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Published on: June 10, 2015
Characterization of Plasmodium vivax Early Transcribed Membrane Protein 11.2 and Exported Protein 1
Yang Cheng1, Feng Lu2, Seong-Kyun Lee3
1Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University, Chuncheon, Gangwon-do, Republic of Korea; Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Rockville, Maryland, United States of America.
Abstract:
In Plasmodium, the membrane of intracellular parasites is initially formed during invasion as an invagination of the red blood cell surface, which forms a barrier between the parasite and infected red blood cells in asexual blood stage parasites. The membrane proteins of intracellular parasites of Plasmodium species have been identified such as early-transcribed membrane proteins (ETRAMPs) and exported proteins (EXPs). However, there is little or no information regarding the intracellular parasite membrane in Plasmodium vivax. In the present study, recombinant PvETRAMP11.2 (PVX_003565) and PvEXP1 (PVX_091700) were expressed and evaluated antigenicity tests using sera from P. vivax-infected patients. A large proportion of infected individuals presented with IgG antibody responses against PvETRAMP11.2 (76.8%) and PvEXP1 (69.6%). Both of the recombinant proteins elicited high antibody titers capable of recognizing parasites of vivax malaria patients. PvETRAMP11.2 partially co-localized with PvEXP1 on the intracellular membranes of immature schizont. Moreover, they were also detected at the apical organelles of newly formed merozoites of mature schizont. We first proposed that these proteins might be synthesized in the preceding schizont stage, localized on the parasite membranes and apical organelles of infected erythrocytes, and induced high IgG antibody responses in patients.
Insights
Researchers identified key membrane proteins, PvETRAMP11.2 and PvEXP1, in Plasmodium vivax malaria parasites. These proteins trigger significant IgG antibody responses in infected individuals, suggesting their potential role in malaria diagnosis and vaccine development.
Area of Science:
- Malariology
- Parasitology
- Immunology
Background:
- Intracellular parasites in Plasmodium form a membrane during red blood cell invasion.
- Early-transcribed membrane proteins (ETRAMPs) and exported proteins (EXPs) are known membrane proteins in Plasmodium species.
- Limited information exists on intracellular parasite membranes in Plasmodium vivax.
Purpose of the Study:
- To investigate the antigenicity of recombinant PvETRAMP11.2 and PvEXP1 in Plasmodium vivax.
- To explore the localization and potential function of these proteins within the parasite.
Main Methods:
- Recombinant expression of PvETRAMP11.2 and PvEXP1.
- Antigenicity testing using sera from Plasmodium vivax-infected patients.
- Immunofluorescence assays to determine protein co-localization and localization within merozoites.
Main Results:
- High IgG antibody responses were observed against PvETRAMP11.2 (76.8%) and PvEXP1 (69.6%) in infected individuals.
- Both proteins elicited high antibody titers recognizing Plasmodium vivax parasites.
- PvETRAMP11.2 and PvEXP1 were found to co-localize on intracellular membranes of immature schizonts and apical organelles of merozoites.
Conclusions:
- PvETRAMP11.2 and PvEXP1 are synthesized in schizonts and localize to parasite membranes and merozoite apical organelles.
- These proteins induce significant IgG antibody responses in Plasmodium vivax-infected patients.
- The findings suggest potential roles for PvETRAMP11.2 and PvEXP1 in malaria pathogenesis and as diagnostic or vaccine targets.
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