BROME MOSAIC VIRUS

雀麦花叶病毒

• 批准号: 8168582
• 负责人: Cheng C Kao
• 金额: $ 2.15万
• 依托单位: BAYLOR COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-01-15 至 2010-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8168582
• 关键词: Arginine; Biological; Brome mosaic virus; Capsid; Charge; Collaborations; Computer Retrieval of Information on Scientific Projects Database; Funding; Goals; Grant; Image; Institution; Mutation; N-terminal; Property; RNA; Research; Research Personnel; Resources; Roentgen Rays; Source; Structure; United States National Institutes of Health; Viral; Virion; alpha helix; arm; interest; mutant; particle; protein structure; viral RNA

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 made a mutant Brome mosaic virus (BMV) that has an interesting biological property. The mutations increase the positive charges inside the viral particles through the addition of two alpha-helices in the N-terminal arginine-rich arm in the capsid subunit of BMV. The X-ray crystal structure of the protein shell of BMV has been solved, but there is no information on the inner layer of RNA and how the N-terminal arm interacts with the RNA. We propose a collaboration where we can use cryo-EM to image and reconstruct the wild-type and mutant BMV. We will then trace the N-terminal arm of the two particles and identify how it interacts with RNA. The goal of this project is to visualize this N-terminal arm that is critical for interaction with the packaged viral RNAs and the structure of the RNAs inside the virion.

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 研究中心，而研究中心不一定是研究者所在的机构。 我们已经取得了一个突变体雀麦花叶病毒（BMV），具有一个有趣的生物学特性。这些突变通过在BMV衣壳亚基的N-末端富含丝氨酸的臂中添加两个α-螺旋来增加病毒颗粒内的正电荷。BMV的蛋白质外壳的X射线晶体结构已经解决，但没有关于RNA内层以及N-末端臂如何与RNA相互作用的信息。 我们提出了一个合作，我们可以使用cryo-EM图像和重建野生型和突变体BMV。 然后，我们将追踪这两个粒子的N-末端臂，并确定它如何与RNA相互作用。 这个项目的目标是可视化这个N-末端臂，它对于与包装的病毒RNA的相互作用和病毒粒子内RNA的结构至关重要。