阿尔法冠状病毒的包膜蛋白的跨膜形状,NL63
Iva Sučec1, Yanina Pankratova1, Mriganka Parasar1
1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Protein science : a publication of the Protein Society
|March 19, 2024
概括
人类冠状病毒NL63包裹 (E) 蛋白形成了一个稳定的α-螺旋结构. 在酸性pH值下其有限的水可访问性表明离子通道活性较弱,这可能解释了与SARS-CoV相比病毒毒性较低.
科学领域:
- 结构生物学是结构生物学.
- 病毒学 病毒学
- 生物物理学的生物物理.
背景情况:
- 冠状病毒 (CoV) 包膜 (E) 蛋白质是病毒蛋白,形成与致病性相关的离子通道.
- CoV E 蛋白质的高分辨率结构很少,以前只有 SARS-CoV E 蛋白质的特征.
研究的目的:
- 为了确定人类冠状病毒 (hCoV) NL63 E蛋白 (NL63 ETM) 的构造和离子通道特性.
- 将NL63 ETM的结构和功能特征与SARS-CoV ETM的结构和功能特征进行比较.
主要方法:
- 利用二维和三维的魔法角旋转NMR测量13C和15N的化学转移,确定NL63 ETM的骨干扭转角度 (φ, ψ).
- 在中性和酸性pH值下,在Ca2+离子的存在下,评估了NL63 ETM在水中的可达性.
主要成果:
- NL63 ETM采用稳定的α-螺旋形状,独立于pH值和N端的ectodomain.
- NL63 ETM的水可达性显示,与Ca2+的酸性pH仅略有增加,与SARS ETM不同,它变得显著更水.
结论:
- 与SARS ETM相比,NL63 ETM的结构稳定性和有限的pH依赖性水合表明其阴离子通道导电性较弱.
- 这种E蛋白通道活性的差异可能导致hCoV-NL63感染相对于SARS-CoV的病毒性较低.
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