| Title: |
A Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability |
| Authors: |
da Silva, Fabio L; Dixon, Matthew WA; Stack, Colin M; Teuscher, Franka; Taran, Elena; Jones, Malcolm K; Lovas, Erica; Tilley, Leann; Brown, Christopher L; Trenholme, Katharine R; Dalton, John P; Gardiner, Donald L; Skinner-Adams, Tina S |
| Publisher Information: |
Elsevier |
| Publication Year: |
2016 |
| Collection: |
Griffith University: Griffith Research Online |
| Subject Terms: |
Microbiology; Microbiology not elsewhere classified; Veterinary sciences |
| Description: |
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. ; Full Text |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| Relation: |
Experimental Parasitology; https://hdl.handle.net/10072/142878 |
| DOI: |
10.1016/j.exppara.2016.06.013 |
| Availability: |
https://hdl.handle.net/10072/142878; https://doi.org/10.1016/j.exppara.2016.06.013 |
| Rights: |
http://creativecommons.org/licenses/by-nc-nd/4.0/ ; © 2016 Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International Licence which permits unrestricted, non-commercial use, distribution and reproduction in any medium, providing that the work is properly cited. ; open access |
| Accession Number: |
edsbas.AF7A198F |
| Database: |
BASE |