Publication in refereed journal
香港中文大学研究人员 ( 现职)
| 韦妙宜教授 (那打素护理学院) |
| 陈基湘教授 (微生物学系) |
| 徐国荣教授 (生物医学学院) |
| 冯国培教授 (生物医学学院) |
全文
| 数位物件识别号 (DOI) http://dx.doi.org/10.1159/000151530 |
引用次数
Web of Sciencehttp://aims.cuhk.edu.hk/converis/portal/Publication/1WOS source URL
其它资讯
摘要The outbreak of severe acute respiratory syndrome (SARS), caused by a distinct coronavirus, in 2003 greatly threatened public health in China, Southeast Asia as well as North America. Over http://aims.cuhk.edu.hk/converis/portal/Publication/1,000 patients died of the SARS virus, representing http://aims.cuhk.edu.hk/converis/portal/Publication/10% of infected people. Like other coronaviruses, the SARS virus also utilizes a surface glycoprotein, namely the spike protein, to infect host cells. The spike protein of SARS virus consists of http://aims.cuhk.edu.hk/converis/portal/Publication/1,255 amino acid residues and can be divided into two sub-domains, Shttp://aims.cuhk.edu.hk/converis/portal/Publication/1 and S2. The Shttp://aims.cuhk.edu.hk/converis/portal/Publication/1 domain mediates the binding of the virus to its receptor angiotensin-converting enzyme 2, which is abundantly distributed on the surface of human lung cells. The S2 domain mediates membrane fusion between the virus and the host cell. Hence two strategies can be used to block the infection of the SARS virus, either by interfering with the binding of the Shttp://aims.cuhk.edu.hk/converis/portal/Publication/1 domain to the receptor or by blocking the fusion of the virus with the cell membrane mediated by the S2 domain. Several antibodies against the Shttp://aims.cuhk.edu.hk/converis/portal/Publication/1 domain have been generated and all of them are able to neutralize the virus in vitro and in vivo using animal models. Unfortunately, point mutations have been identified in the Shttp://aims.cuhk.edu.hk/converis/portal/Publication/1 domain, so that the virus isolated in the future may not be recognized by these antibodies. As no mutation has been found in the S2 domain indicating that this region is more conserved than the Shttp://aims.cuhk.edu.hk/converis/portal/Publication/1 domain, it may be a better target for antibody binding. After predicting the immunogenicity of the epitopes of the S2 domain, we chemically synthesized two peptides and also expressed one of them using a recombinant DNA method. We screened a phage displaying library of human single-chain antibodies (ScFv) against the predicted epitopes and obtained a human ScFv which can recognize the SARS virus in vitro. Copyright (C) 2008 S. Karger AG, Basel.
着者Leung KM, Feng DX, Lou JL, Zhou Y, Fung KP, Waye MMY, Tsui SKW, Chan PKS, Marks JD, Pang SF, Kan YW
期刊名称INTERVIROLOGY
出版年份2008
月份http://aims.cuhk.edu.hk/converis/portal/Publication/1
日期http://aims.cuhk.edu.hk/converis/portal/Publication/1
卷号5http://aims.cuhk.edu.hk/converis/portal/Publication/1
期次3
出版社Karger Publishers
页次http://aims.cuhk.edu.hk/converis/portal/Publication/173 - http://aims.cuhk.edu.hk/converis/portal/Publication/18http://aims.cuhk.edu.hk/converis/portal/Publication/1
国际标準期刊号0300-5526
语言英式英语
关键词antibody; immunology; severe acute respiratory syndrome; single-chain variable fragment
Web of Science 学科类别Virology; VIROLOGY
