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dc.contributor.authorTremp, AZ
dc.contributor.authorSharma, Vikram
dc.contributor.authorCarter, V
dc.contributor.authorLasonder, Edwin
dc.contributor.authorDessens, JT
dc.date.accessioned2017-04-19T12:38:47Z
dc.date.available2017-04-19T12:38:47Z
dc.date.issued2017-04-13
dc.identifier.issn0166-6851
dc.identifier.issn1872-9428
dc.identifier.urihttp://hdl.handle.net/10026.1/9093
dc.description.abstract

Successful sporogony of Plasmodium berghei in vector mosquitoes requires expression of a family of six modular proteins named LCCL lectin domain adhesive-like proteins (LAPs). The LAPs share a subcellular localization in the crystalloid, a unique parasite organelle that forms during ookinete development. Here, LAP interactions in P. berghei were studied using a series of parasite lines stably expressing reporter-tagged LAPs combined with affinity purification and high accuracy label free quantitative mass spectrometry. Our results show that abundant complexes containing LAP1, LAP2 and LAP3 are formed in gametocytes through high avidity interactions. Following fertilization, LAP4, LAP5 and LAP6 are recruited to this complex, a process that is facilitated by LAP1 chiefly through its scavenger receptor cysteine-rich modules. These collective findings provide new insight into the temporal and molecular dynamics of protein complex formation that lead up to, and are required for, crystalloid biogenesis and downstream sporozoite transmission of malaria parasites.

dc.format.extent87-90
dc.format.mediumPrint-Electronic
dc.languageen
dc.language.isoen
dc.publisherElsevier BV
dc.subjectLC/MS/MS
dc.subjectLCCL
dc.subjectcrystalloid organelle
dc.subjecttransmission blockade
dc.titleLCCL protein complex formation in Plasmodium is critically dependent on LAP1.
dc.typejournal-article
dc.typeJournal Article
dc.typeResearch Support, Non-U.S. Gov't
plymouth.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/28414172
plymouth.volume214
plymouth.publication-statusPublished online
plymouth.journalMol Biochem Parasitol
dc.identifier.doi10.1016/j.molbiopara.2017.04.005
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.placeNetherlands
dcterms.dateAccepted2017-04-12
dc.rights.embargodate2018-04-13
dc.identifier.eissn1872-9428
dc.rights.embargoperiod12 months
rioxxterms.versionofrecord10.1016/j.molbiopara.2017.04.005
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/under-embargo-all-rights-reserved
rioxxterms.licenseref.startdate2017-04-13
rioxxterms.typeJournal Article/Review
plymouth.funderLAP function in apicomplexan parasite development::BBSRC
plymouth.oa-locationhttp://www.sciencedirect.com/science/article/pii/S016668511730052X?via=ihub


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