Korean J Parasitol.
2016 Aug;54(4):385-391. 10.3347/kjp.2016.54.4.385.
Characterization of Pv92, a Novel Merozoite Surface Protein of Plasmodium vivax
- Affiliations
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- 1Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University, Chuncheon 24341, Korea. ethan@kangwon.ac.kr
- 2Department of Clinical Laboratory, The First Affiliated Hospital of Anhui Medical University, Hefei, Anhui, People's Republic of China.
- 3Department of Clinical Microbiology and Applied Technology, Mahidol University, Bangkok, Thailand.
- 4Department of Molecular and Cellular Biochemistry, School of Medicine, Kangwon National University, Chuncheon 24341, Korea.
- 5Department of Physiology, School of Medicine, Kangwon National University, Chuncheon 24341, Korea.
- 6Department of Internal Medicine, School of Medicine, Kangwon National University, Chuncheon 24341, Korea.
- 7Department of Anatomy, School of Medicine, Kangwon National University, Chuncheon 24341, Korea.
- KMID: 2353566
- DOI: http://doi.org/10.3347/kjp.2016.54.4.385
Abstract
- The discovery and understanding of antigenic proteins are essential for development of a vaccine against malaria. In Plasmodium falciparum, Pf92 have been characterized as a merozoite surface protein, and this protein is expressed at the late schizont stage, but no study of Pv92, the orthologue of Pf92 in P. vivax, has been reported. Thus, the protein structure of Pv92 was analyzed, and the gene sequence was aligned with that of other Plasmodium spp. using bioinformatics tools. The recombinant Pv92 protein was expressed and purified using bacterial expression system and used for immunization of mice to gain the polyclonal antibody and for evaluation of antigenicity by protein array. Also, the antibody against Pv92 was used for subcellular analysis by immunofluorescence assay. The Pv92 protein has a signal peptide and a sexual stage s48/45 domain, and the cysteine residues at the N-terminal of Pv92 were completely conserved. The N-terminal of Pv92 was successfully expressed as soluble form using a bacterial expression system. The antibody raised against Pv92 recognized the parasites and completely merged with PvMSP1-19, indicating that Pv92 was localized on the merozoite surface. Evaluation of the human humoral immune response to Pv92 indicated moderate antigenicity, with 65% sensitivity and 95% specificity by protein array. Taken together, the merozoite surface localization and antigenicity of Pv92 implicate that it might be involved in attachment and invasion of a merozoite to a new host cell or immune evasion during invasion process.
MeSH Terms
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Animals
Computational Biology
Cysteine
Fluorescent Antibody Technique
Humans
Immune Evasion
Immunity, Humoral
Immunization
Malaria
Merozoites*
Mice
Parasites
Plasmodium falciparum
Plasmodium vivax*
Plasmodium*
Protein Array Analysis
Protein Sorting Signals
Schizonts
Sensitivity and Specificity
Cysteine
Protein Sorting Signals
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