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

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

Publication date: Oct 22, 2024

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.

Concepts Keywords
Affinity ACE2
Coronavirus ACE2 protein, human
Epidemiology Actins
Inactivation Actins
Radixin Angiotensin-Converting Enzyme 2
Angiotensin-Converting Enzyme 2
Cell stiffness
Cortical actin
COVID-19
Cytoskeletal Proteins
Cytoskeletal Proteins
ERM
ezrin
Humans
Membrane Proteins
Membrane Proteins
Microfilament Proteins
Microfilament Proteins
moesin
Phosphorylation
Protein Binding
Protein Domains
radixin
SARS-CoV-2
SARS-CoV-2
Spike Glycoprotein, Coronavirus
Spike Glycoprotein, Coronavirus
spike protein, SARS-CoV-2

Semantics

Type Source Name
disease MESH viral infection
disease MESH infection
disease IDO protein
disease IDO cell
disease MESH COVID-19

Original Article

(Visited 1 times, 1 visits today)