Mechanism of the ribonucleoprotein complex formation of SARS-CoV2 N protein

2023 Fiscal Year Final Research Report

• Project/Area Number: 21H02438
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Single-year Grants
• Section: 一般
• Review Section: Basic Section 43040:Biophysics-related
• Research Institution: Tohoku University
• Principal Investigator: Takahashi Satoshi 東北大学, 多元物質科学研究所, 教授 (30283641)
• Project Period (FY): 2021-04-01 – 2024-03-31
• Keywords: SARS-Cov2 / Nタンパク質 / gRNA / 一分子蛍光分光法 / 蛍光相関分光法

Outline of Final Research Achievements

Interaction between N and RNA fragments with stem-loop and single-stranded structures was investigated. A method for the purification of the N protein was established. The single-molecule FRET spectroscopy and fluorescence correlation spectroscopy showed that N bind with RNA samples strongly irrespective of their secondary structures, and that N attracts two RNA fragments. The results suggest that the function of N is to bind and to attract two parts of the long gRNA and help its compaction. Experimental methods such as fluorescence correlation spectroscopy and single molecule fluorescence spectroscopy have been used to investigate the structure of long RNAs.

Free Research Field

生物物理

Academic Significance and Societal Importance of the Research Achievements

本研究を実施することで、コロナウイルスの複製に必須の働きをもつNタンパク質の機能をより正確に理解することが可能となった。さらには、gRNAとNタンパク質が結合することで、gRNAがフォールディングを起こしてRNPを形成するgRNAのフォールディング仮説を提案した。この仮説を今後証明できれば、ウイルスの成熟過程を阻害するための効果的な方法を提案できる可能性がある。