Publication: Characterization of Pv92, a novel merozoite surface protein of Plasmodium vivax
Issued Date
2016-08-01
Resource Type
ISSN
17380006
00234001
00234001
Other identifier(s)
2-s2.0-84986880039
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Korean Journal of Parasitology. Vol.54, No.4 (2016), 385-391
Suggested Citation
Seong Kyun Lee, Bo Wang, Jin Hee Han, Myat Htut Nyunt, Fauzi Muh, Patchanee Chootong, Kwon Soo Ha, Won Sun Park, Seok Ho Hong, Jeong Hyun Park, Eun Taek Han Characterization of Pv92, a novel merozoite surface protein of Plasmodium vivax. Korean Journal of Parasitology. Vol.54, No.4 (2016), 385-391. doi:10.3347/kjp.2016.54.4.385 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/40764
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Characterization of Pv92, a novel merozoite surface protein of Plasmodium vivax
Other Contributor(s)
Abstract
© 2016, Korean Society for Parasitology and Tropical Medicine. 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.