Korean J Parasitol.
2016 Dec;54(6):725-732. 10.3347/kjp.2016.54.6.725.
Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81₉₅ in 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 230000, China.
- 3Yangzhou University School of Medicine, Yangzhou 225001, China.
- 4Laboratory of Pathogen Infection and Immunity, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu 214122, China.
- 5Department of Medical Research, Yangon 11191, Myanmar.
- 6Department of Molecular and Cellular Biochemistry, School of Medicine, Kangwon National University, Chuncheon 24341, Korea.
- 7Department of Internal Medicine, School of Medicine, Kangwon National University, Chuncheon 24341, Korea.
- 8Department of Physiology, School of Medicine, Kangwon National University, Chuncheon 24341, Korea.
- KMID: 2367413
- DOI: http://doi.org/10.3347/kjp.2016.54.6.725
Abstract
- Plasmodium vivax produces numerous caveola-vesicle complex (CVC) structures beneath the membrane of infected erythrocytes. Recently, a member helical interspersed subtelomeric (PHIST) superfamily protein, PcyPHIST/CVC-81₉₅, was identified as CVCs-associated protein in Plasmodium cynomolgi and essential for survival of this parasite. Very little information has been documented to date about PHIST/CVC-81₉₅ protein in P. vivax. In this study, the recombinant PvPHIST/CVC-81₉₅ N and C termini were expressed, and immunoreactivity was assessed using confirmed vivax malaria patients sera by protein microarray. The subcellular localization of PvPHIST/CVC-81₉₅ N and C termini in blood stage parasites was also determined. The antigenicity of recombinant PvPHIST/CVC-81₉₅ N and C terminal proteins were analyzed by using serum samples from the Republic of Korea. The results showed that immunoreactivities to these proteins had 61% and 43% sensitivity and 96.9% and 93.8% specificity, respectively. The N terminal of PvPHIST/CVC-81₉₅ which contains transmembrane domain and export motif (PEXEL; RxLxE/Q/D) produced CVCs location throughout the erythrocytic-stage parasites. However, no fluorescence was detected with antibodies against C terminal fragment of PvPHIST/CVC-81₉₅. These results suggest that the PvPHIST/CVC-81₉₅ is localized on the CVCs and may be immunogenic in natural infection of P. vivax.
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