Publication: The association of Duffy binding protein region II polymorphisms and its antigenicity in Plasmodium vivax isolates from Thailand.
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Accepted Date
2014-07-28
Issued Date
2014-08-07
Copyright Date
2014
Resource Type
Language
eng
ISSN
1383-5769 (printed)
1873-0329 (electronic)
1873-0329 (electronic)
Rights
Mahidol University
Rights Holder(s)
Elsevier Science
Bibliographic Citation
Chootong P, McHenry AM, Ntumngia FB, Sattabongkot J, Adams JH. The association of Duffy binding protein region II polymorphisms and its antigenicity in Plasmodium vivax isolates from Thailand. Parasitol Int. 2014 Dec;63(6):858-64.
Suggested Citation
Patchanee Chootong, พัชนี ชูทอง, McHenry, Amy M., Ntumngia, Francis B., Jetsumon Sattabongkot, เจตสุมน สัตตบงกช, Adams, John H. The association of Duffy binding protein region II polymorphisms and its antigenicity in Plasmodium vivax isolates from Thailand.. Chootong P, McHenry AM, Ntumngia FB, Sattabongkot J, Adams JH. The association of Duffy binding protein region II polymorphisms and its antigenicity in Plasmodium vivax isolates from Thailand. Parasitol Int. 2014 Dec;63(6):858-64.. doi:10.1016/j.parint.2014.07.014. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/865
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Title
The association of Duffy binding protein region II polymorphisms and its antigenicity in Plasmodium vivax isolates from Thailand.
Corresponding Author(s)
Abstract
Plasmodium vivax Duffy binding protein II (DBPII) plays an important role in
reticulocyte invasion and is a potential vaccine candidate against vivax malaria.
However, polymorphisms in DBPII are a challenge for the successful design of a
broadly protective vaccine. In this study, the genetic diversity of DBPII among
Thai isolates was analyzed from Plasmodium vivax-infected blood samples and
polymorphism characters were defined with the MEGA4 program. Sequence analysis
identified 12 variant residues that are common among Thai DBPII haplotypes with
variant residues L333F, L424I, W437R and I503K having the highest frequency.
Variant residue D384K occurs in combination with either E385K or K386N/Q.
Additionally, variant residue L424I occurs in conjunction with W437R in most Thai
DBPII alleles and these variants frequently occur in combination with the I503K
variant. The polymorphic patterns of Thai isolates were defined into 9 haplotypes
(Thai DBL-1, -2, -3, etc.…). Thai DBL-2, -5, -6 haplotypes are the most common
DBPII variants in Thai residents. To study the association of these Thai DBPII
polymorphisms with antigenic character, the functional inhibition of anti-DBPII
monoclonal antibodies against a panel of Thai DBL variants was characterized by
an in vitro erythrocyte binding inhibition assay. The functional inhibition of
anti-DBPII monoclonal antibodies 3C9, 2D10 and 2C6 against Thai variants was
significantly different, suggesting that polymorphisms of Thai DBPII variants
alter the antigenic character of the target epitopes. In contrast, anti-DBPII
monoclonal antibody 2H2 inhibited all Thai DBPII variants equally well. Our
results suggest that the immune efficacy of a DBPII vaccine will depend on the
specificity of the anti-DBPII antibodies induced and that it is preferable to
optimize responses to conserved epitopes for broadly neutralizing protection
against P. vivax.