刺突 MERS 冠状病毒受体。
Spiking the MERS-coronavirus receptor.
机构信息
Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3508 TD Utrecht, the Netherlands.
出版信息
Cell Res. 2013 Sep;23(9):1069-70. doi: 10.1038/cr.2013.108. Epub 2013 Aug 13.
Abstract
A novel coronavirus, the Middle East respiratory syndrome coronavirus, recently emerged through zoonotic transmission, causing a severe lower respiratory tract infection in humans. In two recent papers, one published in Cell Research, the crystal structure of the viral receptor-binding domain in complex with the host CD26/dipeptidyl peptidase 4 receptor has now been characterized.
摘要
一种新型冠状病毒，即中东呼吸综合征冠状病毒，最近通过动物源传播出现，导致人类发生严重的下呼吸道感染。在最近的两篇论文中，一篇发表在《细胞研究》上，现已对病毒受体结合域与宿主 CD26/二肽基肽酶 4 受体复合物的晶体结构进行了描述。
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本文引用的文献
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Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.MERS-CoV 刺突受体结合域与人受体 DPP4 复合物的结构。
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Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26.新型人类冠状病毒 MERS-CoV 与其受体 CD26 结合的分子基础。
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The receptor binding domain of the new Middle East respiratory syndrome coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing antibodies.新型中东呼吸综合征冠状病毒的受体结合域位于刺突蛋白的 231 个残基区域，该区域能有效地引发中和抗体。
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Isolation of a novel coronavirus from a man with pneumonia in Saudi Arabia.从沙特阿拉伯一名患有肺炎的男子中分离出一种新型冠状病毒。
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Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2.严重急性呼吸综合征冠状病毒适应人类血管紧张素转换酶2的受体及病毒决定因素。
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Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.人二肽基肽酶IV/CD26与底物类似物复合物的晶体结构
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