An improved method for the purification and refolding of r56-kDa proteins from Gilliam and Kato strains of Orientia tsutsugamushi.
The immunodominant 56kDa outer membrane antigens from Orientia tsutsugamushi Kato and Gilliam strains were expressed as inclusion bodies (IBs) in E. coli. The IBs were purified and properly refolded with modifications of a previous procedure used for the production of Karp strain r56 antigen. A mixture of these three r56 proteins exhibited both high sensitivity and specificity for detection of O. tsutsugamushi antibodies by ELISA.
Yang
Qing
Q
Rickettsial Diseases Program, Infectious Diseases Directorate, Naval Medical Research Center, Silver Spring, Maryland 20910, USA.
Ching
Wei-Mei
WM
Jiang
Ju
J
Lousteau
Leslie
L
Richards
Allen L
AL
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D001483:Base Sequence; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D008970:Molecular Weight; D012285:Orientia tsutsugamushi / Q000145:classification / Q000235:genetics / Q000302:isolation & purification*; D011489:Protein Denaturation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D001426:Bacterial Proteins; D017931:DNA Primers; D011994:Recombinant Proteins