Team:Warsaw

From 2008.igem.org

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<p>Our team consists of 9 students of Faculty of Biology, University of
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<p>We have developed a system allowing to search for antibodies with new specificities or screen protein libraries in order to generate interactors for a given bait. Our system changes a protein sequence to maximize its interaction with a given partner. Proteins with modified sequences are then directed to the bacterial outer membrane, where the best interactors are selected. Protein presented on the cell surface is fused with part of &#946;-lactamase protein, while its bait is fused with the complementing part of the enzyme and added to medium. The stronger the interaction between proteins of interest, the more efficient the binding of the two halves of &#946;-lactamase, leading to resistance to ampicillin and survival. Cells expressing less interacting variants die as they don't achieve sufficient complementation of the reporter enzyme. This allows us to select strains producing interactors for any given bait. </p>
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Warsaw. This is the first time a group from Poland participates in the
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iGEM competition. Our plans were really amazing: we wanted to create
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system of biological machines which would allow to investigate protein
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interactions and simultaneously change sequence of one of them in
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order to achieve the strongest possible interaction. To make it work
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we planned to express the tested protein in a bacterial strain in
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which it would be mutated. Selection would occur outside outer
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bacterial membrane, where the protein would be attached. We planned
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that such selection system would allow us to search for antibodies
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with new specificities or screen protein libraries. </p>
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Revision as of 19:30, 27 October 2008

Gallery Bricks Notebook Team Project Home

We have developed a system allowing to search for antibodies with new specificities or screen protein libraries in order to generate interactors for a given bait. Our system changes a protein sequence to maximize its interaction with a given partner. Proteins with modified sequences are then directed to the bacterial outer membrane, where the best interactors are selected. Protein presented on the cell surface is fused with part of β-lactamase protein, while its bait is fused with the complementing part of the enzyme and added to medium. The stronger the interaction between proteins of interest, the more efficient the binding of the two halves of β-lactamase, leading to resistance to ampicillin and survival. Cells expressing less interacting variants die as they don't achieve sufficient complementation of the reporter enzyme. This allows us to select strains producing interactors for any given bait.

Institutions whom we would like to thank for financial and technical support:

University of Warsaw

Faculty of Biology, University of Warsaw

The Universitatis Varsoviensis Fund

Foundation for Polish Science

Warsaw University Foundation

Department of Molecular Biology, IIMCB

Departments belonging to the Faculty of Biology, University of Warsaw, who kindly provided access to laboratory space and equipment:

Department of Plant Molecular Biology

Department of Virology

Department of Bacterial Genetics

Institute of Genetics and Biotechnology