Identification and characterization of Pv50, a novel Plasmodium vivax merozoite surface protein.
Adolescent
Adult
Animals
Antibodies, Protozoan
/ blood
Blotting, Western
Cytokines
/ blood
Female
Humans
Immunity, Humoral
Lymphocyte Count
Malaria, Vivax
/ immunology
Merozoite Surface Protein 1
/ immunology
Merozoites
/ chemistry
Mice
Mice, Inbred BALB C
Plasmodium
/ chemistry
Plasmodium vivax
/ chemistry
Protein Binding
Protozoan Proteins
/ genetics
Recombinant Proteins
/ genetics
T-Lymphocytes
/ immunology
Young Adult
Antigenicity
Immunogenicity
Merozoite surface protein
Plasmodium vivax
Protein interaction
Pv50
Journal
Parasites & vectors
ISSN: 1756-3305
Titre abrégé: Parasit Vectors
Pays: England
ID NLM: 101462774
Informations de publication
Date de publication:
18 Apr 2019
18 Apr 2019
Historique:
received:
04
01
2019
accepted:
04
04
2019
entrez:
20
4
2019
pubmed:
20
4
2019
medline:
14
6
2019
Statut:
epublish
Résumé
Plasmodium vivax contains approximately 5400 coding genes, more than 40% of which code for hypothetical proteins that have not been functionally characterized. In a previous preliminary screening using pooled serum samples, numerous hypothetical proteins were selected from among those that were highly transcribed in the schizont-stage of parasites, and highly antigenic P. vivax candidates including hypothetical proteins were identified. However, their immunological and functional activities in P. vivax remain unclear. From these candidates, we investigated a P. vivax 50-kDa protein (Pv50, PVX_087140) containing a highly conserved signal peptide that shows high transcription levels in blood-stage parasites. Recombinant Pv50 was expressed in a cell-free expression system and used for IgG prevalence analysis of patients with vivax malaria and healthy individuals. Immune responses were analyzed in immunized mice and mouse antibodies were used to detect the subcellular localization of the protein in blood-stage parasites by immunofluorescence assay. A protein array method was used to evaluate protein-protein interactions to predict protein functional activities during the invasion of parasites into erythrocytes. Recombinant Pv50 showed IgG prevalence in patient samples with a sensitivity of 42.9% and specificity of 93.8% compared to that in healthy individuals. The non-cytophilic antibodies IgG1 and IgG3 were the major components involved in the antibody response in Pv50-immunized mice. Pv50 localized on the surface of merozoites and a specific interaction between Pv50 and PvMSP1 was detected, suggesting that Pv50-PvMSP1 forms a heterodimeric complex in P. vivax. Increased immune responses caused by native P. vivax parasites were detected, confirming its immunogenic effects. This study provides a method for detecting new malaria antigens, and Pv50 may be a vivax malaria vaccine candidate with PvMSP1.
Sections du résumé
BACKGROUND
BACKGROUND
Plasmodium vivax contains approximately 5400 coding genes, more than 40% of which code for hypothetical proteins that have not been functionally characterized. In a previous preliminary screening using pooled serum samples, numerous hypothetical proteins were selected from among those that were highly transcribed in the schizont-stage of parasites, and highly antigenic P. vivax candidates including hypothetical proteins were identified. However, their immunological and functional activities in P. vivax remain unclear. From these candidates, we investigated a P. vivax 50-kDa protein (Pv50, PVX_087140) containing a highly conserved signal peptide that shows high transcription levels in blood-stage parasites.
RESULTS
RESULTS
Recombinant Pv50 was expressed in a cell-free expression system and used for IgG prevalence analysis of patients with vivax malaria and healthy individuals. Immune responses were analyzed in immunized mice and mouse antibodies were used to detect the subcellular localization of the protein in blood-stage parasites by immunofluorescence assay. A protein array method was used to evaluate protein-protein interactions to predict protein functional activities during the invasion of parasites into erythrocytes. Recombinant Pv50 showed IgG prevalence in patient samples with a sensitivity of 42.9% and specificity of 93.8% compared to that in healthy individuals. The non-cytophilic antibodies IgG1 and IgG3 were the major components involved in the antibody response in Pv50-immunized mice. Pv50 localized on the surface of merozoites and a specific interaction between Pv50 and PvMSP1 was detected, suggesting that Pv50-PvMSP1 forms a heterodimeric complex in P. vivax.
CONCLUSIONS
CONCLUSIONS
Increased immune responses caused by native P. vivax parasites were detected, confirming its immunogenic effects. This study provides a method for detecting new malaria antigens, and Pv50 may be a vivax malaria vaccine candidate with PvMSP1.
Identifiants
pubmed: 30999945
doi: 10.1186/s13071-019-3434-7
pii: 10.1186/s13071-019-3434-7
pmc: PMC6474066
doi:
Substances chimiques
Antibodies, Protozoan
0
Cytokines
0
Merozoite Surface Protein 1
0
Protozoan Proteins
0
Recombinant Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
176Subventions
Organisme : National Natural Science Foundation of China
ID : 81601787
Organisme : National Natural Science Foundation of China
ID : 81871681
Organisme : Natural Science Foundation of Jiangsu Province
ID : BK20160192
Organisme : national first-class discipline program of Food Science and Technology
ID : JUFSTR20180101
Organisme : National Research Foundation of Korea
ID : MSIP
Organisme : National Research Foundation of Korea
ID : NRF-2017R1A2A2A05069562
Organisme : Basic Science Research Program through the National NRF
ID : 2015R1A4A1038666
Organisme : Society of the Friendly Sons of St. Patrick for the Relief of Emigrants from Ireland (US)
ID : 520170449
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