Team:Paris/Transduction overview

From 2009.igem.org

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(Introduction)
(Introduction)
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With the Jun/Fos dimere:
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'''''With the Jun/Fos dimere:'''''
Jun and Fos are able to form an heterodimer which has a high stability and Jun can dimerize with another Jun (thanks to their leucine zipper motif).
Jun and Fos are able to form an heterodimer which has a high stability and Jun can dimerize with another Jun (thanks to their leucine zipper motif).
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After mutations into the leucine zipper motif of Jun (that allow the Jun/Fos dimerization but avoid the Jun/Jun homodimer formation), we wanted to fuse it with AIDA (an ABC transporter) to send them to the extern membrane.
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After mutations into the leucine zipper motif of Jun (that allow the Jun/Fos dimerization but avoid the Jun/Jun homodimer formation), we wanted to fuse it to AIDA (an ABC transporter) to send them to the extern membrane of bacteria.
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With G3P :
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'''''With G3P :'''''
The viral protein known as G3P is naturally exposed at the surface of the filamentous bacteriophage which enable it to get in the bacteria. The M13 phage has a high affinity for E.coli, and if we could place its G3p on the surface of the vesicles it could activate the fusion with the Outer membrane of the targeted bacteria.
The viral protein known as G3P is naturally exposed at the surface of the filamentous bacteriophage which enable it to get in the bacteria. The M13 phage has a high affinity for E.coli, and if we could place its G3p on the surface of the vesicles it could activate the fusion with the Outer membrane of the targeted bacteria.
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'''''With the SNARE system:'''''
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With the SNARE system:
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Revision as of 18:56, 19 October 2009

iGEM > Paris > Receiving the message > Membrane fusion

Introduction

This part of the project was focus on a precise point

We have planned to explore three different method :


With the Jun/Fos dimere: Jun and Fos are able to form an heterodimer which has a high stability and Jun can dimerize with another Jun (thanks to their leucine zipper motif). After mutations into the leucine zipper motif of Jun (that allow the Jun/Fos dimerization but avoid the Jun/Jun homodimer formation), we wanted to fuse it to AIDA (an ABC transporter) to send them to the extern membrane of bacteria.


With G3P : The viral protein known as G3P is naturally exposed at the surface of the filamentous bacteriophage which enable it to get in the bacteria. The M13 phage has a high affinity for E.coli, and if we could place its G3p on the surface of the vesicles it could activate the fusion with the Outer membrane of the targeted bacteria.


In order to target the G3P at the surface of of the vesicles, we fuse it to the OmpA- Linker protein (created by the Warsaw team)


With the SNARE system: