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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Frontiers Media S.A.,
2020-04-01T00:00:00Z.
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LEADER | 00000 am a22000003u 4500 | ||
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001 | doaj_ef2b7cd02faa4aaea176b7de4156d7d0 | ||
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. |