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Team:LMU-Munich/Spore Coat Proteins/mainresult
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<p align="justify">To ensure that our '''Sporo'''beads show fluorescence on their edge and higher than in wildtype spores, we analysed the microscopy pictures. The following graph (Fig. 6) shows these microscopy pictures and analysis of the strongest of the five constructs integrated into wildtype strain (B53) and the deletion strain (B70).</p> | <p align="justify">To ensure that our '''Sporo'''beads show fluorescence on their edge and higher than in wildtype spores, we analysed the microscopy pictures. The following graph (Fig. 6) shows these microscopy pictures and analysis of the strongest of the five constructs integrated into wildtype strain (B53) and the deletion strain (B70).</p> | ||
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Revision as of 15:47, 26 October 2012
The LMU-Munich team is exuberantly happy about the great success at the World Championship Jamboree in Boston. Our project Beadzillus finished 4th and won the prize for the "Best Wiki" (with Slovenia) and "Best New Application Project".
[ more news ]
GFP as a Proof of Principle
We designed the first GFP-Sporobead to evaluate our system and compare different constructs. This two short time lapse videos show the formation of a spore and following lysis of the mother cell of one of our constructs.
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To ensure that our Sporobeads show fluorescence on their edge and higher than in wildtype spores, we analysed the microscopy pictures. The following graph (Fig. 6) shows these microscopy pictures and analysis of the strongest of the five constructs integrated into wildtype strain (B53) and the deletion strain (B70).
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As shown in Fig. 6, the wild type spore has hardly any fluorescence, whereas both Sporobeads with the integrated construct pSBBs1C-PcotYZ-cotZ-2aa-gfp-terminator give a distinct fluorescence signal around the edge of the spore. Furthermore, it demonstrates that strain B 70 has the highest fluorescence intensity. For more detailed information have a look at our Data page
In summary we successfully developed functional Sporobeads that are capable of displaying any protein of choice on the surface of modified B. subtilis endospores.
