| Title: |
A Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability |
| Authors: |
da Silva, FL; Dixon, MWA; Stack, CM; Teuscher, F; Taran, E; Jones, MK; Lovas, E; Tilley, L; Brown, CL; Trenholme, KR; Dalton, JP; Gardiner, DL; Skinner-Adams, TS |
| Publication Year: |
2016 |
| Collection: |
University of Technology Sydney: OPUS - Open Publications of UTS Scholars |
| Subject Terms: |
Mycology & Parasitology; Erythrocytes; Erythrocyte Membrane; Humans; Plasmodium falciparum; Aminopeptidases; Recombinant Proteins; RNA; Protozoan; Antibodies; Microscopy; Electron; Transmission; Fluorescence; Atomic Force; Blotting; Western; Northern; Transfection; Sequence Alignment; Cell Adhesion; Amino Acid Sequence; Erythrocyte Deformability; Elasticity; Gene Knockout Techniques; Real-Time Polymerase Chain Reaction |
| Description: |
© 2016 Elsevier Inc. 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 aminopeptidase with a preference for N-terminal proline substrates. In addition genetic deletion of this exopeptidase was shown to lead to an increase in the deformability of parasite-infected red cells and in reduced adherence to the endothelial cell receptor CD36 under flow conditions. Our studies suggest that PfPAP plays a role in the rigidification and adhesion of infected red blood cells to endothelial surface receptors, a role that may make this protein a novel target for anti-disease interventions strategies. |
| Document Type: |
article in journal/newspaper |
| File Description: |
application/pdf |
| Language: |
unknown |
| ISSN: |
0014-4894 |
| Relation: |
Experimental Parasitology; Experimental Parasitology, 2016, 169 pp. 13 - 21; http://hdl.handle.net/10453/103626 |
| Availability: |
http://hdl.handle.net/10453/103626 |
| Accession Number: |
edsbas.4DB40741 |
| Database: |
BASE |