INTERNAL FUSION PEPTIDE OF THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 中心，不一定是研究者的机构。 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。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. 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.