The GPI-anchored 6-Cys Protein Pv12 is Present in Detergent-resistant Microdomains of Plasmodium vivax Blood Stage Schizonts

Moreno-Pérez, Darwin A.; Areiza-Rojas, Rafael; Flórez-Buitrago, Ximena; Silva, Yolanda; Patarroyo, Manuel Elkín; Patarroyo, Manuel A.

doi:10.1016/j.protis.2012.03.001

Cited by 15 publications

(31 citation statements)

References 48 publications

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“…This RR was common in different P. vivax strains but not in phylogenetically-related species (Additional file 1: Figure S1). This characteristic has been found in several P. vivax antigens described in the P. vivax VCG-I strain located on the parasite surface (Pv12 [12], ARP [43]) or in the apical pole (Pv34 [44], RON1 [45], RON2 [46] and RON4 [47, 48]). DNA sequences from different P. vivax strains and phylogenetically-related species were thus compared to ascertain whether gama gene diversity has been modulated by immune pressure.…”

Section: Discussionmentioning

confidence: 85%

“…Unfortunately, basic P. vivax research has been delayed mainly due to the parasite’s preference for invading reticulocytes which are difficult to obtain in the high percentages needed for propagating P. vivax in vitro [12, 13]. However, it has been possible to characterise several molecules forming part of the parasite’s selective human reticulocyte invasion route, such as reticulocyte binding proteins (RBPs) [14, 15], merozoite surface protein 1 (MSP-1) [16], some proteins from the tryptophan-rich antigen (TRAg) family [17] and the recently described rhoptry neck protein 5 (RON5) [18].…”

Section: Introductionmentioning

confidence: 99%

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PvGAMA reticulocyte binding activity: predicting conserved functional regions by natural selection analysis

et al. 2017

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BackgroundAdhesin proteins are used by Plasmodium parasites to bind and invade target cells. Hence, characterising molecules that participate in reticulocyte interaction is key to understanding the molecular basis of Plasmodium vivax invasion. This study focused on predicting functionally restricted regions of the P. vivax GPI-anchored micronemal antigen (PvGAMA) and characterising their reticulocyte binding activity.ResultsThe pvgama gene was initially found in P. vivax VCG-I strain schizonts. According to the genetic diversity analysis, PvGAMA displayed a size polymorphism very common for antigenic P. vivax proteins. Two regions along the antigen sequence were highly conserved among species, having a negative natural selection signal. Interestingly, these regions revealed a functional role regarding preferential target cell adhesion.ConclusionsTo our knowledge, this study describes PvGAMA reticulocyte binding properties for the first time. Conserved functional regions were predicted according to natural selection analysis and their binding ability was confirmed. These findings support the notion that PvGAMA may have an important role in P. vivax merozoite adhesion to its target cells.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-017-2183-8) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 85%

Section: Introductionmentioning

confidence: 99%

PvGAMA reticulocyte binding activity: predicting conserved functional regions by natural selection analysis

et al. 2017

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“…Pv12, the Pf12 orthologue in P. vivax , was shown to be transcribed in schizonts and localized to the surface and rhoptries of merozoites by immunofluorescence (Li et al, 2012; Cheng et al, 2013; Moreno-Perez et al, 2013). The interaction of Pv12 and Pv41 has recently been reported in addition to a novel interaction with PVX_110945 (Hostetler et al, 2015).…”

Section: 6-cys Proteins In Asexual Erythrocytic Stagesmentioning

confidence: 99%

“…Low genetic diversity was observed for Pv12 in a Colombian parasite population (Forero-Rodriguez et al, 2014) but a higher number of polymorphisms was found in parasite populations from the China-Myanmar border (Wang et al, 2014). Pv12 is recognized by sera of naturally infected patients (Chen et al, 2010; Moreno-Perez et al, 2013; Franca et al, 2016) and a strong association in reduced risk of clinical disease and antibody levels was recently reported (Franca et al, 2016). …”

Section: 6-cys Proteins In Asexual Erythrocytic Stagesmentioning

confidence: 99%

The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle

Arredondo

Kappe

2017

International Journal for Parasitology

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During their life cycle Plasmodium parasites rely upon an arsenal of proteins that establish key interactions with the host or vector, and between the parasite sexual stages, with the purpose of ensuring infection, reproduction and proliferation. Among these is a group of secreted or membrane-anchored proteins known as the six-cysteine (6-cys) family. This is a small but important family with only 14 members thus far identified, each stage-specifically expressed during the parasite life cycle. 6-cys proteins often localize at the parasite surface or interface with the host and are conserved in different Plasmodium species. The unifying feature of the family is the s48/45 domain, presumably involved in adhesion and structurally related to Ephrins, the ligands of Eph receptors. The most prominent s48/45 members are currently under functional investigation and are being pursued as vaccine candidates. In this review, we examine what is known about the 6-cys family, their structure and function, and discuss future research directions.

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“…It was found that Pv RBSA could trigger an immune response during natural P. vivax malaria infection (Fig. 2), as described for other surface antigens in the P. vivax VCG-I strain, such as Pv MSP-10 [37], Pv 12 [38] and Pv ARP [30]. Once Pv RBSA localisation pattern and ability to trigger an immune response had been determined, it was ascertained whether the protein could bind to the most immature human reticulocytes using anti-CD71 monoclonal antibody (a specific marker for the cells [39]).…”

Section: Discussionmentioning

confidence: 66%

Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes

et al. 2017

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Background Plasmodium vivax uses multiple ligand-receptor interactions for preferential invasion of human reticulocytes. Several of these ligands have been identified by in silico approaches based on the role displayed by their orthologs in other Plasmodium species during initial adhesion or invasion. However, the cell adhesion role of proteins that are exclusive to species that specifically invade reticulocytes (as P. vivax and P. cynomolgi) has not been evaluated to date. This study aimed to characterise an antigen shared between Plasmodium species that preferentially infect reticulocytes with a focus on assessing its binding activity to target cells.ResultsAn in silico analysis was performed using P. vivax proteome data to identify and characterise one antigen shared between P. vivax and P. cynomolgi. This led to identification of the pvrbsa gene present in the P. vivax VCG-I strain genome. This gene is transcribed in mature schizonts and encodes a protein located on the parasite surface. rPvRBSA was antigenic and capable of binding to a population of reticulocytes with a different Duffy phenotype. Interestingly, the molecule showed a higher percentage of binding to immature human reticulocytes (CD71hi).ConclusionsThis study describes for the first time, a molecule involved in host cell binding that is exclusive in reticulocyte-infecting Plasmodium species. This suggest that PvRBSA is an antigenic adhesin that plays a role in parasite binding to target cells.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-017-2185-6) contains supplementary material, which is available to authorized users.

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The GPI-anchored 6-Cys Protein Pv12 is Present in Detergent-resistant Microdomains of Plasmodium vivax Blood Stage Schizonts

Cited by 15 publications

References 48 publications

PvGAMA reticulocyte binding activity: predicting conserved functional regions by natural selection analysis

PvGAMA reticulocyte binding activity: predicting conserved functional regions by natural selection analysis

The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle

Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes

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