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学科主题: 基础医学
题名:
A study on antigenicity and receptor-binding ability of fragment 450-650 of the spike protein of SARS coronavirus
作者: Zhao, Jincun1; Wang, Wei1; Yuan, Zhihong1; Jia, Rujing1; Zhao, Zhendong1; Xu, Xiaojun1; Lv, Ping1; Zhang, Yan1; Jiang, Chengyu1; Gao, Xiao-Ming1
关键词: SARS-CoV ; S protein ; receptor-binding motif ; B cell epitope
刊名: VIROLOGY
发表日期: 2007-03-15
DOI: 10.1016/j.virol.2006.09.022
卷: 359, 期:2, 页:362-370
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Virology
研究领域[WOS]: Virology
关键词[WOS]: ACUTE RESPIRATORY SYNDROME ; ANGIOTENSIN-CONVERTING ENZYME-2 ; POTENT NEUTRALIZING ANTIBODIES ; SYNTHETIC PEPTIDES ; S-PROTEIN ; IDENTIFICATION ; EPITOPES ; DOMAIN ; GLYCOPROTEIN
英文摘要:

The spike (S) protein of SARS coronavirus (SARS-CoV) is responsible for viral binding with ACE2 molecules. Its receptor-binding motif (S-RBM) is located between residues 424 and 494, which folds into 2 anti-parallel beta-sheets, beta 5 and beta 6. We have previously demonstrated that fragment 450-650 of the S protein (S450-650) is predominantly recognized by convalescent sera of SARS patients. The N-terminal 60 residues (450-510) of the S450-650 fragment covers the entire 6 strand of S-RBM. In the present study, we demonstrate that patient sera predominantly recognized 2 linear epitopes outside the 6 fragment, while the mouse antisera, induced by immunization of BALB/c mice with recombinant S450-650, mainly recognized the beta 6 strand-containing region. Unlike patient sera, however, the mouse antisera were unable to inhibit the infectivity of S protein-expressing (SARS-CoV-S) pseudovirus. Fusion protein between green fluorescence protein (GFP) and S450-650 (S450-650-GFP) was able to stain Vero E6 cells and deletion of the beta 6 fragment rendered the fusion product (S511-650-GFP) unable to do so. Similarly, recombinant S450-650, but not S511-650, was able to block the infection of Vero E6 cells by the SARS-CoV-S pseudovirus. Co-precipitation experiments confirmed that S450-650 was able to specifically bind with ACE2 molecules in lysate of Vero E6 cells. However, the ability of S450-510, either alone or in fusion with GFP, to bind with ACE2 was significantly poorer compared with S450-650. Our data suggest a possibility that, although the beta 6 strand alone is able to bind with ACE2 with relatively high affinity, residues outside the S-RBM could also assist the receptor binding of SARS-CoV-S protein. (c) 2006 Elsevier Inc. All rights reserved.

语种: 英语
WOS记录号: WOS:000244816400012
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/52201
Appears in Collections:基础医学院_免疫学系_期刊论文

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作者单位: 1.Peking Univ, Hlth Sci Ctr, Dept Immunol, Beijing 100083, Peoples R China
2.Peking Union Med Coll, Inst Basic Med Sci, Beijing, Peoples R China

Recommended Citation:
Zhao, Jincun,Wang, Wei,Yuan, Zhihong,et al. A study on antigenicity and receptor-binding ability of fragment 450-650 of the spike protein of SARS coronavirus[J]. VIROLOGY,2007,359(2):362-370.
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