Team:Toulouse/Project/binding

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         <p class="texte"> In order to be more effective in the fight against the pythopathogen, our optimized bacterium has to be anchored to the fungus. This module matches with the <B> binding ability </B> of SubtiTree. Thus, we designed a chimeric protein (<a href="http://parts.igem.org/Part:BBa_K1364005"target="_blank">BBa_K1364005</a>) to make <B> a bridge between the bacterial peptidoglycan and the fungal chitin </B>, which is the main component of the pathogen’s cell wall. According to the work of the Imperial College 2010 iGEM team, we used the CWB domain of the LytC protein (coding for a N-acetylmuramoyl-Lalanine amidase) to bind our chimeric protein to <I> Bacillus subtilis </I> cell wall. On the other side of our protein, we added the domain 4 of  GbpA from <I> Vibrio Cholerae </I>, which is known to recognize N-AcetylGlucosamine oligosaccharides called chitin.
         <p class="texte"> In order to be more effective in the fight against the pythopathogen, our optimized bacterium has to be anchored to the fungus. This module matches with the <B> binding ability </B> of SubtiTree. Thus, we designed a chimeric protein (<a href="http://parts.igem.org/Part:BBa_K1364005"target="_blank">BBa_K1364005</a>) to make <B> a bridge between the bacterial peptidoglycan and the fungal chitin </B>, which is the main component of the pathogen’s cell wall. According to the work of the Imperial College 2010 iGEM team, we used the CWB domain of the LytC protein (coding for a N-acetylmuramoyl-Lalanine amidase) to bind our chimeric protein to <I> Bacillus subtilis </I> cell wall. On the other side of our protein, we added the domain 4 of  GbpA from <I> Vibrio Cholerae </I>, which is known to recognize N-AcetylGlucosamine oligosaccharides called chitin.

Revision as of 16:03, 15 October 2014