AlphaFold3 predictions files for PfVps16 paper

The organelles of the apical complex (rhoptries, micronemes and dense granules) are critical for erythrocyte invasion by the malaria parasite <i>Plasmodium falciparum</i>. Though they have essential roles in the parasite lifecycle, the mechanisms behind their biogenesis are still poorly defined. The Class C Vps proteins Vps11, 16, 18 and 33 constitute the core of the CORVET and HOPS complexes implicated in vesicle tethering and fusion in the eukaryotic endolysosomal system. Work in the model apicomplexan <i>Toxoplasma gondii</i> has revealed that TgVps11 is essential for the generation of the apical complex. <i>P. falciparum</i> possesses all the four subunits of the Vps-C complex, and very recent work has shown that some of its components were critical for host-cell cytosol trafficking and the biogenesis of the apical complex. We here show that the <i>P. falciparum</i> orthologue of Vps16, a member of the Vps-C complex, is expressed throughout the asexual erythrocytic cycle and that it is potentially associated with the Golgi apparatus and the rhoptries in schizont stage parasites. We then demonstrate by immunoprecipitation and mass spectrometry that PfVps16 interacts with all the members of the canonical Vps-C complex along with the Vps3 CORVET component. Interestingly, three uncharacterized <i>Plasmodium</i> specific proteins are also found as interactors of PfVps16 and structural predictions revealed that two of them possess folds commonly found in proteins present in membrane tethering complexes. These findings suggest that <i>P. falciparum</i> may possess both conserved and parasite-specific features within its endosomal tethering machinery.