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Hum Cell . Interaction of SARS-CoV-2 Spike protein with ACE2 induces cortical actin modulation, including dephosphorylation of ERM proteins and red

tetano

Editor, Senior Moderator
Hum Cell


. 2024 Oct 22;38(1):3.
doi: 10.1007/s13577-024-01142-2. Interaction of SARS-CoV-2 Spike protein with ACE2 induces cortical actin modulation, including dephosphorylation of ERM proteins and reduction of cortical stiffness

Thi Ly Do[SUP] 1 [/SUP], Kouichi Tachibana[SUP] 2 [/SUP], Norio Yamamoto[SUP] 3 [/SUP], Kiyoshi Ando[SUP] 2 [/SUP], Takaaki Isoda[SUP] 1 [/SUP], Takanori Kihara[SUP] 4 [/SUP]



Affiliations
Abstract

Cell surface cortical actin is a regulatory target for viral infection. We aimed to investigate the effect of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection on host cell cortical stiffness, an indicator of cortical actin structure. The receptor-binding domain (RBD) of SARS-CoV-2 Spike (S) protein induced a reduction in cortical stiffness in ACE2-expressing cells. The interaction of RBD with ACE2 caused the inactivation of Ezrin/Radixin/Moesin (ERM) proteins. We further investigated the effects of the RBD of SARS-CoV-2 Omicron variants, BA.1 and BA.5. These RBDs influenced cortical stiffness depending on their affinity for ACE2. Our study provides the first evidence that the interaction of the SARS-CoV-2 S protein with ACE2 induces mechanobiological signals and attenuates the cortical actin.

Keywords: ACE2; Cell stiffness; Cortical actin; ERM; SARS-CoV-2.

 
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