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Team:Brown
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<p>Our team submits a library of well characterized and standardized promoters and sensors for eukaryotic cells. We will also contribute the first eucaryotic standart chassis for iGem featuring standardized genome integration sites.</p> | <p>Our team submits a library of well characterized and standardized promoters and sensors for eukaryotic cells. We will also contribute the first eucaryotic standart chassis for iGem featuring standardized genome integration sites.</p> | ||
Revision as of 16:01, 19 October 2009
Welcome to the Brown iGEM wiki!
Brown iGEM is a team of nine undergraduate students from diverse backgrounds in science and engineering. We are mentored by Brown graduate students, postdocs, and faculty from across the university. With support from Brown Undergraduate Teaching and Research Awards and Brown Multidisciplinary Labs, we have been conducting unique research and experiments over the past 4 months in preparation for iGEM jamboree at MIT in November 2009. The 2009 Brown iGEM team aims to treat allergic rhinitis by taking an innovative synthetic biological approach to create self-regulating drug factory in the nose.
The Project
Every year, over fifty million people in the US suffer from allergic rhinitis, the most common type of allergy. Allergens, such as pollen, dust, and dander result in nasal congestion, itching, burning, sneezing, and overall discomfort. Current treatments include over-the-counter antihistamines, however, side effects of these drugs include drowsiness, restlessness, and poor concentration. For patients suffering from chronic allergies and inflammation, there is a great need for an alternative strategy for combating allergic symptoms without causing significant side effects.
The 2009 Brown University iGEM team worked to treat allergic rhinitis by engineering Staphylococcus epidermidis, a microbe endogenous to the human nasal flora, to secrete a recombinant histamine-binding protein in response to the elevated histamine concentrations of an allergic response. The engineered strain of S. epidermidis will function as a self-regulating drug factory in the nose, providing relief, without any negative side effects.
System Components
| rEV131 (HBP2) is a high affinity histamine binding protein secreted by the tick Rhipicephalus appendiculatus. rEV131 has the ability to outcompete host histamine receptors for the ligand, effectively combating the allergic response. | 
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| Chimeric protein Taz1 contains an aspartate-binding periplasmic domain (Tar) and a cytoplasmic kinase domain (EnvZ). This histamine sensor will respond to changing levels of histamine, so that histamine binding protein production will be triggered only as histamine levels dramatically increase in the presence of an allergen. |
Parts
Our team submits a library of well characterized and standardized promoters and sensors for eukaryotic cells. We will also contribute the first eucaryotic standart chassis for iGem featuring standardized genome integration sites.
