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 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.
Glenz
Karin
K
Department of Pharmaceutical Biology, Julius-von-Sachs-Institut für Biowissenschaften, Julius-Maximilians Universität Wuerzburg, Julius-von-Sachs-Platz 2, 97082 Wuerzburg, Germany.
Bouchon
Bernadette
B
Stehle
Thomas
T
Wallich
Reinhard
R
Simon
Markus M
MM
Warzecha
Heribert
H
D000954:Antigens, Surface / Q000235:genetics / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D001428:Bacterial Vaccines; D001483:Base Sequence; D002736:Chloroplasts / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D008074:Lipoproteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D030821:Plants, Genetically Modified / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000378:metabolism; D014026:Nicotiana / Q000235:genetics / Q000378:metabolism*; D014162:Transfection / Q000379:methods*
D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; D008074:Lipoproteins; C072045:OspA protein; D011994:Recombinant Proteins