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dc.contributor.authorTran, TN
dc.contributor.authorGardiner, DL
dc.contributor.authorSkinner-Adams, TS
dc.contributor.authorAndrews, KT
dc.date.accessioned2017-05-03T16:57:46Z
dc.date.available2017-05-03T16:57:46Z
dc.date.issued2008
dc.date.modified2012-08-28T08:54:18Z
dc.identifier.issn0020-7519
dc.identifier.doi10.1016/S0020-7519(07)00459-6
dc.identifier.urihttp://hdl.handle.net/10072/25406
dc.description.abstractP. falciparum (Pf) histone deacetylases (HDACs) have been proposed as new antimalarial drug targets. In higher eukaryotes, HDACs are involved in regulating gene expression and cellular development. The Pf genome encodes for at least five putative HDACs. One PfHDAC (PFI1260c; PfHDAC-1) shares greater than 50% sequence homology with class I HDACs from yeast, mice, and humans. Two Pf class II HDAC homologues (PF14_0690 (PfHDAC-2) & PF10_0078) have limited sequence similarity to mammalian HDACs, except in predicted deacetylase domains. One of two class III HDAC homologues (PfSir2) has been "knocked-out" in Pf and appears to play a role in regulating virulence gene expression (var genes). We have now begun to characterize the class I and II PfHDACs in order to understand the role of these enzymes in Plasmodium and to guide rational development of new antimalarial agents. We have found that PfHDAC-1 and 2 are transcribed in ring, trophozoite and schizont stage Pf parasites, as determined by Northern blot. Western blot using polyclonal antisera shows that PfHDAC-1 is expressed in all intraerythrocytic stages. Localization of PfHDAC-1 within the infected erythrocyte had been confirmed as being predominantly nuclear using transgenic Pf parasites over-expressing PfHDAC-1 fused to GFP or c-myc tags. Pf extracts display deacetylase activity and this activity can be inhibited by classic class I/II mammalian HDAC inhibitors such as trichostatin A (TSA). This work contributes to our understanding of the role of HDACs in Pf and to the development of antimalarial agents that act on this new class of drug target within the parasite.
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier Ltd
dc.publisher.placeUnited Kingdom
dc.publisher.urihttps://www.sciencedirect.com/journal/international-journal-for-parasitology/vol/38/suppl/S1
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofconferencename3rd Meeting on Molecular Approaches to Malaria (MAM 2008)
dc.relation.ispartofconferencetitleINTERNATIONAL JOURNAL FOR PARASITOLOGY
dc.relation.ispartofdatefrom2008-02-03
dc.relation.ispartofdateto2008-02-07
dc.relation.ispartoflocationLorne, AUSTRALIA
dc.relation.ispartofpagefromS63
dc.relation.ispartofpagetoS63
dc.relation.ispartofvolume38
dc.rights.retentionY
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchZoology
dc.subject.fieldofresearchVeterinary Sciences
dc.subject.fieldofresearchcode0605
dc.subject.fieldofresearchcode0608
dc.subject.fieldofresearchcode0707
dc.titlePlasmodium falciparum histone deacetylases
dc.typeConference output
dc.type.descriptionE3 - Conferences (Extract Paper)
dc.type.codeE - Conference Publications
gro.date.issued2008
gro.hasfulltextNo Full Text
gro.griffith.authorAndrews, Katherine T.
gro.griffith.authorSkinner-Adams, Tina
gro.griffith.authorGardiner, Donald


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    Contains papers delivered by Griffith authors at national and international conferences.

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