Publication: Immunoprofiling of the tryptophan-rich antigen family in Plasmodium vivax
Issued Date
2015-01-01
Resource Type
ISSN
10985522
00199567
00199567
Other identifier(s)
2-s2.0-84937802181
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Infection and Immunity. Vol.83, No.8 (2015), 3083-3095
Suggested Citation
Bo Wang, Feng Lu, Yang Cheng, Jun Hu Chen, Hye Yoon Jeon, Kwon Soo Ha, Jun Cao, Myat Htut Nyunt, Jin Hee Han, Seong Kyun Lee, Myat Phone Kyaw, Jetsumon Sattabongkot, Eizo Takashima, Takafumi Tsuboi, Eun Taek Han Immunoprofiling of the tryptophan-rich antigen family in Plasmodium vivax. Infection and Immunity. Vol.83, No.8 (2015), 3083-3095. doi:10.1128/IAI.03067-14 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/36176
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Immunoprofiling of the tryptophan-rich antigen family in Plasmodium vivax
Abstract
© 2015, American Society for Microbiology. Tryptophan-rich antigens (TRAgs) are an antigen family that has been identified in human and rodent malaria parasites. TRAgs have been proposed as candidate antigens for potential vaccines. The Plasmodium vivax TRAg (PvTRAg) family includes 36 members. Each PvTRAg contains a tryptophan-rich (TR) domain in the C-terminal region. In this study, we recombinantly expressed all 36 PvTRAgs using a cell-free expression system, and, for the first time, profiled the IgG antibody responses against all PvTRAgs in the sera from 96 vivax malaria patients and 40 healthy individuals using protein microarray technology. The mean seropositive rate for all PvTRAgs was 60.3%. Among them, nine PvTRAgs were newly identified in this study and showed a seropositive rate of >50%. Five of them, PvTRAg_13, PvTRAg_15, PvTRAg_16, PvTRAg_26, and PvTRAg_29, produced higher levels of IgG antibody, even in low-endemicity countries. In addition, the results of an immunofluorescence analysis suggest that PvTRAgs are, at least in part, associated with caveola-vesicle complexes, a unique structure of P. vivax-infected erythrocytes. The mechanism of formation and the function of these abundant membrane structures are not known. Further investigation aimed at determining the functions of these proteins would lead to a better understanding of the blood-stage biology of P. vivax.