Parasites, Hosts and Diseases

  • 제54권6호
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  • Pages.725-732
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  • 2016
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  • 2982-5164(pISSN)
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  • 1738-0006(eISSN)
대한기생충학·열대의학회 (The Korea Society for Parasitology and Tropical Medicine)
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Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-8195 in Plasmodium vivax

  • Wang, Bo (Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University) ;
  • Lu, Feng (Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University) ;
  • Han, Jin-Hee (Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University) ;
  • Lee, Seong-Kyun (Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University) ;
  • Cheng, Yang (Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University) ;
  • Nyunt, Myat Htut (Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University) ;
  • Ha, Kwon-Soo (Department of Molecular and Cellular Biochemistry, School of Medicine, Kangwon National University) ;
  • Hong, Seok-Ho (Department of Internal Medicine, School of Medicine, Kangwon National University) ;
  • Park, Won Sun (Department of Physiology, School of Medicine, Kangwon National University) ;
  • Han, Eun-Taek (Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University)
  • 투고 : 2016.08.23
  • 심사 : 2016.11.29
  • 발행 : 2016.12.31
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초록

Plasmodium vivax produces numerous caveola-vesicle complex (CVC) structures beneath the membrane of infected erythrocytes. Recently, a member helical interspersed subtelomeric (PHIST) superfamily protein, $PcyPHIST/CVC-81_{95}$, 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 $PHIST/CVC-81_{95}$ protein in P. vivax. In this study, the recombinant $PvPHIST/CVC-81_{95}$ N and C termini were expressed, and immunoreactivity was assessed using confirmed vivax malaria patients sera by protein microarray. The subcellular localization of $PvPHIST/CVC-81_{95}$ N and C termini in blood stage parasites was also determined. The antigenicity of recombinant $PvPHIST/CVC-81_{95}$ 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 $PvPHIST/CVC-81_{95}$ 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 $PvPHIST/CVC-81_{95}$. These results suggest that the $PvPHIST/CVC-81_{95}$ is localized on the CVCs and may be immunogenic in natural infection of P. vivax.

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피인용 문헌

  1. Molecular characterization of Plasmodium falciparum PHISTb proteins as potential targets of naturally-acquired immunity against malaria vol.5, pp.None, 2016, https://doi.org/10.12688/wellcomeopenres.15919.2
  2. Familial Hyperckemia and Calf Hypertrophy Secondary to a Caveolin-3 Mutation vol.100, pp.7, 2021, https://doi.org/10.1097/phm.0000000000001604