Team:Michigan/Future/

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<h1><font size="10"> Scientific Outreach</font></h1></p><font size="3"><font color="#191970"> University of Michigan iGEM Team </font></font color></p>
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<h1><font size="10"> Future Directions</font></h1></p><font size="3"><font color="#191970"> University of Michigan iGEM Team </font></font color></p>
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<p style="position:absolute;top:100px;left:0px"> This year our team reached out to the community by helping to educate young girls on the tools used in synthetic biology. Not only does it help future scientists get involved at an early age, but it also helps promote gender diversity. We feel it is important to help educate the next generation of women in science by giving them the opportunity to work with DNA and the principals of synthetic biologyat a young age. So we decided to collaborate with the GISE, Girls In Science and Engineering, camp to teach them about synthetic biology. </p>
 
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<p style="position:absolute;top:100px;left:0px"> GISE is a summer camped aimed at getting middle school aged girls involved with science. Our time with the middle schoolers and high schoolers not only allowed the girls to get a look into what studying science in college entails, it also gave our team members experience mentoring the girls, a win-win in the end. We provided the girls with the materials to extract DNA from strawberries and bananas, comparing the yield of DNA and making hypotheses as to what the cause of the yield difference was.  The girls were also able to make neclaces out of their own DNA, following a cheek swab and DNA isolation. </p></br>
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<p>To improve our project we will compare our antibody scFv purification system with industrially used purification systems. OsmY has shown to be secreted in higher amounts than the industrially used pelB tag (Qian et al., 2008). In hopes that our purification system allows more scFv production we will compare the amount of scFv produced per liter of media using our construct to an industrially used construct.</p></br>
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<p>One must also consider the limitation of our system. The scFv we used has already been secreted in E.coli and shown to function (Meyer, et al., 2012). It would be interesting for us to test a variety of antibodies to find which type of antibodies are easily excreted in E.coli with our construct. Perhaps a wider variety of antibodies can be secreted using our system than the common industrial system.</p></br>
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<p> We received oustanding feedback from the campers, many of whom were repeat campers from previous years. Some of the girls from the earliest years of the camp are prospective team members for next year's team and have attended our practice presentations for the conference in Boston. We feel that this in itself is a great sign that our work with the girls is spreading the word on synthetic biology and building interest in the team. </p></div>
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<p>Our system isn’t constrained to antibodies; we could also use it for other disulfide bonded protein such as various cofactors, insulin, etc.
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Finally, in search of mimicking antibody’s agglutination properties it would be interesting to purify two antibody scFv linked together by a single peptide chain; enabling one construct to bind two antigens.</p></br>
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<p> References:</br></br>
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Meyer, T. et al. Identification of immunogenic proteins and generation of antibodies against Salmonella Typhimurium using phage display. BMC Biotechnology 12, 29 (2012).
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Qian, Z.-G. G., Xia, X., Choi, J. H. & my Lee, S. Y. Proteome-based identification of fusion partner for high-level extracellular production of recombinant proteins in Escherichia coli. Biotechnology and bioengineering 101, 587–601 (2008). </p>
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Latest revision as of 03:37, 18 October 2014

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Future Directions

University of Michigan iGEM Team

To improve our project we will compare our antibody scFv purification system with industrially used purification systems. OsmY has shown to be secreted in higher amounts than the industrially used pelB tag (Qian et al., 2008). In hopes that our purification system allows more scFv production we will compare the amount of scFv produced per liter of media using our construct to an industrially used construct.


One must also consider the limitation of our system. The scFv we used has already been secreted in E.coli and shown to function (Meyer, et al., 2012). It would be interesting for us to test a variety of antibodies to find which type of antibodies are easily excreted in E.coli with our construct. Perhaps a wider variety of antibodies can be secreted using our system than the common industrial system.


Our system isn’t constrained to antibodies; we could also use it for other disulfide bonded protein such as various cofactors, insulin, etc. Finally, in search of mimicking antibody’s agglutination properties it would be interesting to purify two antibody scFv linked together by a single peptide chain; enabling one construct to bind two antigens.


References:

Meyer, T. et al. Identification of immunogenic proteins and generation of antibodies against Salmonella Typhimurium using phage display. BMC Biotechnology 12, 29 (2012).

Qian, Z.-G. G., Xia, X., Choi, J. H. & my Lee, S. Y. Proteome-based identification of fusion partner for high-level extracellular production of recombinant proteins in Escherichia coli. Biotechnology and bioengineering 101, 587–601 (2008).

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