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データを開く
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基本情報
| 登録情報 | データベース: PDB / ID: 6m39 | ||||||
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| タイトル | Cryo-EM structure of SADS-CoV spike | ||||||
要素 | Spike glycoprotein | ||||||
キーワード | VIRAL PROTEIN / SADS-CoV spike | ||||||
| 機能・相同性 | 機能・相同性情報host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated virion attachment to host cell / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion membrane / membrane 類似検索 - 分子機能 | ||||||
| 生物種 | Swine acute diarrhea syndrome coronavirus (ウイルス) | ||||||
| 手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.55 Å | ||||||
データ登録者 | Ouyang, S. / Hongxin, G. | ||||||
| 資金援助 | 中国, 1件
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引用 | ジャーナル: J Virol / 年: 2020タイトル: Cryo-electron Microscopy Structure of the Swine Acute Diarrhea Syndrome Coronavirus Spike Glycoprotein Provides Insights into Evolution of Unique Coronavirus Spike Proteins. 著者: Hongxin Guan / Youwang Wang / Vanja Perčulija / Abdullah F U H Saeed / Yichang Liu / Jinyu Li / Syed Sajid Jan / Yu Li / Ping Zhu / Songying Ouyang / ![]() 要旨: Coronaviruses (CoV) have caused a number of major epidemics in humans and animals, including the current pandemic of coronavirus disease 2019 (COVID-19), which has brought a renewed focus on the ...Coronaviruses (CoV) have caused a number of major epidemics in humans and animals, including the current pandemic of coronavirus disease 2019 (COVID-19), which has brought a renewed focus on the evolution and interspecies transmission of coronaviruses. Swine acute diarrhea syndrome coronavirus (SADS-CoV), which was recently identified in piglets in southern China, is an alphacoronavirus that originates from the same genus of horseshoe bats as severe acute respiratory syndrome CoV (SARS-CoV) and that was reported to be capable of infecting cells from a broad range of species, suggesting a considerable potential for interspecies transmission. Given the importance of the coronavirus spike (S) glycoprotein in host range determination and viral entry, we report a cryo-electron microscopy (cryo-EM) structure of the SADS-CoV S trimer in the prefusion conformation at a 3.55-Å resolution. Our structure reveals that the SADS-CoV S trimer assumes an intrasubunit quaternary packing mode in which the S1 subunit N-terminal domain (S1-NTD) and the S1 subunit C-terminal domain (S1-CTD) of the same protomer pack together by facing each other in the lying-down state. SADS-CoV S has several distinctive structural features that may facilitate immune escape, such as a relatively compact architecture of the S trimer and epitope masking by glycan shielding. Comparison of SADS-CoV S with the spike proteins of the other coronavirus genera suggested that the structural features of SADS-CoV S are evolutionarily related to those of the spike proteins of the other genera rather than to the spike protein of a typical alphacoronavirus. These data provide new insights into the evolutionary relationship between spike glycoproteins of SADS-CoV and those of other coronaviruses and extend our understanding of their structural and functional diversity. In this article, we report the atomic-resolution prefusion structure of the spike protein from swine acute diarrhea syndrome coronavirus (SADS-CoV). SADS-CoV is a pathogenic alphacoronavirus that was responsible for a large-scale outbreak of fatal disease in pigs and that was reported to be capable of interspecies transmission. We describe the overall structure of the SADS-CoV spike protein and conducted a detailed analysis of its main structural elements. Our results and analyses are consistent with those of previous phylogenetic studies and suggest that the SADS-CoV spike protein is evolutionarily related to the spike proteins of betacoronaviruses, with a strong similarity in S1-NTDs and a marked divergence in S1-CTDs. Moreover, we discuss the possible immune evasion strategies used by the SADS-CoV spike protein. Our study provides insights into the structure and immune evasion strategies of the SADS-CoV spike protein and broadens the understanding of the evolutionary relationships between coronavirus spike proteins of different genera. | ||||||
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構造の表示
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| 構造ビューア | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 6m39.cif.gz | 507 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb6m39.ent.gz | 413.2 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 6m39.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
| その他 | その他のダウンロード |
-検証レポート
| 文書・要旨 | 6m39_validation.pdf.gz | 2.4 MB | 表示 | wwPDB検証レポート |
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| 文書・詳細版 | 6m39_full_validation.pdf.gz | 2.4 MB | 表示 | |
| XML形式データ | 6m39_validation.xml.gz | 84.6 KB | 表示 | |
| CIF形式データ | 6m39_validation.cif.gz | 124.4 KB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/m3/6m39 ftp://data.pdbj.org/pub/pdb/validation_reports/m3/6m39 | HTTPS FTP |
-関連構造データ
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リンク
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集合体
| 登録構造単位 | ![]()
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要素
| #1: タンパク質 | 分子量: 108920.773 Da / 分子数: 3 / 由来タイプ: 組換発現 由来: (組換発現) Swine acute diarrhea syndrome coronavirus (ウイルス)発現宿主: Insect cell expression vector pTIE1 (その他) 参照: UniProt: A0A2P1G7F5 #2: 糖 | ChemComp-NAG / 研究の焦点であるリガンドがあるか | Y | Has protein modification | Y | |
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-実験情報
-実験
| 実験 | 手法: 電子顕微鏡法 |
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| EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
| 構成要素 | 名称: SADS-CoV spike trimer / タイプ: COMPLEX / Entity ID: #1 / 由来: RECOMBINANT |
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| 由来(天然) | 生物種: Swine acute diarrhea syndrome coronavirus (ウイルス) |
| 由来(組換発現) | 生物種: Insect cell expression vector pTIE1 (その他) |
| 緩衝液 | pH: 7.5 |
| 試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
| 急速凍結 | 凍結剤: ETHANE |
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電子顕微鏡撮影
| 実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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| 顕微鏡 | モデル: FEI TITAN KRIOS |
| 電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
| 電子レンズ | モード: BRIGHT FIELD |
| 撮影 | 電子線照射量: 60 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
| CTF補正 | 詳細: Gctf / タイプ: NONE |
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| 3次元再構成 | 解像度: 3.55 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 35000 / 対称性のタイプ: POINT |
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万見について




Swine acute diarrhea syndrome coronavirus (ウイルス)
中国, 1件
引用
UCSF Chimera







PDBj


