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1Identification of an epitope of SARS-coronavirus nucleocapsid protein显示文摘The nucleocapsid (N) protein of severe acute respiratory syndrome-coronavirus (SARS-CoV) is a majorvirion structural protein. In this study, two epitopes (N1 and N2) of the N protein of SARS-CoV werepredicted by bioinformatics analysis. After immunization with two peptides, the peptides-specific antibodieswere isolated from the immunized rabbits. The further experiments demonstrated that N1 peptide-inducedpolyclonal antibodies had a high affinity to bind to E. coli expressed N protein of SARS-CoV. Furthermore, itwas confirmed that N1 peptide-specific IgG antibodies were detectable in the sera of severe acute respiratorysyndrome (SARS) patients. The results indicated that an epitope of the N protein has been identified andN protein specific Abs were produced by peptide immunization, which will be useful for the study of SARS-CoV.YINGLIN XuSHEN RUIFuYANG YIXUELI YONGYONGJI YouYuHE MuDESHI WEILU TIELIUSHI BINGSUN JINWANG HONGXIAWANG HUALIANGJIANG JIANHUASHEN YOUHUAXIE YUANWANG GANGPEI BBIFENSHEN JIARUIWU 2003Cell Research2003,13,3:22
2LRH-1/hB1F and HNF1 synergistically up-regulate hepatitis B virus gene transcription and DNA replication显示文摘Enhancer Ⅱ(ENII)is one of the critical cis-elements in the Hepatitis B Virus(HBV)genome for the hepatic viral gene transcription and DNA replication.The liver-specific activity of ENII is regulated by multiple liver-enriched transcription factors,including LRH-1/hB 1 F,HNF 1,HNF3β,HNF4 and C/EBP.Knowledge on the interplay of these important factors is still limited.In this study,we demonstrate a functional synergism between the orphan nuclear receptor LRH-1/hB 1F and the homeoprotein HNF1 in up-regulating the liver-specific activity of ENII.This synergism is sufficient for initiating the viral gene transcription and DNA replication in non-hepatic cells.We have defined the activation domains in hB 1F and HNF 1 that contribute to the synergism.We further show that hB 1F and HNF1 can interact directly in vitro and have mapped the domains required for this interaction.YANNINGCAI QINGZHOU YUYINGKONG MEILI BENOITVIOLLET YOUHUAXIE YUANWANG 2003Cell Research2003,13,6:6
331nstitute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Taiyuan Road,Shanghai 200031, China.显示文摘 Spike protein is one of the major structural proteins of severe acute respiratory syndrome-coronavirus. It is essential for the interaction of the virons with host cell receptors and subsequent fusion of the viral envelop with host cell membrane to allow infection. Some spike proteins of coronavirus, such as MHV, HCoV-OC43, AIBV and BcoV, are proteolytically cleaved into two subunits, S 1 and S2. In contrast, TGV, FIPV and HCoV-229E are not. Many studies have shown that the cleavage of spike protein seriously affects its function. In order to investigate the maturation and proteolytic processing of the S protein of SARS CoV, we generated S 1 and S2 subunit specific antibodies (Abs) as well as N, E and 3CL protein-specific Abs. Our results showed that the antibodies could efficiently and specifically bind to their corresponding proteins from E.coli expressed or lysate of SARS-CoV infected Vero-E6 cells by Western blot analysis. Furthermore, the anti-S 1 and S2 Abs were proved to be capable of binding to SARS CoV under electron microscope observation. When S2 Ab was used to perform immune precipitation with lysate of SARS-CoV infected cells, a cleaved S2 fragment was detected with S2-specific mAb by Western blot analysis. The data demonstrated that the cleavage of S protein was observed in the lysate, indicating that proteolytic processing of S protein is present in host cells.XiaoDongWU BoSHANG RuiFuYANG HaoYU ZhiHalMA XuSHEN YongYongJI YingLIN YaDiWU GuoMeiLIN LinTIAN XiaoQingGAN ShengYANG WeiHongJIANG ErHeiDAI XiaoYiWANG HuaLiangJIANG YouHuaXIE XueLiangZHU GangPEI LinLI JiaRuiWU BingSUN 2004Cell Research2004,14,5:0
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