Press releases
Kinesin, a key biomolecular motor protein, can be successfully synthesized by wheat germ from CellFree Sciences
A group led by Assistant Professor Daisuke Inoue (Kyushu University) has successfully synthesised the biomolecular motor protein, kinesin, using wheat germ as a cell-free protein synthesis system and reported its activity. This novel finding is important because kinesin was not only synthesized in abundant amounts, but it was also shown to have a higher motor activity compared to that synthesized by E. coli. More importantly, not only WT kinesin was synthesized by wheat germ, but also several mutated and affinity-tagged kinesins were successfully synthesized as well. This is especially important because it shows that the wheat germ provided by CellFree Sciences is a reliable and fast method for producing wild type, mutated, and tagged proteins in a high-quality manner that will expedite further research.
Title: In vitro Synthesis and Design of Kinesin Biomolecular Motors by Cell-Free Protein Synthesis
Authors: Assistant Professor Daisuke Inoue (Faculty of Design, Kyushu University)
Keisuke Ohashi (Graduate School of Global Food Resources, Hokkaido University)
Associate Professor Taichi E. Takasuka (Research Faculty of Agriculture, Hokkaido University)
Professor Akira Kakugo (Graduate School of Science, Kyoto University)
Journal: ACS Synthetic Biology (part of the American Chemical Society Group)
URL: https://pubs.acs.org/doi/abs/10.1021/acssynbio.3c00235: DOI: 10.1021/acssynbio.3c00235
Image Credit: Daisuke Inoue, Keisuke Ohashi, Taichi E. Takasuka and Akira Kakugo.
The movies introducing wheat cell-free protein synthesis technology and its applications is available on the Protein Island Matsuyama (PIM) website.
The movies introducing the wheat cell-free protein synthesis technology and its applications were created and released as one of the programs of Protein Island Matsuyama (PIM) .
"CF-PPiD", a new protein-protein interaction (PPI) screening technology using human protein bead arrays, was reported in an academic paper.
A new protein-protein interaction (PPI) screening technology "CF-PPiD" ,which applies "proximity-dependent biotin labeling technology" to the "20K Human Protein Bead Array" containing 20,000 human-derived proteins synthesized by the wheat cell-free synthesis system, has been reported as following academic paper.
CF-PPiD technology based on cell-free protein array and proximity biotinylation enzyme for in vitro direct interactome analysis Scientific Reports volume 12, Article number: 10592 (2022)
https://www.nature.com/articles/s41598-022-14872-w
Abstract
Protein–protein interaction (PPI) analysis is a key process to understand protein functions. Recently, we constructed a human protein array (20 K human protein beads array) consisting of 19,712 recombinant human proteins produced by a wheat cell-free protein production system. Here, we developed a cell-free protein array technology for proximity biotinylation-based PPI identification (CF-PPiD). The proximity biotinylation enzyme AirID-fused TP53 and -IκBα proteins each biotinylated specific interacting proteins on a 1536-well magnetic plate. In addition, AirID-fused cereblon was shown to have drug-inducible PPIs using CF-PPiD. Using the human protein beads array with AirID-IκBα, 132 proteins were biotinylated, and then selected clones showed these biological interactions in cells. Although ZBTB9 was not immunoprecipitated, it was highly biotinylated by AirID-IκBα, suggesting that this system detected weak interactions. These results indicated that CF-PPiD is useful for the biochemical identification of directly interacting proteins.
※ Now, we, Celfree Science Co. Ltd, are expanding our molecular interaction analysis service using "CF-PPiD" and looking forward to your use of our service.
Our research and development activities were introduced in the weekly Ehime Economic Report.
The weekly Ehime Economic Report (November 8, 2021) No. 2273 introduced our efforts to develop "Targeted Proteolytic Drug (TPD)" in cooperation with Ehime University.
The movies introducing wheat cell-free protein synthesis technology and its applications is now available on the Protein Island Matsuyama (PIM) website.
The movies introducing the wheat cell-free protein synthesis technology and its applications was created and released as one of the programs of Protein Island Matsuyama (PIM) 2020,
CellFree Sciences Co., Ltd. received support from Ehime Prefecture under the "Ehime Prefecture New Growth Manufacturing Company Comprehensive Support Program in FY2021".
We are grateful, that Ehime Prefecture selected an application by CellFree Sciences under their "Ehime Prefecture New Growth Manufacturing Company Comprehensive Support Program in FY2021".
Having access to a unique set of about 23,000 human full-length proteins, CellFree Sciences will apply their own technologies including a protein bead array platform to search for new drug targets and therapeutic concepts.
While about 10 to 15% of the human proteins could play a role in disease, presently only about 2% of the human proteins can be directly targeted by a drug. Hence, there is a clear need to expand the number of druggable proteins to develop new therapeutic concepts and to cover a wider range of disease. In this project, we will apply new concepts to target drug targets for proteolytic degradation utilizing E3 ligases. Having extensive knowledge on E3 ligases, it is hoped that utilizing E3 ligases will offer new leads allowing for targeted proteolysis of selected targets while having less side effects than other drug candidates.
Project period: July 5, 2021-February 28, 2022.
Dr. Yaeta Endo, Special University Professor Emeritus, received the Ehime News Paper's Award
Dr. Yaeta Endo, who is the Special University Professor Emeritus, received the Ehime News Paper’s Award for developing wheat germ cell free protein expression system.
The development serological markers for detecting recent Plasmodium vivax infection has been successful
The international research group comprising of Proteo-Science Center, Ehime University’s Dr. Eizo Takashima, Dr. Masayuki Morita, and Dr. Takafumi Tsuboi along with CellFree Sciences Co., Ltd.’s Dr. Matthias Harbers succeeded in developing a serological diagnostic marker that can identify those with dormant liver stage infections, which are the causes of Plasmodium vivax recurrences.
This result has been achieved by an international joint research project with the main members including Proteo-Science Center, Ehime University, CellFree Sciences Co., Ltd., The Walter and Eliza Hall Institute of Medical Research (WEHI), Pasteur Institute, and Foundation for Innovative New Diagnostics (FIND).
Further, this project was started with assistance from the Global Health Innovative Technology Fund (GHIT Fund) between October 2015 and March 2017.
This research result allows the diagnosis of Plasmodium vivax’s dormant liver stage parasites which has been a difficult challenge in eliminating malaria, for the first time in the world. It can be seen as an important result to safely and effectively promote the treatment.
The paper regarding this research result has been published on the May 12th (Tues.) 2020 issue of the Nature Medicine.
Development and validation of serological markers for detecting recent Plasmodium vivax infection
We in collaboration with Ehime University have developed a new technology to conduct a genome wide evaluation of the specificity of antibodies that can bind to human proteins.
The groups from CellFree Sciences Co., Ltd. (Ryo Morishita, R&D manager) and Proteo-Science Center, Ehime University (Professor Tatsuya Sawasaki) have successfully developed a new technology that identifies proteins for binding to target antibodies. Using about 20,000 human proteins this technology is best suited for veriflying the specificity of antibodies against human proteins.
The new technology utilizes a protein bead array technology developed by CellFree Sciences Co., Ltd. named “CF-PA2Vtech”. The potential of the new method was demonstrated by verifying the specific binding of a commercial anti-PD-1 antibody, where the data demonstrate its binding to several proteins having related linear epitopes.
The results from the research were published by Morishita et al. in the December 18, 2019 issue of Scientific Reports:
CF-PA2Vtech: a cell-free human protein array technology for antibody validation against human proteins