+検索条件
-Structure paper
タイトル | In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges. |
---|---|
ジャーナル・号・ページ | Science, Vol. 370, Issue 6513, Page 203-208, Year 2020 |
掲載日 | 2020年10月9日 |
著者 | Beata Turoňová / Mateusz Sikora / Christoph Schürmann / Wim J H Hagen / Sonja Welsch / Florian E C Blanc / Sören von Bülow / Michael Gecht / Katrin Bagola / Cindy Hörner / Ger van Zandbergen / Jonathan Landry / Nayara Trevisan Doimo de Azevedo / Shyamal Mosalaganti / Andre Schwarz / Roberto Covino / Michael D Mühlebach / Gerhard Hummer / Jacomine Krijnse Locker / Martin Beck / |
PubMed 要旨 | The spike protein (S) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is required for cell entry and is the primary focus for vaccine development. In this study, we combined cryo- ...The spike protein (S) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is required for cell entry and is the primary focus for vaccine development. In this study, we combined cryo-electron tomography, subtomogram averaging, and molecular dynamics simulations to structurally analyze S in situ. Compared with the recombinant S, the viral S was more heavily glycosylated and occurred mostly in the closed prefusion conformation. We show that the stalk domain of S contains three hinges, giving the head unexpected orientational freedom. We propose that the hinges allow S to scan the host cell surface, shielded from antibodies by an extensive glycan coat. The structure of native S contributes to our understanding of SARS-CoV-2 infection and potentially to the development of safe vaccines. |
リンク | Science / PubMed:32817270 / PubMed Central |
手法 | EM (サブトモグラム平均) |
解像度 | 4.9 - 7.9 Å |
構造データ | EMDB-11222: EMDB-11223: EMDB-11347: |