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• W2088898846 startingPage "2576" @default.
• W2088898846 abstract "ABSTRACT We describe here an ∼40-kDa Plasmodium vivax tryptophan-rich antigen (PvTRAg40) which contains 321 amino acids and 11.4% tryptophan residues. This protein shows 65% homology (35% identity) with the previously described PvTRAg, besides sharing 23 of 27 positionally conserved tryptophan residues and similar genomic organization. The nucleotide sequence of the entire tryptophan-rich domain of PvTRAg40 was identical among 35 P. vivax clinical isolates. The protein is expressed by ring, trophozoite, and schizont stages of the parasite. The cDNA covering exon 2 of PvTRAg40 was cloned and expressed in the pPROEXHTa vector, and recombinant protein was purified. A high humoral immune response (90.7% seropositivity; n = 43) against this recombinant protein was detected in humans during the course of natural P. vivax infection. Eighty percent of the total of 20 P. vivax -exposed individuals exhibited lymphoproliferative responses against this antigen. The T cells of these individuals produced larger amounts of interleukin-12 (IL-12), IL-4, and IL-10 than gamma interferon and tumor necrosis factor alpha cytokines in response to the recombinant protein. Production of Th2-biased cytokines, conserved T- and B-cell epitopes, and an enhanced humoral immune response indicate that PvTRAg40 could possibly induce antibody-mediated immune protection against infection." @default.
• W2088898846 created "2016-06-24" @default.
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• W2088898846 date "2008-06-01" @default.
• W2088898846 modified "2023-10-07" @default.
• W2088898846 title "Expression, Purification, and Characterization of the Immunological Response to a 40-Kilodalton Plasmodium vivax Tryptophan-Rich Antigen" @default.
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• W2088898846 doi "https://doi.org/10.1128/iai.00677-07" @default.
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