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Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81(95) in Plasmodium vivax
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 esse...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Korean Society for Parasitology and Tropical Medicine
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5266361/ https://www.ncbi.nlm.nih.gov/pubmed/28095657 http://dx.doi.org/10.3347/kjp.2016.54.6.725 |
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author | Wang, Bo Lu, Feng Han, Jin-Hee Lee, Seong-Kyun Cheng, Yang Nyunt, Myat Htut Ha, Kwon-Soo Hong, Seok-Ho Park, Won Sun Han, Eun-Taek |
author_facet | Wang, Bo Lu, Feng Han, Jin-Hee Lee, Seong-Kyun Cheng, Yang Nyunt, Myat Htut Ha, Kwon-Soo Hong, Seok-Ho Park, Won Sun Han, Eun-Taek |
author_sort | Wang, Bo |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5266361 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The Korean Society for Parasitology and Tropical Medicine |
record_format | MEDLINE/PubMed |
spelling | pubmed-52663612017-01-26 Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81(95) in Plasmodium vivax Wang, Bo Lu, Feng Han, Jin-Hee Lee, Seong-Kyun Cheng, Yang Nyunt, Myat Htut Ha, Kwon-Soo Hong, Seok-Ho Park, Won Sun Han, Eun-Taek Korean J Parasitol Original Article 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. The Korean Society for Parasitology and Tropical Medicine 2016-12 2016-12-31 /pmc/articles/PMC5266361/ /pubmed/28095657 http://dx.doi.org/10.3347/kjp.2016.54.6.725 Text en Copyright © 2016 by The Korean Society for Parasitology and Tropical Medicine This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Article Wang, Bo Lu, Feng Han, Jin-Hee Lee, Seong-Kyun Cheng, Yang Nyunt, Myat Htut Ha, Kwon-Soo Hong, Seok-Ho Park, Won Sun Han, Eun-Taek Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81(95) in Plasmodium vivax |
title | Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81(95) in Plasmodium vivax |
title_full | Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81(95) in Plasmodium vivax |
title_fullStr | Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81(95) in Plasmodium vivax |
title_full_unstemmed | Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81(95) in Plasmodium vivax |
title_short | Characterization of Caveola-Vesicle Complexes (CVCs) Protein, PHIST/CVC-81(95) in Plasmodium vivax |
title_sort | characterization of caveola-vesicle complexes (cvcs) protein, phist/cvc-81(95) in plasmodium vivax |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5266361/ https://www.ncbi.nlm.nih.gov/pubmed/28095657 http://dx.doi.org/10.3347/kjp.2016.54.6.725 |
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