dc.contributor.author | da Silva, Fabio L | |
dc.contributor.author | Dixon, Matthew WA | |
dc.contributor.author | Stack, Colin M | |
dc.contributor.author | Teuscher, Franka | |
dc.contributor.author | Taran, Elena | |
dc.contributor.author | Jones, Malcolm K | |
dc.contributor.author | Lovas, Erica | |
dc.contributor.author | Tilley, Leann | |
dc.contributor.author | Brown, Christopher L | |
dc.contributor.author | Trenholme, Katharine R | |
dc.contributor.author | Dalton, John P | |
dc.contributor.author | Gardiner, Donald L | |
dc.contributor.author | Skinner-Adams, Tina S | |
dc.date.accessioned | 2019-05-23T02:53:04Z | |
dc.date.available | 2019-05-23T02:53:04Z | |
dc.date.issued | 2016 | |
dc.identifier.issn | 0014-4894 | |
dc.identifier.doi | 10.1016/j.exppara.2016.06.013 | |
dc.identifier.uri | http://hdl.handle.net/10072/142878 | |
dc.description.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 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. | |
dc.description.peerreviewed | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | Elsevier | |
dc.relation.ispartofpagefrom | 13 | |
dc.relation.ispartofpageto | 21 | |
dc.relation.ispartofjournal | Experimental Parasitology | |
dc.relation.ispartofvolume | 189 | |
dc.subject.fieldofresearch | Microbiology | |
dc.subject.fieldofresearch | Microbiology not elsewhere classified | |
dc.subject.fieldofresearch | Veterinary sciences | |
dc.subject.fieldofresearchcode | 3107 | |
dc.subject.fieldofresearchcode | 310799 | |
dc.subject.fieldofresearchcode | 3009 | |
dc.title | A Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - Journal Articles | |
dcterms.license | http://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.description.version | Accepted Manuscript (AM) | |
gro.rights.copyright | © 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. | |
gro.hasfulltext | Full Text | |
gro.griffith.author | Skinner-Adams, Tina | |