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New insights into host-parasite ubiquitin proteome dynamics in P. falciparum infected red blood cells using a TUBEs-MS approach

2016-04-29Journal article Restricted access
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dc.contributor.authorMata-Cantero, L.
dc.contributor.authorAzkargorta, M.
dc.contributor.authorAillet, F.
dc.contributor.authorXolalpa, W.
dc.contributor.authorLaFuente, M.J.
dc.contributor.authorElortza, F.
dc.contributor.authorCarvalho, A.S.
dc.contributor.authorMartin-Plaza, J.
dc.contributor.authorMatthiesen, Rune
dc.contributor.authorRodriguez, M.S.
dc.date.accessioned2016-05-24T16:38:35Z
dc.date.available2020-05-01T00:30:11Z
dc.date.issued2016-04-29
dc.description.abstractMalaria, caused by Plasmodium falciparum (P. falciparum), ranks as one of the most baleful infectious diseases worldwide. New antimalarial treatments are needed to face existing or emerging drug resistant strains. Protein degradation appears to play a significant role during the asexual intraerythrocytic developmental cycle (IDC) of P. falciparum. Inhibition of the ubiquitin proteasome system (UPS), a major intracellular proteolytic pathway, effectively reduces infection and parasite replication. P. falciparum and erythrocyte UPS coexist during IDC but the nature of their relationship is largely unknown. We used an approach based on Tandem Ubiquitin-Binding Entities (TUBEs) and 1D gel electrophoresis followed by mass spectrometry to identify major components of the TUBEs-associated ubiquitin proteome of both host and parasite during ring, trophozoite and schizont stages. Ring-exported protein (REX1), a P. falciparum protein located in Maurer's clefts and important for parasite nutrient import, was found to reach a maximum level of ubiquitylation in trophozoites stage. The Homo sapiens (H. sapiens) TUBEs associated ubiquitin proteome decreased during the infection, whereas the equivalent P. falciparum TUBEs-associated ubiquitin proteome counterpart increased. Major cellular processes such as DNA repair, replication, stress response, vesicular transport and catabolic events appear to be regulated by ubiquitylation along the IDC P. falciparum infection.pt_PT
dc.description.sponsorshipThis work was funded by the GSK OPEN lab foundation (GSKOLF, grant number TC001), MINECO-Spain grant BFU2011-28536 (MSR). LMC was supported by the GSKOLF. GSKOLF had no role in study design, data collection and analysis, or preparation of the manuscript, but they had to agree on the publication of this work. RM is sustained by the Fundação para a Ciência e a Tecnologia (FCT) investigator 2012 program. ASC is supported by grant SFRH/BPD/85569/2012 funded by Fundação para a Ciência e Tecnologia. The authors would like to acknowledge networking support by the Proteostasis COST Action (BM1307).pt_PT
dc.identifier.citationJ Proteomics. 2016 Apr 29;139:45-59. doi: 10.1016/j.jprot.2016.03.004. Epub 2016 Mar 10.pt_PT
dc.identifier.doi10.1016/j.jprot.2016.03.004pt_PT
dc.identifier.issn1874-3919
dc.identifier.urihttp://hdl.handle.net/10400.18/3819
dc.language.isoengpt_PT
dc.publisherElsevier/European Proteomics Association (EuPA)pt_PT
dc.relation.publisherversionhttp://www.sciencedirect.com/science/article/pii/S1874391916300598pt_PT
dc.subjectDrug Targetspt_PT
dc.subjectMalariapt_PT
dc.subjectMass Spectrometrypt_PT
dc.subjectPlasmodium falciparumpt_PT
dc.subjectTUBEspt_PT
dc.subjectUbiquitinpt_PT
dc.subjectComputational and Experimental Biologypt_PT
dc.subjectInfecções Sistémicas e Zoonosespt_PT
dc.titleNew insights into host-parasite ubiquitin proteome dynamics in P. falciparum infected red blood cells using a TUBEs-MS approachpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage59pt_PT
oaire.citation.startPage45pt_PT
oaire.citation.titleJournal of Proteomicspt_PT
oaire.citation.volume139pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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