叶林柏
病毒感染和致病的关系、基因工程药物及抗病毒药物等
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- 姓名:叶林柏
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博士生导师
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学科领域:
光学
- 研究兴趣:病毒感染和致病的关系、基因工程药物及抗病毒药物等
叶林柏,男,武汉大学教授,武汉大学病毒研究所所长,武汉大学和美国UNC大学联合培养博士。1970年获武汉大学生物学学士学位,1981年获武汉大学病毒及分子生物学专业硕士学位,1985-1986加拿大Queen’s大学访问研究员,1990-1994作为在职博士到美国北卡大学医学院肿瘤研究中心工作,主要的研究方向:病毒感染和致病的关系、基因工程药物及抗病毒药物等,已发表研究论文近100篇,曾先后获国家自然科学二等奖、教育部科技进步一等奖等多项奖,获国家新药证书一项,著有《分子生物学》、《基础分子生物学》、《分子生物学模拟试题与详解》等著作三部,专利3项。
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叶林柏
,-0001,():
-1年11月30日
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叶林柏, Jing Liu, Fan Yang, Lin-Bai Ye∗, Xiao-Jun Yang, Khalid A. Timani, Yi Zheng, Yu-Hua Wang
Journal of Ethnopharmacology 95(2004)265-272,-0001,():
-1年11月30日
A bioactive fraction (GLPG) was extracted and purified from the mycelia of Ganoderma lucidum by EtOH precipitation and DEAEcellulose column chromatography. GLPG was a proteoglycan and had a carbohydrate:protein ratio of 10.4:1. Its antiviral activities against herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) were investigated by the cytopathic effect (CPE) inhibition assay in cell culture. This kind of polysaccharide inhibited the development of the cytopathic effect in dose-dependent manner in HSV-infected cells, moreover did not show any cytotoxic effects on cells even when a concentration was as high as 2000 ug/ml. In order to study the possible mode of action of the antiviral activity of GLPG, cells were treated with GLPG before, during and after infection, and the viral titers in the supernatant of cell culture 48 h post-infection were tested by TCID50 assay. The antiviral effects in pre-treated and treated during virus infection with GLPG were more remarkable than the treatment of post-infection. Although the precise mechanism has yet to be defined, our work suggested that GLPG inhibits viral replication by interfering with the early events of viral adsorption and entry into target cells. Thus, this proteoglycan seems to be a potential candidate for anti-HSV agents.
Ganoderma lucidum proteoglycan (, GLPG), , Antiherpetic activity, Herpes simplex viruses, Cytopathic effect (, CPE), , TCID50
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【期刊论文】Hepatitis C Virus Non-structural Protein NS4B Can Modulate an Unfolded Protein Response
叶林柏, Yi Zheng, Bo Gao, Li Ye, Lingbao Kong, Wei Jing, Xiaojun Yang, Zhenghui Wu and Linbai Ye*
The Journal of Microbiology, December 2005, p.529-536,-0001,():
-1年11月30日
Viral infection causes stress to the endoplasmic reticulum (ER). The response to endoplasmic reticulum stress, known as the unfolded protein response (UPR), is designed to eliminate misfolded proteins and allow the cell to recover. The role of hepatitis C virus (HCV) non-structural protein NS4B, a component of the HCV replicons that induce UPR, is incompletely understood. We demonstrate that HCV NS4B could induce activating transcription factor (ATF6) and inositol-requiring enzyme 1 (IRE1), to favor the HCV subreplicon and HCV viral replication. HCV NS4B activated the IRE1 pathway, as indicated by splicing of X box-binding protein (Xbp-1) mRNA. However, transcriptional activation of the XBP-1 target gene, EDEM (ER degradation-enhancing α-mannosidase-like protein, a protein degradation factor), was inhibited. These results imply that NS4B might induce UPR through ATF6 and IRE1-XBP1 pathways, but might also modify the outcome to benefit HCV or HCV subreplicon replication.
hepatitis C virus (, HCV), , non-structural protein NS4B, unfolded protein response (, UPR),
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叶林柏, Khalid Amine Timani, Qingjiao Liao, Linbai Ye*, Yingchun Zeng, Jing Liu, Yi Zheng, Li Ye, Xiaojun Yang, Kong Lingbao, Jingrong Gao, Ying Zhu
Virus Research 114(2005)23-34,-0001,():
-1年11月30日
Anovel coronavirus (CoV) has recently been identified as the aetiological agent of severe acute respiratory syndrome (SARS). Nucleocapsid (N) proteins of the Coronaviridae family have no discernable homology, but they share a common nucleolar-cytoplasmic distribution pattern. There are three putative nuclear localization signal (NLS) motifs present in the N. To determine the role of these putative NLSs in the intracellular localization of the SARS-CoV N, we performed a confocal microscopy analysis using rabbit anti-N antisera. In this report, we show that the wild type N was distributed mainly in the cytoplasm. The N-terminal of the N, which contains the NLS1 (aa38-44), was localized to the nucleus. The C-terminus of the N, which contains both NLS2 (aa257-265) and NLS3 (aa369-390) was localized to the cytoplasm and the nucleolus. Results derived from analysis of various deletion mutations show that the region containing amino acids 226-289 is able to mediate nucleolar localization. The deletion of two hydrophobic regions that flanked the NLS3 recovered its activity and localized to the nucleus. Furthermore, deletion of leucine rich region (220-LALLLLDRLNRL) resulted in the accumulation of N to the cytoplasm and nucleolus, and when fusing this peptide to EGFP localization was cytoplasmic, suggesting that the N may act as a shuttle protein. Differences in nuclear/nucleolar localization properties of N from other members of coronavirus family suggest a unique function for N, which may play an important role in the pathogenesis of SARS.
SARS-CoV, Nucleocapsid protein, Nuclear localization signal, Nucleolar localization, Cell cycle arrest
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叶林柏, Khalid Amine Timani a, Li Yea, Linbai Ye a, *, Ying Zhua, Zhenghui Wu a, Zuojiong Gongb
Journal of Clinical Virology 30(2004)309-312,-0001,():
-1年11月30日
Anovel coronavirus has been associated with aworldwide outbreak of atypical pneumonia referred to as Severe Acute Respiratory Syndrome (SARS-CoV). SARS-CoV nucleocapsid (N) protein has been cloned sequenced and expressed in Escherichia coli strain. PurifiedNproteinwas used to measure the SARS-CoV specific IgG antibodies from 16 SARS-CoV infected patients'sera and from 131 control subjects using ELISA assay. Specific antibody responses to the purified recombinant N protein after 10, 20, and 30 days of disease onset were observed in 13 of 16 (81.3%), 16 of 16 (100%) and 16 of 16 (100%) SARS patients sera, respectively. Comparison of detection results with a commercially available diagnostic kit coated with a mixture of SARS-CoV viral proteins showed 9 of 16 (56.3%), 13 of 16 (81.3%), and 15 of 16 (93.7%) positive responses, respectively. None of 131 control sera gave positive reaction in either assay. This data suggests that the N protein of SARS-CoV is immunodominant and this ELISA based test assay for detecting the SARS-CoV N antigen may hold a significant value for SARS diagnosis.
SARS-CoV, Nucleocapsid protein, Expression and purification, ELISA
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