Plasmodium vivax: functional analysis of a highly conserved PvRBP-1 protein region

Cantor, Elvia Marı́a; Lombo, Tania; Cepeda, Alexandra; Espinosa, Ana; Barrero, Carlos; Guzmán, Fanny; Gunturiz, María Luz; Urquiza, Mauricio; Ocampo, Marisol; Patarroyo, Manuel Elkín

doi:10.1016/s0166-6851(01)00355-3

Cited by 21 publications

(11 citation statements)

References 16 publications

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“…Therefore, extensive research is underway to identify and characterize additional potential vaccine antigens from P. vivax . In recent years, several P. vivax antigens have been identified and characterized, including apical membrane antigen‐1 (PvAMA1), Duffy‐binding protein (PvDBP), circumsporozoite protein (PvCSP), rhoptry‐associated protein 1 (PvRAP‐1), rhoptry‐associated protein 2 (PvRAP‐2), reticulocytes‐binding proteins 1 and 2 (PvRBP‐1 and PvRBP‐2), surface protein 25 (PvS25), merozoite surface protein 1 (PvMSP1), PvMSP3 (α, β and γ), PvMSP8, MSP10, tryptophan‐rich antigens PvTRAg and PvTARAg55 (6–16).…”

Section: Details Of Th1 and Th2 Cytokines Levels In 16 P Vivax‐exposmentioning

confidence: 99%

Cellular immune responses to recombinant Plasmodium vivax tryptophan‐rich antigen (PvTRAg) among individuals exposed to vivax malaria

Alam¹,

Bora²,

Mittra³

et al. 2008

Parasite Immunology

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Plasmodium vivax, the most widespread species of human malaria parasite responsible for 70-80 million cases each year requires a vaccine. In recent years, many potential vaccine candidate antigens have been identified from P. vivax including PvTRAg. We describe here cellular immune response to recombinant PvTRAg expressed in Escherichia coli. The in vitro stimulation of PBMCs derived from P. vivax-exposed individuals (n = 16) showed strong proliferative response (SI > 2.2) to PvTRAg as compared to PBMCs from normal healthy controls (n = 8). Although both Th1 (IFN-gamma, TNF-alpha and IL-12) and Th2 (IL-4 and IL-10) cytokines were secreted by the PBMCs of the P. vivax-exposed individuals in response to PvTRAg, the overall response was more inclined towards Th2. In conclusion, recombinant PvTRAg was found to elicit strong cellular immune response among the P. vivax-exposed individuals.

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Section: Details Of Th1 and Th2 Cytokines Levels In 16 P Vivax‐exposmentioning

confidence: 99%

Cellular immune responses to recombinant Plasmodium vivax tryptophan‐rich antigen (PvTRAg) among individuals exposed to vivax malaria

Alam¹,

Bora²,

Mittra³

et al. 2008

Parasite Immunology

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“…8 kb–9 kb). Thus, overlapping peptides were used to define the binding domains of Pvrbp1 [16], [17], [18]. The other investigation was confined to an assessment of Pvrbp1 and Pvrbp2 diversity in four isolates from different geographical regions [19], which revealed a remarkably high diversity in Pvrbp2 as compared to Pvrbp1 and its homolog in P. falciparum and provided an indication as to the sub-domains it might be worth to focus on in future studies.…”

Section: Introductionmentioning

confidence: 99%

Genetic Diversity in New Members of the Reticulocyte Binding Protein Family in Thai Plasmodium vivax Isolates

et al. 2012

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Background Plasmodium vivax merozoites specifically invade reticulocytes. Until recently, two reticulocyte-binding proteins (Pvrbp1 and Pvrbp2) expressed at the apical pole of the P. vivax merozoite were considered to be involved in reticulocyte recognition. The genome sequence recently obtained for the Salvador I (Sal-I) strain of P. vivax revealed additional genes in this family, and in particular Pvrbp2a, Pvrbp2b (Pvrbp2 has been renamed as Pvrbp2c) and two pseudogenes Pvrbp2d and Pvrbp3. It had been previously found that Pvrbp2c is substantially more polymorphic than Pvrbp1. The primary goal of this study was to ascertain the level of polymorphism of these new genes.Methodology/Principal FindingsThe sequence of the Pvrbp2a, Pvrbp2b, Pvrbp2d and Pvrbp3 genes were obtained by amplification/cloning using DNA purified from four isolates collected from patients that acquired the infection in the four cardinal regions of Thailand (west, north, south and east). An additional seven isolates from western Thailand were analyzed for gene copy number variation. There were significant polymorphisms exhibited by these genes (compared to the reference Sal-I strain) with the ratio of mutations leading to a non-synonymous or synonymous amino acid change close to 3∶1 for Pvrbp2a and Pvrbp2b. Although the degree of polymorphism exhibited by these two genes was higher than that of Pvrbp1, it did not reach the exceptional diversity noted for Pvrbp2c. It was interesting to note that variations in the copy number of Pvrbp2a and Pvrbp2b occurred in some isolates.Conclusions/SignificanceThe evolution of different members of the Pvrbp2 family and their relatively high degree of polymorphism suggests that the proteins encoded by these genes are important for parasite survival and are under immune selection. Our data also shows that there are highly conserved regions in rbp2a and rbp2b, which might provide suitable targets for future vaccine development against the blood stage of P. vivax.

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“…PvRBP receptors have yet to be identified, in part because it is not possible to culture blood stages of P. vivax ; however, PvRBP1 peptides that bind to reticulocytes, have been identified (Cantor et al, 2001; Urquiza et al, 2002). A short review by Li and Han (2012) describes the RBPs in further detail.…”

Section: Parasite Interaction With the Host Cellmentioning

confidence: 99%

The apicomplexan glideosome and adhesins – Structures and function

Boucher

Bosch

2015

Journal of Structural Biology

110

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The apicomplexan family of pathogens, which includes Plasmodium spp. and Toxoplasma gondii, are primarily obligate intracellular parasites and invade multiple cell types. These parasites express extracellular membrane protein receptors, adhesins, to form specific pathogen-host cell interaction complexes. Various adhesins are used to invade a variety of cell types. The receptors are linked to an actomyosin motor, which is part of a complex comprised of many proteins known as the invasion machinery or glideosome. To date, reviews on invasion have focused primarily on the molecular pathways and signals of invasion, with little or no structural information presented. Over 75 structures of parasite receptors and glideosome proteins have been deposited with the Protein Data Bank. These structures include adhesins, motor proteins, bridging proteins, inner membrane complex and cytoskeletal proteins, as well as co-crystal structures with peptides and antibodies. These structures provide information regarding key interactions necessary for target receptor engagement, machinery complex formation, how force is transmitted, and the basis of inhibitory antibodies. Additionally, these structures can provide starting points for the development of antibodies and inhibitory molecules targeting protein-protein interactions, with the aim to inhibit invasion. This review provides an overview of the parasite adhesin protein families, the glideosome components, glideosome architecture, and discuss recent work regarding alternative models.

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Plasmodium vivax: functional analysis of a highly conserved PvRBP-1 protein region

Cited by 21 publications

References 16 publications

Cellular immune responses to recombinant Plasmodium vivax tryptophan‐rich antigen (PvTRAg) among individuals exposed to vivax malaria

Cellular immune responses to recombinant Plasmodium vivax tryptophan‐rich antigen (PvTRAg) among individuals exposed to vivax malaria

Genetic Diversity in New Members of the Reticulocyte Binding Protein Family in Thai Plasmodium vivax Isolates

The apicomplexan glideosome and adhesins – Structures and function

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