Presence of Memory T Cells and Naturally Acquired Antibodies in Plasmodium vivax Malaria-Exposed Individuals Against a Group of Tryptophan-Rich Antigens With Conserved Sequences

Zeeshan, Mohammad; Bora, Hema; Sharma, Yagya D.

doi:10.1093/infdis/jis650

Cited by 23 publications

(37 citation statements)

References 41 publications

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“…However, it is difficult to verify whether anti-PvTRAg is stable in the P. vivax population based on incident measurement of antibody levels among different individuals. In the current study, we evaluated antibody responses against all PvTRAgs and found different sensitivities, whereas a previous report described a 75% to 100% seropositive rate (11). This may be due to the different origins of the serum samples, as we used samples from low-endemicity area, whereas the previous study used samples from areas of high endemicity, where reinfection was common (11).…”

Section: Discussionmentioning

confidence: 84%

“…These antibodies induced from malaria parasite infection were found to play important roles in several mechanisms, including inhibition of parasite invasion, blockage of parasite development, and enhancement of the phagocytic activity of monocytes and macrophages (26,27). In the current study, we analyzed IgG antibody responses against all of the PvTRAg family proteins in a larger number of serum samples from vivax malaria patients and malaria-naive individuals than in previous PvTRAg studies (11,16). Nine novel TRAg proteins (PvTRAg_3, PvTRAg_7, PvTRAg_13, PvTRAg_14, PvTRAg_15, PvTRAg_18, PvTRAg_20, PvTRAg_26, and PvTRAg_35) showed higher IgG positivity (Ն51.8%) in patients' sera.…”

Section: Discussionmentioning

confidence: 99%

“…Boosting the response or memory response of anti-PvTRAg antibodies may induce memory T cells and/or B cells. The stability of antiPvTRAg antibodies in 5-or 10-year recovery subjects could determine the antigenicity of PvTRAgs in the induction of memory Th2 cell response in a previous study (11). However, it is difficult to verify whether anti-PvTRAg is stable in the P. vivax population based on incident measurement of antibody levels among different individuals.…”

Section: Discussionmentioning

confidence: 99%

“…Tryptophan-rich antigens (TRAgs), which contain positionally conserved tryptophan residues in a tryptophan-rich (TR) domain, have been identified in murine and human malaria parasites (6)(7)(8)(9)(10)(11). The tryptophan-rich proteins PypAg-1 and PypAg-3 were first characterized from Plasmodium yoelii, which showed binding to mouse erythrocytes (6,7).…”

mentioning

confidence: 99%

“…Remarkably, more tryptophan-rich protein-coding genes have been found in the P. vivax genome (36 genes) than in any other malaria parasite species (9). Fifteen of the tryptophan-rich antigens of P. vivax (PvTRAgs) that induced significant cellular and humoral responses in humans have been immunologically characterized and have shown few genetic polymorphisms in the parasite population (11). Recently, 10 of the 36 PvTRAgs have been shown to bind to human erythrocytes (14) and might be exploited to develop therapeutic agents against vivax malaria.…”

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confidence: 99%

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Immunoprofiling of the Tryptophan-Rich Antigen Family in Plasmodium vivax

Wang

Cheng

et al. 2015

Infect Immun

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h 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.

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Section: Discussionmentioning

confidence: 84%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Immunoprofiling of the Tryptophan-Rich Antigen Family in Plasmodium vivax

Wang

Cheng

et al. 2015

Infect Immun

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Host–parasite interaction: multiple sites in the Plasmodium vivax tryptophan‐rich antigen PvTRAg38 interact with the erythrocyte receptor band 3

et al. 2016

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Tryptophan-rich antigens of malarial parasites interact with host molecules and play an important role in parasite survival. Merozoite expressed Plasmodium vivax tryptophan-rich antigen PvTRAg38 binds to human erythrocytes and facilitates parasite growth in a heterlologous Plasmodium falciparum culture system. Recently, we identified band 3 in human erythrocytes as one of its receptors, although the receptor-ligand binding mechanisms remain unknown. In the present study, using synthetic mutated peptides of PvTRAg38, we show that multiple amino acid residues of its 12 amino acid domain (KWVQWKNDKIRS) at position 197-208 interact with three different ectodomains of band 3 receptor on human erythrocytes. Our findings may help in the design of new therapeutic approaches for malaria.

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