Molecular ans stractural basis of beta-barrel membrane pore-forming proteins for design of cell-specific nanotools.

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K14897
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Applied biochemistry
• Research Institution: Tohoku University
• Principal Investigator: Kaneko Jun 東北大学, 農学研究科, 准教授 (30221188)
• Project Period (FY): 2016-04-01 – 2018-03-31
• Keywords: β-PFTs / 膜孔形成機構

Outline of Final Research Achievements

Molecular mechanism of beta-barrel membrane pore-forming toxin of Staphylococcus aureus was investigated.
In target cell specificity, loop 4 of Hlg2 and LukE rim domain, which contacts with host cell surface, was essential to binding to human erythrocytes, and loop1 and 2 were found to be assisting the binding. We also found that the interaction between Asp in the cap region involved in the prestem retention in LukF and basic amino acids in the adjacent Hlg2 cap site by membrane pore formation involved in the prestem release of γ-hemolysin. Furthermore, double cysteine mutant of α-hemolysin capable of regulating the release of prestem was constructed. Using this system, now the residues involved in the stem insertion are being analyzed.

Free Research Field

分子生物学・細菌学