Low genetic polymorphism of merozoite surface proteins 7 and 10 in Colombian Plasmodium vivax isolates

Garzón‐Ospina, Diego; Romero-Murillo, Liza; Tobón, Luisa F.; Patarroyo, Manuel A.

doi:10.1016/j.meegid.2010.12.002

Cited by 21 publications

(23 citation statements)

References 25 publications

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“…Therefore, the immune response must be directed against conserved regions to avoid different parasite strains evading immunity, thereby reducing vaccine efficacy. According to the selection signal identification strategy, low genetic diversity was found in the GAMA-encoding gene, comparable to that observed in msp4 [55, 56], msp7A/7 K/7 F/7 L [57, 58], msp8 [59], msp10 [57, 59], pv12 , pv38 [22, 24], pv41 [23, 24], rap1/2 [60] and ron4 [48] which seem involved in host cell invasion. Despite the lack of statistically significant values for d N -d S difference, K S divergence amongst species was greater than K N , suggesting negative selection.…”

Section: Discussionmentioning

confidence: 59%

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: 59%

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

et al. 2017

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“…We thus analysed MSP7 proteins from other Plasmodium species to assess functional divergence amongst MSP7 clades (paralogous) but also within clades (orthologous). Unlike a previous study [15], just the MSP7 C-terminal region was analysed here, taking into account that this region has the domain (MSP_7C) defining members of this family, it is the only MSP7 region in the protein complex [7], in P. vivax MSP7s C-terminal regions are highly conserved and under negative selection whilst other regions are highly polymorphic [23–25] and most regions binding to red blood cells are in the MSP7 C-terminal region [21]. We have found changes in evolutionary rates amongst paralogous proteins in this region.…”

Section: Discussionmentioning

confidence: 99%

“…The C-terminal region is involved in gene conversion [23]. Moreover, this region is highly conserved and under negative selection, suggesting functional/structural constraint [23–25]; by contrast, some P. vivax MSP7 proteins’ central regions have high genetic diversity, maintained by balancing selection, possibly as an immune evasion mechanism [23, 24]. …”

Section: Introductionmentioning

confidence: 99%

Evidence of functional divergence in MSP7 paralogous proteins: a molecular-evolutionary and phylogenetic analysis

2016

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BackgroundThe merozoite surface protein 7 (MSP7) is a Plasmodium protein which is involved in parasite invasion; the gene encoding it belongs to a multigene family. It has been proposed that MSP7 paralogues seem to be functionally redundant; however, recent experiments have suggested that they could have different roles.ResultsThe msp7 multigene family has been described in newly available Plasmodium genomes; phylogenetic relationships were established in 12 species by using different molecular evolutionary approaches for assessing functional divergence amongst MSP7 members. Gene expansion and contraction rule msp7 family evolution; however, some members could have had concerted evolution. Molecular evolutionary analysis showed that relaxed and/or intensified selection modulated Plasmodium msp7 paralogous evolution. Furthermore, episodic diversifying selection and changes in evolutionary rates suggested that some paralogous proteins have diverged functionally.ConclusionsEven though msp7 has mainly evolved in line with a birth-and-death evolutionary model, gene conversion has taken place between some paralogous genes allowing them to maintain their functional redundancy. On the other hand, the evolutionary rate of some MSP7 paralogs has become altered, as well as undergoing relaxed or intensified (positive) selection, suggesting functional divergence. This could mean that some MSP7s can form different parasite protein complexes and/or recognise different host receptors during parasite invasion. These results highlight the importance of this gene family in the Plasmodium genus.Electronic supplementary materialThe online version of this article (doi:10.1186/s12862-016-0830-x) contains supplementary material, which is available to authorized users.

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“…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.…”

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

et al. 2013

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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.

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Low genetic polymorphism of merozoite surface proteins 7 and 10 in Colombian Plasmodium vivax isolates

Cited by 21 publications

References 25 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

Evidence of functional divergence in MSP7 paralogous proteins: a molecular-evolutionary and phylogenetic analysis

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

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