Characterization and antigenicity of the promising vaccine candidate Plasmodium vivax 34kDa rhoptry antigen (Pv34)

Mongui, Alvaro; Angel, Diana I.; Gallego, Gina Marcela; Reyes, Claudia; Martinez, Paola; Guhl, Felipe; Patarroyo, Manuel A.

doi:10.1016/j.vaccine.2009.10.034

Cited by 16 publications

(12 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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%

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

et al. 2017

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 85%

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

et al. 2017

Self Cite

View full text Add to dashboard Cite

show abstract

“…Ten micrograms of each recombinant PvMSP1P protein was prepared in reducing sample buffer, separated by 12% SDS-PAGE, and then stained with Coomassie brilliant blue. P. vivax parasites rich in schizonts were harvested from 10 ml of a patient blood sample (parasitemia Ͼ 0.1%) by the Percoll gradient method (20), and the parasite proteins were extracted in SDS-PAGE loading buffer. One tenth of the parasite lysate was loaded in each lane and then separated by 12% SDS-PAGE.…”

Section: Methodsmentioning

confidence: 99%

“…Thirty-one putative GPI-APs from the P. vivax genome have been identified, and 30 of them are predicted to be orthologs of GPI-APs in P. falciparum (13). Among them, only eight GPI-APs (PvMSP-1, -4, -5, -8, and -10, Pv12, Pv34, and Pv38) have been identified as possible blood-stage vaccine candidates (14)(15)(16)(17)(18)(19)(20)(21), and the rest remain uncharacterized.…”

mentioning

confidence: 99%

The Plasmodium vivax Merozoite Surface Protein 1 Paralog Is a Novel Erythrocyte-Binding Ligand of P. vivax

et al. 2013

View full text Add to dashboard Cite

dMerozoite surface protein 1 of Plasmodium vivax (PvMSP1), a glycosylphosphatidylinositol-anchored protein (GPI-AP), is a malaria vaccine candidate for P. vivax. The paralog of PvMSP1, named P. vivax merozoite surface protein 1 paralog (PvMSP1P; PlasmoDB PVX_099975), was recently identified and predicted as a GPI-AP. The similarities in genetic structural characteristics between PvMSP1 and PvMSP1P (e.g., size of open reading frames, two epidermal growth factor-like domains, and GPI anchor motif in the C terminus) led us to study this protein. In the present study, different regions of the PvMSP1P protein, demarcated based on the processed forms of PvMSP1, were expressed successfully as recombinant proteins [i.e., 83 (A, B, and C), 30, 38, 42, 33, and 19 fragments]. We studied the naturally acquired immune response against each fragment of recombinant PvMSP1P and the potential ability of each fragment to bind erythrocytes. The N-terminal fragment (83A) and two C-terminal fragments (33 and 19) reacted strongly with sera from P. vivax-infected patients, with 50 to 68% sensitivity and 95 to 96% specificity, respectively. Due to colocalization of PvMSP1P with PvMSP1, we supposed that PvMSP1P plays a similar role as PvMSP1 during erythrocyte invasion. An in vitro cytoadherence assay showed that PvMSP1P, especially the 19-kDa C-terminal region, could bind to erythrocytes. We also found that human sera from populations naturally exposed to vivax malaria and antisera obtained by immunization using the recombinant molecule PvMSP1P-19 inhibited in vitro binding of human erythrocytes to PvMSP1P-19. These results provide further evidence that the PvMSP1P might be an essential parasite adhesion molecule in the P. vivax merozoite and is a potential vaccine candidate against P. vivax.

show abstract

“…To date, five P. vivax rhoptry proteins (RAP1 (Perez-Leal et al, 2006), RAP 2 (Patarroyo et al, 2005), RhopH3 (Mongui et al, 2007), Pv38 (Mongui et al, 2008), Pv34 (Mongui et al, 2009)) have been described by screening the complete P. vivax genome sequence (Carlton et al, 2008) and using a P. vivax strain adapted to Aotus monkeys as a source for parasite DNA, RNA and proteins (Pico de Coana et al, 2003). The characterized proteins might play an important role in human reticulocyte invasion and some of them have been evaluated as vaccine candidates in the Aotus animal model (Rojas-Caraballo et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Identifying and characterizing a member of the RhopH1/Clag family in Plasmodium vivax

Moreno-Pérez

Mongui

Soler

et al. 2011

Gene

Self Cite

View full text Add to dashboard Cite

Characterization and antigenicity of the promising vaccine candidate Plasmodium vivax 34kDa rhoptry antigen (Pv34)

Cited by 16 publications

References 39 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 Plasmodium vivax Merozoite Surface Protein 1 Paralog Is a Novel Erythrocyte-Binding Ligand of P. vivax

Identifying and characterizing a member of the RhopH1/Clag family in Plasmodium vivax

Contact Info

Product

Resources

About