An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and Immunogenicity

Background:Plasmodium tryptophan-rich (TR) proteins have been proposed as potential vaccine candidate antigens. Among them, P. vivax tryptophan-rich antigens (PvTR-Ags), which have positionally conserved tryptophan residues in a TR domain, are highly antigenic in humans. Several of these antigens, i...

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Main Authors: Liping Fan (Author), Jinxing Xia (Author), Jilong Shen (Author), Qiang Fang (Author), Hui Xia (Author), Meijuan Zheng (Author), Jin-Hee Han (Author), Eun-Taek Han (Author), Bo Wang (Author), Yuanhong Xu (Author)
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Published: Frontiers Media S.A., 2020-04-01T00:00:00Z.
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042 |a dc 
100 1 0 |a Liping Fan  |e author 
700 1 0 |a Jinxing Xia  |e author 
700 1 0 |a Jilong Shen  |e author 
700 1 0 |a Qiang Fang  |e author 
700 1 0 |a Qiang Fang  |e author 
700 1 0 |a Hui Xia  |e author 
700 1 0 |a Hui Xia  |e author 
700 1 0 |a Meijuan Zheng  |e author 
700 1 0 |a Jin-Hee Han  |e author 
700 1 0 |a Eun-Taek Han  |e author 
700 1 0 |a Bo Wang  |e author 
700 1 0 |a Yuanhong Xu  |e author 
245 0 0 |a An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and Immunogenicity 
260 |b Frontiers Media S.A.,   |c 2020-04-01T00:00:00Z. 
500 |a 2296-2565 
500 |a 10.3389/fpubh.2020.00148 
520 |a Background:Plasmodium tryptophan-rich (TR) proteins have been proposed as potential vaccine candidate antigens. Among them, P. vivax tryptophan-rich antigens (PvTR-Ags), which have positionally conserved tryptophan residues in a TR domain, are highly antigenic in humans. Several of these antigens, including PvTRAg-26, have exhibited erythrocyte-binding activities.Methods: Subclasses of IgG antibodies against PvTRAg-26 were detected by enzyme-linked immunosorbent assay in 35 P. vivax infected patients and mice immunized with the recombinant antigen to characterize its antigenicity and immunogenicity. Moreover, the antigen-specific immune responses and Th1/Th2-type cytokine patterns of splenocytes from the immunized animals were determined in vitro. The subcellular localization of PvTRAg-26 in ring-stage parasites was also detected by indirect immunofluorescence assay.Results: The IgG1 and IgG3 levels in P. vivax-infected patients were significantly higher than those in uninfected individuals. In the PvTRAg-26-immunized mice, elevated levels of antigen-specific IgG antibodies were observed, dominated by the IgG1 subclass, and Th1-type cytokines were remarkably increased compared with Th2-type cytokines. Additionally, the subcellular location of the PvTRAg-26 protein was closely associated with the caveola-vesicle complex on the infected-erythrocyte membrane in the early ring stage of P. vivax.Conclusions: PvTRAg-26, a P. vivax TR antigen, with high antigenicity and immunogenicity, induces Th1-cytokine response and increases production of IgG1 antibodies. This immune profiling study provided a substantial evidence that PvTRAg-26 may be a potential candidate for P. vivax vaccine development. 
546 |a EN 
690 |a malaria 
690 |a Plasmodium vivax 
690 |a tryptophan-rich antigens 
690 |a immunogenicity 
690 |a vaccine candidate 
690 |a Public aspects of medicine 
690 |a RA1-1270 
655 7 |a article  |2 local 
786 0 |n Frontiers in Public Health, Vol 8 (2020) 
787 0 |n https://www.frontiersin.org/article/10.3389/fpubh.2020.00148/full 
787 0 |n https://doaj.org/toc/2296-2565 
856 4 1 |u https://doaj.org/article/ef2b7cd02faa4aaea176b7de4156d7d0  |z Connect to this object online.