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dc.contributor.authorda Silva, Fabio L
dc.contributor.authorDixon, Matthew WA
dc.contributor.authorStack, Colin M
dc.contributor.authorTeuscher, Franka
dc.contributor.authorTaran, Elena
dc.contributor.authorJones, Malcolm K
dc.contributor.authorLovas, Erica
dc.contributor.authorTilley, Leann
dc.contributor.authorBrown, Christopher L
dc.contributor.authorTrenholme, Katharine R
dc.contributor.authorDalton, John P
dc.contributor.authorGardiner, Donald L
dc.contributor.authorSkinner-Adams, Tina S
dc.date.accessioned2019-05-23T02:53:04Z
dc.date.available2019-05-23T02:53:04Z
dc.date.issued2016
dc.identifier.issn0014-4894
dc.identifier.doi10.1016/j.exppara.2016.06.013
dc.identifier.urihttp://hdl.handle.net/10072/142878
dc.description.abstractInfection 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.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.relation.ispartofpagefrom13
dc.relation.ispartofpageto21
dc.relation.ispartofjournalExperimental Parasitology
dc.relation.ispartofvolume189
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchMicrobiology not elsewhere classified
dc.subject.fieldofresearchVeterinary sciences
dc.subject.fieldofresearchcode3107
dc.subject.fieldofresearchcode310799
dc.subject.fieldofresearchcode3009
dc.titleA Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.description.versionAccepted 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.hasfulltextFull Text
gro.griffith.authorSkinner-Adams, Tina


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