Isolation and purification of recombinant outer surface protein C (rOspC) of Borrelia burgdorferi sensu lato.
The aim of this work was isolation and purification of the major immunodominant protein, Outer surface protein C (OspC) of three members of the species group Borrelia burgdorferi, the causative agent of Lyme disease. Our aim was to obtain this protein in a quantity and purity sufficient for immunization of experimental animals. For optimalization of protein purification's yield we used immobilized metal ion affinity chromatography (IMAC) under different conditions. The greatest efficiency was achieved by using of HiTrap Chelating Column under native conditions.
Krupka
Michal
M
Department of Immunology, Palacký University, Olomouc, Czech Republic. majkl.krupka@centrum.cz
Bĕláková
Jana
J
Sebestová
Martina
M
Tuhácková
Jana
J
Raska
Milan
M
Vrzal
Vladimír
V
Weigl
Evzen
E
D000942:Antigens, Bacterial / Q000096:biosynthesis* / Q000302:isolation & purification; D001425:Bacterial Outer Membrane Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D004926:Escherichia coli; D005822:Genetic Vectors; D022123:Lyme Disease Vaccines / Q000096:biosynthesis* / Q000302:isolation & purification; D019444:Vaccines, DNA / Q000096:biosynthesis* / Q000302:isolation & purification
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D022123:Lyme Disease Vaccines; C079616:OspC protein; D019444:Vaccines, DNA