INTERNAL FUSION PEPTIDE OF THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS

严重急性呼吸系统综合症冠状病毒的内部融合肽

• 批准号: 8364059
• 负责人: MAOCHEN GE
• 金额: $ 0.08万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-09-01 至 2012-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8364059
• 关键词: C-terminal; Characteristics; Cleaved cell; Coronavirus; Coronavirus spike protein; Funding; Grant; Link; Lipids; Location; Mediating; Mutagenesis; N-terminal; National Center for Research Resources; Peptides; Principal Investigator; Protein S; Proteins; Relative (related person); Reporting; Research; Research Infrastructure; Resources; SARS coronavirus; Severe Acute Respiratory Syndrome; Site; Source; Technology; United States National Institutes of Health; Viral; Viral Fusion Proteins; cost; synthetic peptide

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. We have initiated a study of lipid interactions of a synthetic peptide corresponding to the internal fusion peptide from SARS-CoV (IFP18). Fusion peptide can be classified as an N-terminal or internal, depending on their location relative to the cleavage site of the viral fusion protein. The coronavirus spike protein (S) protein is known to be cleaved at the S1/S2 boundary. This cleavage site is not closely linked to a fusion peptide. It was reported that a synthetic peptide, consisting of 18 resides, immediately C-terminal to a second S2 cleavage site of SARS-CoV (IFP18), promotes lipid mixing. Mutagenesis studies showed that some conserved residues in this sequence of SARS-CoV are critical in viral fusion mediated by SARS-Cov. Thus, this peptide was suggested to be an internal fusion peptide [1]. [1] Madu, I.G., S.L. Roth, S. Belouzard, and G.R. Whittaker. 2009. Characterization of highly conserved domains within the severe acute respiratory syndrome coronavirus spike protein S2 domain with characteristics of a viral fusion peptide. J. Virol. 83:7411-7421.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 我们已经开始了一个合成肽的脂质相互作用的研究，对应于内部融合肽从SARS-CoV（IFP 18）。融合肽可根据其相对于病毒融合蛋白切割位点的位置分为N-末端或内部。已知冠状病毒刺突蛋白（S）蛋白在S1/S2边界处被切割。该切割位点不与融合肽紧密连接。据报道，由18个残基组成的合成肽，紧邻SARS-CoV的第二个S2切割位点（IFP 18）的C-末端，促进脂质混合。突变研究表明，该序列中的一些保守残基在SARS-CoV介导的病毒融合中起关键作用。因此，该肽被认为是内部融合肽[1]。 [1]Madu，I. G.，S.L. Roth，S. Belouzard和G.R.惠特克2009.具有病毒融合肽特征的严重急性呼吸综合征冠状病毒刺突蛋白S2结构域内高度保守结构域的表征J. Virol. 83：7411-7421。