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dc.contributor.authorPatchanee Chootongen_US
dc.contributor.authorTasanee Panichakulen_US
dc.contributor.authorChongrak Permmongkolen_US
dc.contributor.authorSamantha J. Barnesen_US
dc.contributor.authorRachanee Udomsangpetchen_US
dc.contributor.authorJohn H. Adamsen_US
dc.contributor.otherDepartment of Clinical Microbiology and Applied Technology-
dc.date.accessioned2013-06-17T08:10:50Z-
dc.date.accessioned2017-06-20T16:08:13Z-
dc.date.available2013-06-17T08:10:50Z-
dc.date.available2017-06-20T16:08:13Z-
dc.date.created2013-06-17-
dc.date.issued2012-04-
dc.identifier.citationPlos One. Vol.7, No.4 (2012), e35769en_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/2067-
dc.description.abstractPlasmodium vivax Duffy binding protein region II (DBPII) is an important vaccine candidate for antibody-mediated immunity against vivax malaria. A significant challenge for vaccine development of DBPII is its highly polymorphic nature that alters sensitivity to neutralizing antibody responses. Here, we aim to characterize naturally-acquired neutralizing antibodies against DBPII in individual Thai residents to give insight into P. vivax vaccine development in Thailand. Anti-DBPII IgG significantly increased in acute vivax infections compared to uninfected residents and naive controls. Antibody titers and functional anti-DBPII inhibition varied widely and there was no association between titer and inhibition activity. Most high titer plasmas had only a moderate to no functional inhibitory effect on DBP binding to erythrocytes, indicating the protective immunity against DBPII binding is strain specific. Only 5 of 54 samples were highly inhibitory against DBP erythrocyte-binding function. Previously identified target epitopes of inhibitory anti-DBPPII IgG (H1, H2 and H3) were localized to the dimer interface that forms the DARC binding pocket. Amino acid polymorphisms (monomorphic or dimorphic) in H1 and H3 protective epitopes change sensitivity of immune inhibition by alteration of neutralizing antibody recognition. The present study indicates Thai variant H1.T1 (R308S), H3.T1 (D384G) and H3.T3 (K386N) are the most important variants for a DBPII candidate vaccine needed to protect P. vivax in Thai residents.en_US
dc.language.isoen_USen_US
dc.publisherMahidol Universityen_US
dc.rightsMahidol Universityen_US
dc.subjectAnti-Duffy Binding Proteinen_US
dc.subjectplasmodium vivax Vaccineen_US
dc.subjectThailanden_US
dc.titleCharacterization of Inhibitory Anti-Duffy Binding Protein II Immunity: Approach to Plasmodium vivax Vaccine Development in Thailanden_US
dc.typeArticleen_US
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3338783/pdf/pone.0035769.pdf-
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