N-glycosylation and homodimeric folding significantly enhance the immunoreactivity of Mycobacterium tuberculosis virulence factor CFP32 when produced in the yeast Pichia pastoris.

We previously reported that immunoreactivity of recombinant CFP32 (Rv0577), a virulence factor of Mycobacterium tuberculosis, was higher when produced in transformed Pichia pastoris as compared to transformed E. coli. In this study, we show that this difference is partly due to the N-glycosylation of the recombinant CFP32 (rCFP32) by the yeast Pichia pastoris.