A Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability

FL da Silva; MWA Dixon; CM Stack; F Teuscher; E Taran; MK Jones; E Lovas; L Tilley; CL Brown; KR Trenholme; JP Dalton; DL Gardiner; TS Skinner-Adams

Journal article

A Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability

FL da Silva, MWA Dixon, CM Stack, F Teuscher, E Taran, MK Jones, E Lovas, L Tilley, CL Brown, KR Trenholme, JP Dalton, DL Gardiner, TS Skinner-Adams

Experimental Parasitology | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2016

DOI: 10.1016/j.exppara.2016.06.013

Abstract

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 ..

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University of Melbourne Researchers

Matthew Dixon Author

Elena Taran Author

Leann Tilley Author

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Grants

Awarded by Australian Research Council

Funding Acknowledgements

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).