Team:Linkoping Sweden

Linkoping Sweden -



Overexpression of chaperones in Escherichia coli!

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Problematic protein folding is a cause of monetary loss for protein producing industries [1], and also the cause of neurodegenerative diseases such as Alzheimer’s and Parkinson's [2]. Molecular chaperones are important factors in protein folding. Chaperones are proteins that can fold other unfolded proteins and refold misfolded ones. More correctly folded proteins equals higher average protein production output.
Why did LiU iGEM 2018 choose the project?
The team was inspired by those suffering of Alzheimer's and many team members know someone personally who is afflicted with the disease. LiU iGEM 2018 also wanted to keep working on last year's project, in which they wanted to understand the connection between Alzheimer's and chaperones [3]. Another source of inspiration is that Linköping university has conducted a lot of research concerning chaperones which made it interesting to contribute [4].

Why is this project needed?
Research on chaperones is important because dementia is on the rise. Between 2010 and 2015 the cost of dementia related diseases increased by 35 %, up to a worldwide total of $818 billion [5]. During 2018 this number is expected to be around $1 trillion [5]. These costs arise from the increasing amount of people falling ill with dementia related diseases but also an increase in treatment [5]. Our team hopes to create easier access to the many proteins involved in these dementia related diseases, thus increasing the knowledge about them. The aim with our research is to optimize protein production by increasing the ratio of correctly folded proteins in E. coli. This will help researchers working with proteins that are prone to misfold or aggregate. By increasing successful protein folding, production will be easier and cheaper.
How do we plan on solving the problem?
We will attempt to create a bacterial strain that is optimized for production of hard-to-fold proteins. A plasmid containing genes for the molecular chaperones will be inserted into the genome of the E.coli strain BL21 DE3 gold. The chaperones that will be studied are the bacterial GroEL/GroES, DnaJ/DnaK, GrpE and Trigger factor. These systems will be regulated by different promotors which lets us control the expression with precision. We will use a mathematical model to find the concentrations where the production of correctly folded proteins is at a maximum.
The industry will be able to use this bacterial strain to increase the yield of for example: Amyloid-β and Tau, proteins which are prone to aggregation and play a major role in Alzheimer’s disease [2]. The bacteria could also illustrate the role of chaperones in neurodegenerative diseases. Both of the mentioned examples could be used in research. Using the strain to increase the yield of proteins that are not prone to aggregation will be tested in a later stage.
[1] Singh A, Upadhyay V, Upadhyay AK, Singh SM, and Panda AK. Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process. Microbial Cell Factories. 2015;14:41.
[2] Martone R, Piotrowski N [Internet]. Alzheimer's disease. Magill’s Medical Guide. [cited 2018 June 12]. Available from: Research Starters.
[3] LiU iGEM [Internet]. Linköping: iGEM LiU. Forgetful folding; [cited 2018 June 12]. Available from:
[4] Hammarström Lab [Internet]. Linköping: Hammarström Lab. [cited 2018 June 12]. Available from:
[5] Wimo A, Guerchet M, Ali GC, Wu YT, Prina AA, Winblad B, et al. The worldwide costs of dementia 2015 and comparisons with 2010. Elsevier. 2017;13:1-7.

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