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

Journal article

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

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 Infectious Diseases

Elena Taran Author Chemical Engineering

Leann Tilley Author Biochemistry and Pharmacology

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Grants

Awarded by National Health & Medical Research Council of Australia

Awarded by Australia 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).