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Nature:MERS-CoV与CD26受体的结合

  1. Nature
  2. 受体

来源:Nature中文网 2013-08-08 14:20

到2013年7月中旬,被最近出现的类似SARS的“中东呼吸综合症冠状病毒” (MERS-CoV) 感染的90个病例已被确认,其中包括43个死亡病例。ACE2 (angiotensin converting enzyme 2) 对SARS冠状病毒起一个细胞表面受体的作用,但MERS-CoV的功能受体是“二肽基肽酶-4”,亦称为CD26。

到2013年7月中旬,被最近出现的类似SARS的“中东呼吸综合症冠状病毒” (MERS-CoV) 感染的90个病例已被确认,其中包括43个死亡病例。ACE2 (angiotensin converting enzyme 2) 对SARS冠状病毒起一个细胞表面受体的作用,但MERS-CoV的功能受体是“二肽基肽酶-4”,亦称为CD26。这篇论文介绍了MERS-CoV刺突蛋白的受体结合域的晶体结构(包括自由状态和与该受体相结合状态的结构)。这些结构显示了一个“核心子域”,与SARS-CoV刺突蛋白的“核心子域”同源,同时还显示了一个独特的、由链支配的(strand-dominated)外部受体结合主题,其作用是识别CD26。一个适当折叠的“受体结合域”也许具有用在一种MERS-CoV疫苗中、充当一个“免疫原”的潜力。(生物谷 Bioon.com)

生物谷推荐的英文摘要

Nature  doi:10.1038/nature12328

Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26

Guangwen Lu,  Yawei Hu,  Qihui Wang,  Jianxun Qi,  Feng Gao,  Yan Li,  Yanfang Zhang,  Wei Zhang,  Yuan Yuan,  Jinku Bao,  Buchang Zhang,  Yi Shi,  Jinghua Yan  & George F. Gao

The newly emergent Middle East respiratory syndrome coronavirus (MERS-CoV) can cause severe pulmonary disease in humans1, 2, representing the second example of a highly pathogenic coronavirus, the first being SARS-CoV3. CD26 (also known as dipeptidyl peptidase 4, DPP4) was recently identified as the cellular receptor for MERS-CoV4. The engagement of the MERS-CoV spike protein with CD26 mediates viral attachment to host cells and virus–cell fusion, thereby initiating infection. Here we delineate the molecular basis of this specific interaction by presenting the first crystal structures of both the free receptor binding domain (RBD) of the MERS-CoV spike protein and its complex with CD26. Furthermore, binding between the RBD and CD26 is measured using real-time surface plasmon resonance with a dissociation constant of 16.7 nM. The viral RBD is composed of a core subdomain homologous to that of the SARS-CoV spike protein, and a unique strand-dominated external receptor binding motif that recognizes blades IV and V of the CD26 β-propeller. The atomic details at the interface between the two binding entities reveal a surprising protein–protein contact mediated mainly by hydrophilic residues. Sequence alignment indicates, among betacoronaviruses, a possible structural conservation for the region homologous to the MERS-CoV RBD core, but a high variation in the external receptor binding motif region for virus-specific pathogenesis such as receptor recognition.

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