Oral Presentation Lorne Infection and Immunity 2013

New insights into the structure and function of a major virulence protein translocon in Plasmodium falciparum (#2)

Brendan S Crabb 1 , Tania F de Koning-Ward 2 , Jamie Rossjohn 3 , Alan F Cowman 4 , Paul R Gilson 1
  1. Burnet Institute, Melbourne, VIC, Australia
  2. Medicine, Deakin University, Geelong, VIC, Australia
  3. Biochemistry & Molecular Biology, Monash University, Clayton, VIC, Australia
  4. Infection and Immunity, Walter and Eliza Hall Institutte, Melbourne, VIC, Australia

A few years ago we discovered a protein complex that we proposed is the translocon responsible for export of the major family of exported virulence proteins in the human malaria parasite P. falciparum. Despite this advance, many key questions remain about the mechanism and action of this translocon, termed PTEX, and indeed genetic proof of its role in translocation has been lacking. Our group have collaborated closely in recent years to address these questions.  We have generated new data using biochemical, structural biology, super-resolution microscopy, electron microscopy and knockout and conditional knockout approaches that are consistent with a key role for PTEX in virulence protein translocation. These data also signficantly advance our understanding of the mechanism by which this protein translocation occurs.