Abstract
Plasmodium vivax is most common but non-cultivable human malaria parasite which is poorly characterized at the molecular level. Here, we describe the identification and characterization of a
P. vivax Tryptophan-Rich Antigen (PvTRAg) which contains unusually high (8.28%) tryptophan residues and is expressed by all blood stages of the parasite. The
pvtrag gene comprises a 978
bp open reading frame interrupted by two introns. The first intron is located in the 5′-untranslated region while the second one is positioned 174
bp downstream to the ATG codon. The encoded ∼40
kDa protein contains a transmembrane domain near the N-terminus followed by a tryptophan-rich domain with significantly high surface probability and antigenic index. It is localized in the parasite cytoplasm as well as in the cytoplasm of the parasitized erythrocyte. The purified
E. coli expressed recombinant PvTRAg protein showed a very high seropositivity rate for the presence of antibodies amongst the
P. vivax patients, indicating that the antigen generates significant humoral immune response during the natural course of
P. vivax infection. Analysis of various field isolates revealed that the tryptophan-rich domain is highly conserved except for three-point mutations. The PvTRAg could be a potential vaccine candidate since similar tryptophan-rich antigens of
P. yoelii have shown protection against malaria in murine model.