The Plasmodium falciparum exportome contains non-canonical PEXEL/HT proteinsSchulze, J., Kwiatkowski, M., Borner, J., Schlueter, H., Bruchhaus, I., Burmester, T., Spielmann, T. & Pick, C., Jul-2015, In : Molecular Microbiology. 97, 2, p. 301-314 14 p.
Research output: Contribution to journal › Article › Academic › peer-review
The pathogenicity of Plasmodium falciparum is partly due to parasite-induced host cell modifications. These modifications are facilitated by exported P.falciparum proteins, collectively referred to as the exportome. Export of several hundred proteins is mediated by the PEXEL/HT, a protease cleavage site. The PEXEL/HT is usually comprised of five amino acids, of which R at position 1, L at position 3 and E, D or Q at position 5 are conserved and important for export. Non-canonical PEXEL/HTs with K or H at position 1 and/or I at position 3 are presently considered non-functional. Here, we show that non-canonical PEXEL/HT proteins are overrepresented in P.falciparum and other Plasmodium species. Furthermore, we show that non-canonical PEXEL/HTs can be cleaved and can promote export in both a REX3 and a GBP reporter, but not in a KAHRP reporter, indicating that non-canonical PEXEL/HTs are functional in concert with a supportive sequence environment. We then selected P.falciparum proteins with a non-canonical PEXEL/HT and show that some of these proteins are exported and that their export depends on non-canonical PEXEL/HTs. We conclude that PEXEL/HT plasticity is higher than appreciated and that non-canonical PEXEL/HT proteins cannot categorically be excluded from Plasmodium exportome predictions.
|Number of pages||14|
|Publication status||Published - Jul-2015|
- MALARIA PARASITES, HOST-CELL, INFECTED ERYTHROCYTE, PLASMEPSIN V, VIRULENCE, PTEX, IDENTIFICATION, ANTIGEN, SIGNAL