Plasmodium berghei and Plasmodium falciparum LC-MS/MS

Previously published data indicated that PgCHT2 forms a high molecular weight (HMW), reduction-sensitive complex; data suggested that the binding partner is the ookinete-produced von Willebrand A-domain-containing protein, WARP. To test the hypothesis that transgenic P.berghei ookinete-produced PfCHT1 could form a high molecular homo-multimer or, alternatively, could interact with P. berghei ookinete-produced proteins to produce a HMW hetero-multimer, we created a chimeric P. berghei parasites expressing PfCHT1 to replace PbCHT1, allowing production of large numbers of PfCHT1-expressing ookinetes.Mass spectrometry analysis was carried out on the chitin affinity pulled down proteins from the Pb-PfCHT1(r) ookinete culture supernatant.