Abstract
Plasmodium falciparum serine-repeat antigen (SERA) is one potential blood-stage vaccine candidate and is expressed as a protomer that is subsequently processed into four fragments (P47, P50, P6, and P17). Although recent evidence shows that P50 exhibits chymotrypsin-like protease activity, the function of SERA is still largely unknown. Here, we found that apart from cathepsin L-like cysteine protease, P50 showed significant homology to silicatein-α and testin which were shown to bind to cellular components, suggesting that SERA may have similar function. Immunoprecipitation of schizont lysate and molecular assignment of its precipitate by mass spectrometry provided evidence that SERA forms a homodimer through disulfide bond. Moreover, analysis of the fate of SERA using cell-free system revealed that the kinetics of conversion of SERA dimer into monomer is faster than that of processing of SERA monomer into various fragments. These findings may contribute to elucidate a possible function of SERA other than a protease.
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