Team:Linkoping Sweden

From 2013.igem.org

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Our Project idea is to first grow E.Coli that has been genetically modified to produce an antibody with the enzyme luciferase attached to its constant part. At first the antibody will be constructed to adhere to an egg antigen, but our long time goal is to be able to switch to whichever antigen desired. Luciferase is an enzyme that cleaves luciferin in the presence of ATP, giving rise to a long lasting green light by the principle of luminescence. Luminescence is superior to fluorescence due to, e.g. lack of fading.  
Our Project idea is to first grow E.Coli that has been genetically modified to produce an antibody with the enzyme luciferase attached to its constant part. At first the antibody will be constructed to adhere to an egg antigen, but our long time goal is to be able to switch to whichever antigen desired. Luciferase is an enzyme that cleaves luciferin in the presence of ATP, giving rise to a long lasting green light by the principle of luminescence. Luminescence is superior to fluorescence due to, e.g. lack of fading.  
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To distinguish between the antibodies that has adhered to the antigen and the ones that has not, we use RFP attached to a fake, but identical, antigen. The extra antibodies adhere to the fake antigen and their light gets canceled out. The cancellation is due to the properties of RFP, which acts as a quencher on the light emitted from the luciferase/luciferin complex. The fake antigen with RFP attached will also be grown inside a genetically modified E.Coli.  
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To distinguish between the antibodies that has adhered to the antigen and the ones that has not, we use RFP attached to a fake, but identical, antigen. The extra antibodies adhere to the fake antigen and the luminescence from luciferase gets transferred to RFP through a process called FRET. This results in two emitted lights green and red, by this we can distinguish between a fake antigen and a true antigen. The fake antigen with RFP attached will also be grown inside a genetically modified E.Coli.  
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By first adding the antibodies to a solution with known concentrations of egg antigen and then adding the fake antigen complex, to cancel out the unbounded antibodies, the intensity of light emitted should be proportional to the concentration of antigen in the solution. This way we can determine how much antigen are present, and if there are any at all.
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By first adding the antibodies to a solution with known concentrations of egg antigen and then adding the fake antigen complex, to bind the unbounded antibodies, the intensity of light emitted should be proportional to the concentration of antigen in the solution. This way we can determine how much antigen are present in real life sample, and if there are any at all.
For a more in depth explanation of our project, head on over to the [[Team:Linkoping_Sweden/Project|project]] part of this website.
For a more in depth explanation of our project, head on over to the [[Team:Linkoping_Sweden/Project|project]] part of this website.

Revision as of 14:51, 8 August 2013

About Us

Our team consists of twelve students from Linköping University who are interested in biotechnology. All of us have been studying engineering in technincal or chemical biology for at least three years. In our group we also have two seniors, a professor who is head of the division of information coding and a med. doctor in biomedicine. Our goal with the project is to reach the finals in the iGEM competition and to be able to take our team and project to Boston.

You can read more about the members of LiU iGEM on our team page.

Our idea

Our Project idea is to first grow E.Coli that has been genetically modified to produce an antibody with the enzyme luciferase attached to its constant part. At first the antibody will be constructed to adhere to an egg antigen, but our long time goal is to be able to switch to whichever antigen desired. Luciferase is an enzyme that cleaves luciferin in the presence of ATP, giving rise to a long lasting green light by the principle of luminescence. Luminescence is superior to fluorescence due to, e.g. lack of fading.

To distinguish between the antibodies that has adhered to the antigen and the ones that has not, we use RFP attached to a fake, but identical, antigen. The extra antibodies adhere to the fake antigen and the luminescence from luciferase gets transferred to RFP through a process called FRET. This results in two emitted lights green and red, by this we can distinguish between a fake antigen and a true antigen. The fake antigen with RFP attached will also be grown inside a genetically modified E.Coli.

By first adding the antibodies to a solution with known concentrations of egg antigen and then adding the fake antigen complex, to bind the unbounded antibodies, the intensity of light emitted should be proportional to the concentration of antigen in the solution. This way we can determine how much antigen are present in real life sample, and if there are any at all.

For a more in depth explanation of our project, head on over to the project part of this website.

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