Conference Agenda
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Daily Overview |
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CP11: Cells, Molecules & Genes 2 - 10 min talks Location: Lecture Theatre 1 Session Chair: Ellis Joch, Griffith University Session Chair: Wisam Dawood, Griffith University | |
| Presentation 5 | |
Pfs16 forms an oligomeric complex with a membrane-spanning pore in the malaria parasite parasitophorous vacuole membrane 1: UNSW Sydney, Australia; 2: Australian National University Pfs16 is a 16 kDa protein expressed early in the process of gametocyte development in Plasmodium falciparum. It localises to the parasitophorous vacuole membrane (PVM) of gametocytes. Previous studies have focused exclusively on its monomeric form. However, AlphaFold modelling predicts that Pfs16 assembles into an oligomeric complex containing a membrane-spanning pore. Given the essential role of Pfs16 in parasite transmission, we aimed to characterise this oligomeric structure and its function, which could provide new insights for transmission-blocking strategies. A combination of molecular and structural biology techniques was employed, including chemical crosslinking, Western blotting, native gel electrophoresis, and surface biotinylation, to explore its oligomeric subunits. Its functional activity was characterised using electrophysiological analysis in the Xenopus oocyte expression system. Both in silico modelling and experimental data indicate that Pfs16 forms a pentameric complex. Electrophysiological analysis in Xenopus oocytes has demonstrated that the membrane-spanning pore exhibits ion-conducting activity, supporting the presence of a functional pore. These results provide evidence that Pfs16 assembles into an oligomeric, likely pentameric, ion channel. Given its essential role in gametocyte development and transmission, targeting this complex may represent a promising strategy for the development of transmission-blocking interventions. | |
