Identification of Immunodominant B-cell Epitope Regions of Reticulocyte Binding Proteins in Plasmodium vivax by Protein Microarray Based Immunoscreening

The Korean Journal of Parasitology
Jin-Hee HanEun-Taek Han

Abstract

Plasmodium falciparum can invade all stages of red blood cells, while Plasmodium vivax can invade only reticulocytes. Although many P. vivax proteins have been discovered, their functions are largely unknown. Among them, P. vivax reticulocyte binding proteins (PvRBP1 and PvRBP2) recognize and bind to reticulocytes. Both proteins possess a C-terminal hydrophobic transmembrane domain, which drives adhesion to reticulocytes. PvRBP1 and PvRBP2 are large (> 326 kDa), which hinders identification of the functional domains. In this study, the complete genome information of the P. vivax RBP family was thoroughly analyzed using a prediction server with bioinformatics data to predict B-cell epitope domains. Eleven pvrbp family genes that included 2 pseudogenes and 9 full or partial length genes were selected and used to express recombinant proteins in a wheat germ cell-free system. The expressed proteins were used to evaluate the humoral immune response with vivax malaria patients and healthy individual serum samples by protein microarray. The recombinant fragments of 9 PvRBP proteins were successfully expressed; the soluble proteins ranged in molecular weight from 16 to 34 kDa. Evaluation of the humoral immune response to each recombina...Continue Reading

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Dec 3, 2016·International Journal for Parasitology·Wai-Hong ThamJulian C Rayner
Aug 31, 2019·Cellular Microbiology·Li-Jin ChanWai-Hong Tham
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Jun 28, 2020·Veterinary Medicine and Science·Negar HooshmandNader Ghaleh Golab Behbahan
Dec 29, 2020·PLoS Neglected Tropical Diseases·Pyo Yun ChoTong-Soo Kim

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Methods Mentioned

BETA
protein array

Software Mentioned

BepiPred
BcePred
GraphPad Prism
ABCpred
Protean
Excel

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