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dc.contributor.authorMuh, Fauzi
dc.contributor.authorLee, Seong-Kyun
dc.contributor.authorHoque, Mohammad Rafiul
dc.contributor.authorHan, Jin-Hee
dc.contributor.authorPark, Ji-Hoon
dc.contributor.authorFirdaus, Egy Rahman
dc.contributor.authorMoon, Robert W.
dc.contributor.authorLau, Yee Ling
dc.contributor.authorHan, Eun-Taek
dc.date.accessioned2019-07-18T11:30:08Z
dc.date.available2019-07-18T11:30:08Z
dc.date.issued2018-07-27
dc.identifier.citationMuh , F , Lee , S-K , Hoque , M R , Han , J-H , Park , J-H , Firdaus , E R , Moon , R W , Lau , Y L & Han , E-T 2018 , ' In vitro invasion inhibition assay using antibodies against Plasmodium knowlesi Duffy binding protein alpha and apical membrane antigen protein 1 in human erythrocyte-adapted P. knowlesi A1-H.1 strain ' , Malaria Journal , vol. 17 , 272 . https://doi.org/10.1186/s12936-018-2420-4en
dc.identifier.issn1475-2875
dc.identifier.otherPURE: 259673185
dc.identifier.otherPURE UUID: b39ef903-81ff-4911-a345-f19b9f363142
dc.identifier.otherWOS: 000440181600001
dc.identifier.otherScopus: 85050721633
dc.identifier.otherORCID: /0000-0002-3966-9110/work/59698773
dc.identifier.urihttp://hdl.handle.net/10023/18124
dc.description.abstractBackground: The rapid process of malaria erythrocyte invasion involves ligand-receptor interactions. Inducing antibodies against specific ligands or receptors that abrogate the invasion process is a key challenge for blood stage vaccine development. However, few candidates were reported and remain to be validated for the discovery of new vaccine candidates in Plasmodium knowlesi. Methods: In order to investigate the efficacy of pre-clinical vaccine candidates in P. knowlesi-infected human cases, this study describes an in vitro invasion inhibition assay, using a P. knowlesi strain adapted to in vitro growth in human erythrocytes, PkA1-H. 1. Recombinant proteins of P. knowlesi Duffy binding protein alpha (PkDBPα) and apical membrane antigen 1 (PkAMA1) were produced in Escherichia coli system and rabbit antibodies were generated from immune animals. Results: PkDBPα and PkAMA1 recombinant proteins were expressed as insoluble and produced as a functional refolded form for this study. Antibodies against PkDBPα and PkAMA1 specifically recognized recombinant proteins and native parasite proteins in schizont-stage parasites on the merozoite organelles. Single and combination of anti-PkDBPα and anti-PkAMA1 antibodies elicited strong growth inhibitory effects on the parasite in concentrationdependent manner. Meanwhile, IgG prevalence of PkDBPα and PkAMA1 were observed in 13.0 and 46.7% in human clinical patients, respectively. Conclusion: These data provide support for the validation of in vitro growth inhibition assay using antibodies of DBPα and AMA1 in human-adapted P. knowlesi parasite PkA1-H. 1 strain.
dc.format.extent11
dc.language.isoeng
dc.relation.ispartofMalaria Journalen
dc.rights© The Author(s) 2018. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.en
dc.subjectPlasmodium knowlesien
dc.subjectZoonotic malariaen
dc.subjectPkDBP alphaen
dc.subjectPkAMA1en
dc.subjectInvasionen
dc.subjectInhibitionen
dc.subjectQH301 Biologyen
dc.subjectRM Therapeutics. Pharmacologyen
dc.subjectNDASen
dc.subject.lccQH301en
dc.subject.lccRMen
dc.titleIn vitro invasion inhibition assay using antibodies against Plasmodium knowlesi Duffy binding protein alpha and apical membrane antigen protein 1 in human erythrocyte-adapted P. knowlesi A1-H.1 strainen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Medicineen
dc.identifier.doihttps://doi.org/10.1186/s12936-018-2420-4
dc.description.statusPeer revieweden


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