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dc.contributor.authorBouyer, G
dc.contributor.authorReininger, L
dc.contributor.authorRamdani, G
dc.contributor.authorD Phillips, L
dc.contributor.authorSharma, Vikram
dc.contributor.authorEgee, S
dc.contributor.authorLangsley, G
dc.contributor.authorLasonder, Edwin
dc.date.accessioned2016-06-02T12:00:20Z
dc.date.issued2017-05-01
dc.identifier.issn1079-9796
dc.identifier.issn1096-0961
dc.identifier.urihttp://hdl.handle.net/10026.1/4795
dc.description.abstract

The phosphorylation status of red blood cell proteins is strongly altered during the infection by the malaria parasite Plasmodium falciparum. We identify the key phosphorylation events that occur in the erythrocyte membrane and cytoskeleton during infection, by a comparative analysis of global phospho-proteome screens between infected (obtained at schizont stage) and uninfected RBCs. The meta-analysis of reported mass spectrometry studies revealed a novel compendium of 495 phosphorylation sites in 182 human proteins with regulatory roles in red cell morphology and stability, with about 25% of these sites specific to infected cells. A phosphorylation motif analysis detected 7 unique motifs that were largely mapped to kinase consensus sequences of casein kinase II and of protein kinase A/protein kinase C. This analysis highlighted prominent roles for PKA/PKC involving 78 phosphorylation sites. We then compared the phosphorylation status of PKA (PKC) specific sites in adducin, dematin, Band 3 and GLUT-1 in uninfected RBC stimulated or not by cAMP to their phosphorylation status in iRBC. We showed cAMP-induced phosphorylation of adducin S59 by immunoblotting and we were able to demonstrate parasite-induced phosphorylation for adducin S726, Band 3 and GLUT-1, corroborating the protein phosphorylation status in our erythrocyte phosphorylation site compendium.

dc.format.extent35-44
dc.format.mediumPrint-Electronic
dc.languageen
dc.language.isoen
dc.publisherElsevier BV
dc.subjectErythrocyte
dc.subjectP. falciparum
dc.subjectProtein phosphorylation
dc.subjectcAMP/protein kinase A
dc.subjectGLUT-1
dc.subjectCytoskeleton
dc.titlePlasmodium falciparum infection induces dynamic changes in the erythrocyte phospho-proteome.
dc.typejournal-article
dc.typeJournal Article
dc.typeResearch Support, Non-U.S. Gov't
plymouth.author-urlhttps://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000374512600008&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=11bb513d99f797142bcfeffcc58ea008
plymouth.volume58
plymouth.publication-statusPublished
plymouth.journalBlood cells, molecules & diseases
dc.identifier.doi10.1016/j.bcmd.2016.02.001
plymouth.organisational-group/Plymouth
plymouth.organisational-group/Plymouth/Faculty of Health
plymouth.organisational-group/Plymouth/Faculty of Health/School of Biomedical Sciences
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA01 Clinical Medicine
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA01 Clinical Medicine/UoA01 Clinical Medicine
plymouth.organisational-group/Plymouth/Research Groups
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)/CBR
plymouth.organisational-group/Plymouth/Users by role
plymouth.organisational-group/Plymouth/Users by role/Academics
dc.publisher.placeUnited States
dcterms.dateAccepted2016-02-05
dc.rights.embargodate2017-2-13
dc.identifier.eissn1096-0961
dc.rights.embargoperiodNot known
rioxxterms.versionofrecord10.1016/j.bcmd.2016.02.001
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2017-05-01
rioxxterms.typeJournal Article/Review


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