Team:LMU-Munich/Spore Coat Proteins/mainresult
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===GFP as a Proof of Principle=== | ===GFP as a Proof of Principle=== | ||
- | <p align="justify">We designed the first '''Sporo'''bead to express GFP to evaluate our system and compare different [[Team:LMU-Munich/Spore_Coat_Proteins/cloning|constructs]]. We had to ensure that production is both high and takes place on the edge of spores. The following graph (Fig. 6) shows the microscopy pictures and analysis of the strongest of the five constructs integrated into wildtype W168 (B53) and the deletion strain B 49 (B70).</p> | + | <p align="justify">We designed the first '''Sporo'''bead to express GFP to evaluate our system and compare different [[Team:LMU-Munich/Spore_Coat_Proteins/cloning|constructs]]. |
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+ | This two short time lapse videos shows the formation of a spore and lollowing lysis of the mother cell of one of our constructs. | ||
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+ | We had to ensure that production is both high and takes place on the edge of spores. The following graph (Fig. 6) shows the microscopy pictures and analysis of the strongest of the five constructs integrated into wildtype W168 (B53) and the deletion strain B 49 (B70).</p> | ||
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Revision as of 15:20, 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 Sporobead to express GFP to evaluate our system and compare different constructs. This two short time lapse videos shows the formation of a spore and lollowing lysis of the mother cell of one of our constructs.
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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 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.