Overview

Virus capsids are expected to afford us new aspects for development as an amenable platform for diverse applications in biotechnology, electronics, and medicine, because the proteins allow for easy preparation, self-assembling capability, water solubility, low cytotoxicity and biocompatibility. In particular, much attention has been paid to capsids from virus infecting hyperthermophilic archaea due to their extremely high stability and morphological diversity. Therefore, capsids from hyperthermophilic viruses can be expected to offer ideal properties for application to nanomaterials.

Here, we focused on the capsid of Aeropyrum pernix bacilliform virus 1 (APBV1). The host cell of APBV1, A. pernix, can grow above 90°C under aerobic conditions. Due to its hyperthermostable nature, APBV1 forms robust virion. APBV1 capsid is therefore expected to be a useful building block for the creation of new nanomaterials. The recombinant protein expression system of ORF6-81 composed of the main capsid protein of APBV1 was constructed, allowing the synthesis of nanoparticles from the recombinant capsid protein. In addition, we tried to construct a novel functional nanoparticle by introducing an amino group on the surface of recombinant ORF6-81 nanoparticles via site-directed mutagenesis.

Speaker

Takenori Satomura, Professor, University of Fukui

Dr Satomura is a professor in Division of Engineering, Faculty of Engineering, University of Fukui. He has a PhD in Engineering from University of Tokushima, Japan. His main research interest lies in the relationship between structure and function of proteins derived from extremophiles. In addition, he focuses on the diversity of the shapes of archaea viruses.

Time

14:00–15:00 MYT. Seminar Room 6215 (Building 6, Level 2, Room 15).