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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/31929
Title: The plasmodium vivax merozoite surface protein 1 paralog is a novel erythrocyte-binding ligand of p. vivax
Authors: Yang Cheng
Yue Wang
Daisuke Ito
Deok Hoon Kong
Kwon Soo Ha
Jun Hu Chen
Feng Lu
Jian Li
Bo Wang
Eizo Takashim
Jetsumon Sattabongkot
Takafumi Tsuboi
Eun Taek Han
Kangwon National University
Ehime University
Mahidol University
Zhejiang Academy of Medical Sciences
Chinese Center for Disease Control and Prevention
Jiangsu Institute of Parasitic Diseases
Keywords: Immunology and Microbiology;Medicine
Issue Date: 1-May-2013
Citation: Infection and Immunity. Vol.81, No.5 (2013), 1585-1595
Abstract: Merozoite surface protein 1 of Plasmodium vivax (PvMSP1), a glycosylphosphatidylinositol-anchored protein (GPI-AP), is a malaria vaccine candidate for P. vivax. The paralog of PvMSP1, named P. vivax merozoite surface protein 1 paralog (PvMSP1P; PlasmoDB PVX_099975), was recently identified and predicted as a GPI-AP. The similarities in genetic structural characteristics between PvMSP1 and PvMSP1P (e.g., size of open reading frames, two epidermal growth factor-like domains, and GPI anchor motif in the C terminus) led us to study this protein. In the present study, different regions of the PvMSP1P protein, demarcated based on the processed forms of PvMSP1, were expressed successfully as recombinant proteins [i.e., 83 (A, B, and C), 30, 38, 42, 33, and 19 fragments]. We studied the naturally acquired immune response against each fragment of recombinant PvMSP1P and the potential ability of each fragment to bind erythrocytes. The N-terminal fragment (83A) and two C-terminal fragments (33 and 19) reacted strongly with sera from P. vivax-infected patients, with 50 to 68% sensitivity and 95 to 96% specificity, respectively. Due to colocalization of PvMSP1P with PvMSP1, we supposed that PvMSP1P plays a similar role as PvMSP1 during erythrocyte invasion. An in vitro cytoadherence assay showed that PvMSP1P, especially the 19-kDa C-terminal region, could bind to erythrocytes. We also found that human sera from populations naturally exposed to vivax malaria and antisera obtained by immunization using the recombinant molecule PvMSP1P-19 inhibited in vitro binding of human erythrocytes to PvMSP1P-19. These results provide further evidence that the PvMSP1P might be an essential parasite adhesion molecule in the P. vivax merozoite and is a potential vaccine candidate against P. vivax. © 2013, American Society for Microbiology.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84877818855&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/31929
ISSN: 10985522
00199567
Appears in Collections:Scopus 2011-2015

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