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dc.contributor.authorSaeed, S
dc.contributor.authorTremp, AZ
dc.contributor.authorSharma, V
dc.contributor.authorLasonder, E
dc.contributor.authorDessens, JT
dc.date.accessioned2020-03-10T08:28:59Z
dc.date.issued2020-03-04
dc.identifier.issn1469-221X
dc.identifier.issn1469-3178
dc.identifier.otherARTN e47832
dc.identifier.urihttp://hdl.handle.net/10026.1/15442
dc.description.abstract

Nicotinamide adenine dinucleotide (NAD) and its phosphorylated form (NADP) are vital for cell function in all organisms and form cofactors to a host of enzymes in catabolic and anabolic processes. NAD(P) transhydrogenases (NTHs) catalyse hydride ion transfer between NAD(H) and NADP(H). Membrane-bound NTH isoforms reside in the cytoplasmic membrane of bacteria, and the inner membrane of mitochondria in metazoans, where they generate NADPH. Here, we show that malaria parasites encode a single membrane-bound NTH that localises to the crystalloid, an organelle required for sporozoite transmission from mosquitos to vertebrates. We demonstrate that NTH has an essential structural role in crystalloid biogenesis, whilst its enzymatic activity is required for sporozoite development. This pinpoints an essential function in sporogony to the activity of a single crystalloid protein. Its additional presence in the apicoplast of sporozoites identifies NTH as a likely supplier of NADPH for this organelle during liver infection. Our findings reveal that Plasmodium species have co-opted NTH to a variety of non-mitochondrial organelles to provide a critical source of NADPH reducing power.

dc.format.extente47832-
dc.format.mediumPrint-Electronic
dc.languageen
dc.language.isoen
dc.publisherEMBO
dc.subjectmalaria
dc.subjectoocyst
dc.subjectookinete
dc.subjectsporozoite
dc.subjecttranshydrogenase
dc.subjecttransmission
dc.titleNAD (P) transhydrogenase has vital non‐mitochondrial functions in malaria parasite transmission
dc.typejournal-article
dc.typeArticle
plymouth.author-urlhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000519213200023&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=11bb513d99f797142bcfeffcc58ea008
plymouth.issue3
plymouth.volume21
plymouth.publisher-urlhttp://dx.doi.org/10.15252/embr.201947832
plymouth.publication-statusPublished
plymouth.journalEMBO reports
dc.identifier.doi10.15252/embr.201947832
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.placeEngland
dcterms.dateAccepted2019-12-17
dc.rights.embargodate2020-3-11
dc.identifier.eissn1469-3178
dc.rights.embargoperiodNot known
rioxxterms.versionofrecord10.15252/embr.201947832
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2020-03-04
rioxxterms.typeJournal Article/Review
plymouth.funderLAP function in apicomplexan parasite development::BBSRC


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