Overproduction and Characterization of Recombinant Soluble <i>Trypanosoma brucei</i> Phospholipase A₂.

ABSTRACT: Trypanosoma brucei phospholipase A₂ (TbPLA₂) is a validated drug target but the difficulty in expressing its soluble recombinant protein has limited its exploitation for drug and vaccine development for African and American trypanosomiases. We utilized recombinant deoxyribonucleic acid (DNA) technology approaches to express soluble TbPLA₂ in Escherichia coli and Pichia pastoris and biochemically characterize the purified enzyme. Full-length TbPLA₂ was insoluble and deposited as inclusion bodies when expressed in E. coli. However, soluble and active forms were obtained when both the full-length and truncated TbPLA₂ were expressed in fusion with N-terminal FLAG tag and C-terminal eGFP in P. pastoris, an

SUBMITTER: Adepoju OA 

PROVIDER: S-EPMC11926252 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature