EMD-26794
Tomogram of platelet filopodia in presence of SARS-CoV-2 spike protein
EMD-26794
Tomography
Deposition: 27/04/2022Map released: 15/02/2023
Last modified: 15/02/2023
Sample Organism:
Homo sapiens,
Severe acute respiratory syndrome coronavirus 2
Sample: Platelet deformation induced by SARS-CoV-2 spike protein
Raw data: EMPIAR-11038
Deposition Authors: Kuhn CC, Basnet N, Bodakuntla S
,
Nichols S,
Martinez-Sanchez A ,
Agostini L ,
Soh YM ,
Takagi J ,
Biertumpfel C ,
Mizuno N
Sample: Platelet deformation induced by SARS-CoV-2 spike protein
Raw data: EMPIAR-11038
Deposition Authors: Kuhn CC, Basnet N, Bodakuntla S
,
Nichols S,
Martinez-Sanchez A ,
Agostini L ,
Soh YM ,
Takagi J ,
Biertumpfel C ,
Mizuno N
Direct Cryo-ET observation of platelet deformation induced by SARS-CoV-2 spike protein.
Kuhn CC,
Basnet N,
Bodakuntla S ,
Alvarez-Brecht P,
Nichols S,
Martinez-Sanchez A ,
Agostini L ,
Soh YM ,
Takagi J ,
Biertumpfel C ,
Mizuno N
(2023) Nat Commun , 14 , 620 - 620
,
Alvarez-Brecht P,
Nichols S,
Martinez-Sanchez A ,
Agostini L ,
Soh YM ,
Takagi J ,
Biertumpfel C ,
Mizuno N
(2023) Nat Commun , 14 , 620 - 620
Abstract:
SARS-CoV-2 is a novel coronavirus responsible for the COVID-19 pandemic. Its high pathogenicity is due to SARS-CoV-2 spike protein (S protein) contacting host-cell receptors. A critical hallmark of COVID-19 is the occurrence of coagulopathies. Here, we report the direct observation of the interactions between S protein and platelets. Live imaging shows that the S protein triggers platelets to deform dynamically, in some cases, leading to their irreversible activation. Cellular cryo-electron tomography reveals dense decorations of S protein on the platelet surface, inducing filopodia formation. Hypothesizing that S protein binds to filopodia-inducing integrin receptors, we tested the binding to RGD motif-recognizing platelet integrins and find that S protein recognizes integrin αvβ3. Our results infer that the stochastic activation of platelets is due to weak interactions of S protein with integrin, which can attribute to the pathogenesis of COVID-19 and the occurrence of rare but severe coagulopathies.
SARS-CoV-2 is a novel coronavirus responsible for the COVID-19 pandemic. Its high pathogenicity is due to SARS-CoV-2 spike protein (S protein) contacting host-cell receptors. A critical hallmark of COVID-19 is the occurrence of coagulopathies. Here, we report the direct observation of the interactions between S protein and platelets. Live imaging shows that the S protein triggers platelets to deform dynamically, in some cases, leading to their irreversible activation. Cellular cryo-electron tomography reveals dense decorations of S protein on the platelet surface, inducing filopodia formation. Hypothesizing that S protein binds to filopodia-inducing integrin receptors, we tested the binding to RGD motif-recognizing platelet integrins and find that S protein recognizes integrin αvβ3. Our results infer that the stochastic activation of platelets is due to weak interactions of S protein with integrin, which can attribute to the pathogenesis of COVID-19 and the occurrence of rare but severe coagulopathies.