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-Structure paper
タイトル | Direct Cryo-ET observation of platelet deformation induced by SARS-CoV-2 spike protein. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 620, Year 2023 |
掲載日 | 2023年2月4日 |
著者 | Christopher Cyrus Kuhn / Nirakar Basnet / Satish Bodakuntla / Pelayo Alvarez-Brecht / Scott Nichols / Antonio Martinez-Sanchez / Lorenzo Agostini / Young-Min Soh / Junichi Takagi / Christian Biertümpfel / Naoko Mizuno / |
PubMed 要旨 | 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 ...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 αβ. 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. |
リンク | Nat Commun / PubMed:36739444 / PubMed Central |
手法 | EM (トモグラフィー) / EM (単粒子) |
解像度 | 3.56 Å |
構造データ | EMDB-26794: Tomogram of platelet filopodia in presence of SARS-CoV-2 spike protein EMDB-26796: Tomogram of platelet protrusion with microtubule in presence of SARS-CoV-2 spike protein EMDB-26798: SARS-CoV-2 spike protein closed conformation |
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