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, Jinxing Xia, Jilong Shen, Qiang Fang, Hui Xia, Meijuan Zheng, Jin-Hee Han, Eun-Taek Han, Bo Wang, Yuanhong Xu
Format: Article
Language:English
Published: Frontiers Media S.A. 2020-04-01
Series:Frontiers in Public Health
Subjects:
Online Access:https://www.frontiersin.org/article/10.3389/fpubh.2020.00148/full
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spelling doaj-ef2b7cd02faa4aaea176b7de4156d7d02020-11-25T02:54:24ZengFrontiers Media S.A.Frontiers in Public Health2296-25652020-04-01810.3389/fpubh.2020.00148517159An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and ImmunogenicityLiping Fan0Jinxing Xia1Jilong Shen2Qiang Fang3Qiang Fang4Hui Xia5Hui Xia6Meijuan Zheng7Jin-Hee Han8Eun-Taek Han9Bo Wang10Yuanhong Xu11Department of Clinical Laboratory, the First Affiliated Hospital of Anhui Medical University, Anhui, ChinaDepartment of Clinical Laboratory, the First Affiliated Hospital of Anhui Medical University, Anhui, ChinaThe Key Laboratories of Parasitology and Zoonoses Anhui and Department of Parasitology, Anhui Medical University, Anhui, ChinaDepartment of Microbiology and Parasitology, Bengbu Medical College, Anhui, ChinaAnhui Key Laboratory of Infection and Immunity, Bengbu Medical College, Bengbu, ChinaDepartment of Microbiology and Parasitology, Bengbu Medical College, Anhui, ChinaAnhui Key Laboratory of Infection and Immunity, Bengbu Medical College, Bengbu, ChinaDepartment of Clinical Laboratory, the First Affiliated Hospital of Anhui Medical University, Anhui, ChinaDepartment of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University, Chuncheon, South KoreaDepartment of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University, Chuncheon, South KoreaDepartment of Clinical Laboratory, the First Affiliated Hospital of Anhui Medical University, Anhui, ChinaDepartment of Clinical Laboratory, the First Affiliated Hospital of Anhui Medical University, Anhui, ChinaBackground: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.https://www.frontiersin.org/article/10.3389/fpubh.2020.00148/fullmalariaPlasmodium vivaxtryptophan-rich antigensimmunogenicityvaccine candidate
collection DOAJ
language English
format Article
sources DOAJ
author Liping Fan
Jinxing Xia
Jilong Shen
Qiang Fang
Qiang Fang
Hui Xia
Hui Xia
Meijuan Zheng
Jin-Hee Han
Eun-Taek Han
Bo Wang
Yuanhong Xu
spellingShingle Liping Fan
Jinxing Xia
Jilong Shen
Qiang Fang
Qiang Fang
Hui Xia
Hui Xia
Meijuan Zheng
Jin-Hee Han
Eun-Taek Han
Bo Wang
Yuanhong Xu
An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and Immunogenicity
Frontiers in Public Health
malaria
Plasmodium vivax
tryptophan-rich antigens
immunogenicity
vaccine candidate
author_facet Liping Fan
Jinxing Xia
Jilong Shen
Qiang Fang
Qiang Fang
Hui Xia
Hui Xia
Meijuan Zheng
Jin-Hee Han
Eun-Taek Han
Bo Wang
Yuanhong Xu
author_sort Liping Fan
title An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and Immunogenicity
title_short An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and Immunogenicity
title_full An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and Immunogenicity
title_fullStr An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and Immunogenicity
title_full_unstemmed An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax: A Study of Its Antigenicity and Immunogenicity
title_sort erythrocyte membrane-associated antigen, pvtrag-26 of plasmodium vivax: a study of its antigenicity and immunogenicity
publisher Frontiers Media S.A.
series Frontiers in Public Health
issn 2296-2565
publishDate 2020-04-01
description 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.
topic malaria
Plasmodium vivax
tryptophan-rich antigens
immunogenicity
vaccine candidate
url https://www.frontiersin.org/article/10.3389/fpubh.2020.00148/full
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