Production of a recombinant bacterial lipoprotein in higher plant chloroplasts

Little is known about the potential of plastids to accomplish post-translational modifications of foreign proteins. In the present study we generated transplastomic tobacco plants that accumulate the outer surface lipoprotein A (OspA)-the basic constituent of the first generation monovalent human va...

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Main Authors: Glenz, Karin (Author) , Bouchon, Bernadette (Author) , Stehle, Thomas (Author) , Wallich, Reinhard (Author) , Simon, Markus M. (Author) , Warzecha, Heribert (Author)
Format: Article (Journal)
Language:English
Published: 2006
In: Nature biotechnology
Year: 2005, Volume: 24, Issue: 1, Pages: 76-77
ISSN:1546-1696
DOI:10.1038/nbt1170
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nbt1170
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nbt1170
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Author Notes:Karin Glenz, Bernadette Bouchon, Thomas Stehle, Reinhard Wallich, Markus M. Simon & Heribert Warzecha
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Summary:Little is known about the potential of plastids to accomplish post-translational modifications of foreign proteins. In the present study we generated transplastomic tobacco plants that accumulate the outer surface lipoprotein A (OspA)-the basic constituent of the first generation monovalent human vaccine against Lyme disease. The recombinant OspA exhibits a lipid modification typical for bacteria and induced protective antibodies in mice, demonstrating that functionally active bacterial lipoproteins can be processed in plants.
Item Description:Published online: 4 December 2005
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Physical Description:Online Resource
ISSN:1546-1696
DOI:10.1038/nbt1170