An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 of Plasmodium vivax
A Study of Its Antigenicity and Immunogenicity
Bibliographic Data
| ID | 22069718 |
|---|---|
| Authors | Liping Fan (0009-0008-8433-3123, Anhui Medical University), Jinxing Xia (0000-0002-1559-0205, First Affiliated Hospital of Anhui Medical University), Jilong Shen (0000-0002-4755-3687, Anhui Medical University), Qiang Fang (0000-0002-0715-2184, Bengbu Medical College), Hui Xia (0009-0004-5941-5427, Bengbu Medical College), Meijuan Zheng (0000-0002-7378-3355, Anhui Medical University), Jin-Hee Han (Kangwon National University), Eun‐Taek Han (0000-0003-1962-7199, Kangwon National University), Eun-Taek Han, Bo Wang (0000-0002-0290-2134, Anhui Medical University, corresponding author), Yuanhong Xu (0000-0003-1549-9820, First Affiliated Hospital of Anhui Medical University, corresponding author) |
| Year | 2020 |
| Volume | 8 |
| Pages | 148-148 |
| Publication date | 2020-04-28 |
| Peer Reviewed | Yes |
| Open Access | Yes |
| Type | ARTICLE |
| Venue | Frontiers in Public Health (JOURNAL) |
| Journal identifiers | ISSN: 2296-2565 • E-ISSN: 2296-2565 |
| Publisher | Frontiers Media SA (PUBLISHER • CH) |
| DOI | 10.3389/fpubh.2020.00148 |
| PMID | 32411650 |
| OpenAlex | W3023594329 |
| Language | EN |
| References cited | 62 |
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
Antibody · Antigen · Antigenicity · Biology · Immune system · Immunogenicity · Immunoglobulin G · Malaria · Plasmodium falciparum · Plasmodium vivax · HIV Research and Treatment · Malaria Research and Control · Trypanosoma species research and implications · Immunology · Virology
| Citation velocity | historical |
|---|---|
| Highly cited | No |