A Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability
Fabio L da Silva, Matthew WA Dixon, Colin M Stack, Franka Teuscher, Elena Taran, Malcolm K Jones, Erica Lovas, Leann Tilley, Christopher L Brown, Katharine R Trenholme, John P Dalton, Donald L Gardiner, Tina S Skinner-Adams
EXPERIMENTAL PARASITOLOGY | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2016
Infection with the apicomplexan parasite Plasmodium falciparum is a major cause of morbidity and mortality worldwide. One of the striking features of this parasite is its ability to remodel and decrease the deformability of host red blood cells, a process that contributes to disease. To further understand the virulence of Pf we investigated the biochemistry and function of a putative Pf S33 proline aminopeptidase (PfPAP). Unlike other P. falciparum aminopeptidases, PfPAP contains a predicted protein export element that is non-syntenic with other human infecting Plasmodium species. Characterization of PfPAP demonstrated that it is exported into the host red blood cell and that it is a prolyl ..View full abstract
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Awarded by National Health & Medical Research Council of Australia
Awarded by Australia Research Council
This work was supported by the National Health & Medical Research Council of Australia (1098992, 1078065 and 0602541) and the Australia Research Council (PD0666128 and DP110100624).