An unusual tryptophan-rich domain characterizes two secreted antigens of Plasmodium yoelii-infected erythrocytes

Burns, James M.; Adeeku, Eric K.; Belk, Carla C.; Dunn, Patricia D.

doi:10.1016/s0166-6851(00)00252-8

Cited by 33 publications

(28 citation statements)

References 25 publications

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“…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).…”

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confidence: 99%

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confidence: 99%

“…The tryptophan-rich proteins PypAg-1 and PypAg-3 were first characterized from Plasmodium yoelii, which showed binding to mouse erythrocytes (6,7). PypAg-1 and PypAg-3, which are reportedly exported to the membranes of P. yoelii-infected erythrocytes, induce immune responses, and mice immunized with recombinant proteins were protected against parasite challenge infection with P. yoelii (7). Homologs of PypAg-1 and PypAg-3 have been identified in P. falciparum and named tryptophan-threonine-rich antigens (PfTryThrA) and P. falciparum merozoite-associated tryptophan-rich antigen (PfMaTrA), respectively (8,12).…”

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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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confidence: 99%

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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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“…In addition to a putative transmembrane domain, the N-terminal portion of pypAg-1 contains a domain unusually rich in tryptophan residues. This tryptophan-rich domain is conserved in pypAg-3, another P. yoelii antigen with a similar pattern of expression that was also identified with the pAg immunization serum (7). The C terminus of pypAg-1 contains a 155-amino-acid, highly charged repeat domain.…”

Section: Vol 68 2000mentioning

confidence: 63%

“…We previously characterized pypAg-1 as one P. yoelii antigen that contributed to the pAg-induced protection. This antigen is expressed by P. yoelii trophozoites, exported to the erythrocyte membrane, and eventually secreted from infected erythrocytes (7,8). In addition to a putative transmembrane domain, the N-terminal portion of pypAg-1 contains a domain unusually rich in tryptophan residues.…”

Section: Vol 68 2000mentioning

confidence: 99%

A Protective Glycosylphosphatidylinositol-Anchored Membrane Protein ofPlasmodium yoeliiTrophozoites and Merozoites Contains Two Epidermal Growth Factor-Like Domains

2000

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Using sera from mice immunized and protected against Plasmodium yoelii malaria, we identified a novel blood-stage antigen gene, pypag-2. The 2.1-kb pypag-2 cDNA contains a single open reading frame that encodes a 409-amino-acid protein with a predicted molecular mass of 46.8 kDa. Unlike many characterized plasmodial antigens, blocks of tandemly repeated amino acids are lacking in the pypAg-2 protein sequence. Recombinant pypAg-2, comprising the full-length protein minus the predicted N-terminal signal and C-terminal anchor sequences, was produced and used to raise a high-titer polyclonal rabbit antiserum. This antiserum was used to identify and characterize the native protein through immunoblotting, immunoprecipitation and immunofluorescence assays. Consistent with the presence of a glycosylphosphatidylinositol anchor, pypAg-2 fractionated with the detergent phase of Triton X-114-solubilized proteins and could be metabolically labeled with [ 3 H]palmitic acid. By immunofluorescence, pypAg-2 expression was localized to both the trophozoite and merozoite membranes. Similar to Plasmodium falciparum merozoite surface protein 1, pypAg-2 contains two C-terminal epidermal growth factor (EGF)-like domains. Most importantly, immunization with recombinant pypAg-2 protected mice against lethal P. yoelii malaria. Thus, pypAg-2 is a target of protective immune responses and represents a novel addition to the family of merozoite surface proteins that contain one or more EGF-like domains.

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Genes coding for tryptophan-rich proteins are transcribed throughout the asexual cycle of Plasmodium falciparum

Ntumngia¹,

Bahamontes-Rosa²,

Kun³

2005

Parasitol Res

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Multigene families are a common feature in Plasmodia spp. and constitute a substantial content of the parasite genome. Here, we analyse the structural organisation and sequence diversity of two further members of the Trp-rich multigene family of P. falciparum. The complete DNA sequence of both genes was determined from a series of laboratory adapted and field isolates. Based on the amino acid sequences, we have termed them tryptophan-rich antigen-3 (TrpA-3) and lysine-tryptophan-rich antigen (LysTrpA). Analysis of the genes using reverse transcriptase-polymerase chain reaction (RT-PCR), showed that both genes are transcribed and that introns are spliced out at predicted positions. Gene expression profiles obtained from microarray analysis indicate that both genes are expressed in the mid-stages of the asexual cycle. In-frame stop codons were detected which interrupted the reading frame of LysTrpA. Whereas the number of the Trp-rich proteins is rather low in P. falciparum, P. chabaudi, P. berghei and P. yoelii, this family seems to have 15 or more members in P. knowlesi and P. vivax.

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An unusual tryptophan-rich domain characterizes two secreted antigens of Plasmodium yoelii-infected erythrocytes

Cited by 33 publications

References 25 publications

Immunoprofiling of the Tryptophan-Rich Antigen Family in Plasmodium vivax

Immunoprofiling of the Tryptophan-Rich Antigen Family in Plasmodium vivax

A Protective Glycosylphosphatidylinositol-Anchored Membrane Protein ofPlasmodium yoeliiTrophozoites and Merozoites Contains Two Epidermal Growth Factor-Like Domains

Genes coding for tryptophan-rich proteins are transcribed throughout the asexual cycle of Plasmodium falciparum

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