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Plasmodium vivax: immunological properties of tryptophan-rich antigens PvTRAg 35.2 and PvTRAg 80.6
Authors:Pooja Mittra  Neeru Singh  Yagya D. Sharma
Affiliation:1. BioService, Malaria Research and Reference Reagent Resource Center (MR4), American Type Culture Collection (ATCC), Manassas, VA 20110-2209, USA;2. Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20852, USA;3. Malaria Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), Aruna Asaf Ali Marg, New Delhi, India;1. Material Science Research Laboratory, Department of Physics, University of Lucknow, Lucknow 226 007, India;2. Department of Physics, BBD University, Lucknow 227 015, India
Abstract:Need for malaria vaccine necessitates the characterization of potential antigens of the Plasmodium parasite. Recently, we have identified several Plasmodium vivax tryptophan-rich antigens (PvTRAgs). Here, we describe the immunological characterization of hitherto undescribed two such antigens PvTRAg 35.2 and PvTRAg 80.6 which are respective homologue of Plasmodium falciparum merozoite associated tryptophan-rich antigen (PfMaTrA) and P. falciparum tryptophan and threonine rich antigen (PfTryThrA) involved in erythrocyte invasion. Each of the pvtrag genes is comprised of two exons where exon 2 encodes for major part of the protein. PvTRAg 35.2 and PvTRAg 80.6 showed 97.06% and 94.12% (n = 34) seropositivity rates, and 92.3% (n = 13) and 100% (n = 29) lymphoproliferative responses, respectively, among P. vivax exposed individuals. Geometric mean values of IL-12, IFN-γ, TNF-α, IL-4 and IL-10 in PBMC culture supernatants of P. vivax exposed individuals were 182.02, 60.3, 62.84, 196.01 and 177.17 pg/ml against PvTRAg 35.2 and 185.27, 58.15, 64.56, 142.01 and 157.2 pg/ml against PvTRAg 80.6 showing mixed immune response with distinct biased towards anti-inflammatory Th2 phenotype. The pvtrag 35.2 gene was highly conserved in the parasite population whereas pvtrag 80.6 showed minor variations in the N-terminal region but highly conserved in the C-terminal region containing tryptophan-rich domain.
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