Publication: Characterization of Inhibitory Anti-Duffy Binding Protein II Immunity: Approach to Plasmodium vivax Vaccine Development in Thailand
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Issued Date
2012-04
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eng
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Mahidol University
Bibliographic Citation
Plos One. Vol.7, No.4 (2012), e35769
Suggested Citation
Patchanee Chootong, Tasanee Panichakul, Chongrak Permmongkol, Samantha J. Barnes, Rachanee Udomsangpetch, John H. Adams Characterization of Inhibitory Anti-Duffy Binding Protein II Immunity: Approach to Plasmodium vivax Vaccine Development in Thailand. Plos One. Vol.7, No.4 (2012), e35769. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/2067
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Title
Characterization of Inhibitory Anti-Duffy Binding Protein II Immunity: Approach to Plasmodium vivax Vaccine Development in Thailand
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Abstract
Plasmodium 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.
