptor, compared to the prototype RBD. Moreover, we identified β- and γ-actin as omicron-specific binding partners of RBD. Protein complex predictions revealed that many omicron-specific amino acid substitutions affected the affinity between RBD of the omicron variant and actin. Our findings indicate that proteins localized to different cellular compartments exhibit strong binding to the omicron RBD.
Keywords: COVID-19; actin; fluorescence correlation spectroscopy; protein–protein interaction; spike protein.
. 2024 Aug 7;13(16):1318.
doi: 10.3390/cells13161318. Interaction of Receptor-Binding Domain of the SARS-CoV-2 Omicron Variant with hACE2 and Actin
Ai Fujimoto[SUP] 1 [/SUP], Haruki Kawai[SUP] 1 [/SUP], Rintaro Kawamura[SUP] 1 [/SUP], Akira Kitamura[SUP] 2 3 [/SUP]
Affiliations
- PMID: 39195208
- DOI: 10.3390/cells13161318
The omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was identified in 2021 as a variant with heavy amino acid mutations in the spike protein, which is targeted by most vaccines, compared to previous variants. Amino acid substitutions in the spike proteins may alter their affinity for host viral receptors and the host interactome. Here, we found that the receptor-binding domain (RBD) of the omicron variant of SARS-CoV-2 exhibited an increased affinity for human angiotensin-converting enzyme 2, a viral cell receptor, compared to the prototype RBD. Moreover, we identified β- and γ-actin as omicron-specific binding partners of RBD. Protein complex predictions revealed that many omicron-specific amino acid substitutions affected the affinity between RBD of the omicron variant and actin. Our findings indicate that proteins localized to different cellular compartments exhibit strong binding to the omicron RBD.
Keywords: COVID-19; actin; fluorescence correlation spectroscopy; protein–protein interaction; spike protein.