The Cytoplasmic Domain of the SARS-CoV-2 Envelope Protein Assembles into a β-Sheet Bundle in Lipid Bilayers.
The Cytoplasmic Domain of the SARS-CoV-2 Envelope Protein Assembles into a β-Sheet Bundle in Lipid Bilayers.
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DOI：
10.1016/j.jmb.2023.167966
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发表时间：
2023-03-01
影响因子：
5.6
通讯作者：
Hong, Mei
中科院分区：
文献类型：
--
作者：
Dregni, Aurelio J.;McKay, Matthew J.;Surya, Wahyu;Queralt-Martin, Maria;Medeiros-Silva, Joao;Wang, Harrison K.;Aguilella, Vicente;Torres, Jaume;Hong, Mei
严重的急性呼吸综合征冠状病毒2（SARS-COV-2）包膜（E）蛋白在内质网的脂质膜中形成五聚离子通道。这些功能的基础，在这里我们研究了E的构象和动力学蛋白质构造（残基8-65）包含跨膜结构域，大多数使用固态NMR和15N化学移位的细胞质结构域。循环无序的NMR光谱蛋白质的C末端的第三个β链是很好的水合，表明它在β-束的表面上无法从这里获得的含糊不清，因此在此相互作用的相互作用是构造的，因此，在此相互构造的含糊之处，这是从这里获得的。这些联系人数据表明，当蛋白质在脂质双层中以高浓度存在时，SARS-COV-2 E蛋白的细胞质结构域具有强烈的希望。
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) envelope (E) protein forms a pentameric ion channel in the lipid membrane of the endoplasmic reticulum Golgi intermediate compartment (ERGIC) of the infected cell. The cytoplasmic domain of E interacts with host proteins to cause virus pathogenicity and may also mediate virus assembly and budding. To understand the structural basis of these functions, here we investigate the conformation and dynamics of an E protein construct (residues 8–65) that encompasses the transmembrane domain and the majority of the cytoplasmic domain using solid-state NMR. 13C and 15N chemical shifts indicate that the cytoplasmic domain adopts a β-sheet-rich conformation that contains three β-strands separated by turns. The five subunits associate into an umbrella-shaped bundle that is attached to the transmembrane helices by a disordered loop. Water-edited NMR spectra indicate that the third β-strand at the C terminus of the protein is well hydrated, indicating that it is at the surface of the β-bundle. The structure of the cytoplasmic domain cannot be uniquely determined from the inter-residue correlations obtained here due to ambiguities in distinguishing intermolecular and intramolecular contacts for a compact pentameric assembly of this small domain. Instead, we present four structural topologies that are consistent with the measured inter-residue contacts. These data indicate that the cytoplasmic domain of the SARS-CoV-2 E protein has a strong propensity to adopt β-sheet conformations when the protein is present at high concentrations in lipid bilayers. The equilibrium between the β-strand conformation and the previously reported α-helical conformation may underlie the multiple functions of E in the host cell and in the virion.
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影响因子：
2.7
作者：
Helmus JJ;Jaroniec CP
通讯作者：
Jaroniec CP
影响因子：
3.7
作者：
Godet M;L'Haridon R;Vautherot JF;Laude H
通讯作者：
Laude H
影响因子：
2.2
作者：
Hou, Guangjin;Yan, Si;Trebosc, Julien;Amoureux, Jean-Paul;Polenova, Tatyana
通讯作者：
Polenova, Tatyana
DPC和SDS胶束中SARS Corona病毒E蛋白的C末端尾部的9分组合肽的自组装的结构见解：一项高分辨率和低分辨率光谱研究。
DOI：
10.1016/j.bbamem.2017.10.015
发表时间：
2018-03
期刊：
Biochimica et biophysica acta. Biomembranes
影响因子：
--
作者：
Ghosh A;Bhattacharyya D;Bhunia A
通讯作者：
Bhunia A
影响因子：
5.9
作者：
Javorsky A;Humbert PO;Kvansakul M
通讯作者：
Kvansakul M