Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81₉₅ in Plasmodium vivax.
10.3347/kjp.2016.54.6.725
- Author:
Bo WANG
1
;
Feng LU
;
Jin Hee HAN
;
Seong Kyun LEE
;
Yang CHENG
;
Myat Htut NYUNT
;
Kwon Soo HA
;
Seok Ho HONG
;
Won Sun PARK
;
Eun Taek HAN
Author Information
1. Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University, Chuncheon, 24341, Korea. ethan@kangwon.ac.kr
- Publication Type:Original Article
- Keywords:
Plasmodium vivax;
PvPHIST/CVC-81₉₅;
caveola-vesicle complex;
immunoreactivity
- MeSH:
Antibodies;
Erythrocytes;
Fluorescence;
Humans;
Malaria, Vivax;
Membranes;
Parasites;
Plasmodium cynomolgi;
Plasmodium vivax*;
Plasmodium*;
Protein Array Analysis;
Republic of Korea;
Sensitivity and Specificity
- From:The Korean Journal of Parasitology
2016;54(6):725-732
- CountryRepublic of Korea
- Language:English
-
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.
