The use of a 'universal' yeast expression vector to produce an antigenic protein of Mycobacterium leprae.
This report describes the use of a recombinant yeast expression vector to synthesize and secrete the Mycobacterium leprae 18 kDa antigenic protein. The protein is secreted with a short hydrophilic 'flag' octapeptide fused to its amino-terminus. The fusion protein can be purified directly from yeast culture supernatant through an anti-flag antibody affinity column and the flag octapeptide removed using enterokinase. The method provides a simple and rapid means of obtaining recombinant 18 kDa antigen in quantities suitable for immunological studies.
Booth
R J
RJ
Department of Immunobiology, University of Auckland Medical School, New Zealand.
Grandison
P M
PM
Prestidge
R L
RL
Watson
J D
JD
D000942:Antigens, Bacterial / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics / Q000276:immunology*; D004926:Escherichia coli / Q000235:genetics; D005822:Genetic Vectors; D009166:Mycobacterium leprae / Q000235:genetics / Q000276:immunology*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000235:genetics
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins