Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/36176
Title: Immunoprofiling of the tryptophan-rich antigen family in Plasmodium vivax
Authors: 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
Kangwon National University
Anhui Medical University
Jiangsu Institute of Parasitic Diseases
National Institute of Allergy and Infectious Diseases
Department of Medical Research
Mahidol University
Ehime University
Chinese Center for Disease Control and Prevention
Keywords: Immunology and Microbiology
Issue Date: 1-Jan-2015
Citation: Infection and Immunity. Vol.83, No.8 (2015), 3083-3095
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84937802181&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/36176
ISSN: 10985522
00199567
Appears in Collections:Scopus 2011-2015

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.