Identification of a reticulocyte-specific binding domain of Plasmodium vivax reticulocyte-binding protein 1 that is homologous to the PfRh4 erythrocyte-binding domain

Han, Jin‐Hee; Lee, Seong-Kyun; Wang, Bo; Muh, Fauzi; Nyunt, Myat Htut; Na, Sunghun; Ha, Kwon‐Soo; Hong, Seok‐Ho; Park, Won Sun; Sattabongkot, Jetsumon; Tsuboi, Takafumi; Han, Eun‐Taek

doi:10.1038/srep26993

Cited by 43 publications

(62 citation statements)

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“…The surface-exposed antigens on merozoites are abundant and serve essential functions that mediate initial contact with erythrocyte surface. This hypothesis was supported by previous functional studies of P. vivax merozoite surface proteins [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19] and Plasmodium falciparum (15,16). Recently, PvMSP1 paralog (PvMSP1P) was reported as a novel erythrocyte binding protein (17).…”

supporting

confidence: 58%

“…The interaction of parasite ligands with erythrocyte surface molecules during P. vivax invasion is essential for successful invasion from initial contact to internalization (9,10). In P. vivax, several adhesive ligands from the merozoite apical region that are important for specific interactions with reticulocytes, including PvRBP1a, PvRBP1b, PvRBP2a, PvRBP2b, and PvEBP2, have been identified (11)(12)(13)(14). All of these apically localized antigens may be responsible for parasite internalization in reticulocytes (9).…”

mentioning

confidence: 99%

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Plasmodium vivax Merozoite Surface Protein 1 Paralog as a Mediator of Parasite Adherence to Reticulocytes

et al. 2018

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parasites preferentially invade reticulocytes in human beings. merozoite surface protein 1 (PvMSP1) and PvMSP1 paralog (PvMSP1P) may have important functions in reticulocyte adherence during invasion. These proteins share similar structures, including the presence of two epidermal growth factor (EGF)-like and glycosylphosphatidylinositol (GPI)-anchored domains at the C terminus. However, there have been no reports concerning the functional activity of PvMSP1P in reticulocyte adherence during invasion. In this study, the ability of PvMSP1P-19 to bind to reticulocytes and normocytes was analyzed. The reticulocyte binding activity of PvMSP1P-19 was 4.0-fold higher than its normocyte binding activity. The binding of PvMSP1P-19 to reticulocytes and normocytes was inhibited in a dose-dependent manner by antibodies from immunized rabbits and by antibodies from vivax parasite-infected patients. Consistently, antibodies against PvMSP1P inhibited parasite invasion during short-term cultivation. Similar to the case for PvDBPII binding activity, PvMSP1P-19 binding activity was reduced in chymotrypsin-treated reticulocytes. However, no significant difference between the binding of PvMSP1P-19 to Duffy-positive and Duffy-negative erythrocytes was found. The minimal binding motif of PvMSP1P-19 was characterized using synthetic peptides. The results showed that the residues at amino acid positions 1791 to 1808 may have an important function in mediating merozoite adherence to reticulocytes. The positively charged residues within the EGF-like domain were shown to constitute a key binding motif. This work presents strong evidence supporting the role of PvMSP1P in host target cell selection and invasion of Duffy-independent pathway in Moreover, PvMSP1P-19-specific antibodies may confer protection against reinvasion.

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confidence: 58%

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Plasmodium vivax Merozoite Surface Protein 1 Paralog as a Mediator of Parasite Adherence to Reticulocytes

et al. 2018

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“…We successfully expressed full-length rRBP2-P1 and characterized its binding to erythrocytes. Like several RBPs (3,13,14), the protein preferentially binds reticulocytes over normocytes. Binding to erythrocytes was sensitive to trypsin and chymotrypsin treatments but insensitive to neuraminidase treatment.…”

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confidence: 99%

“…. Most RBPs (RBP1a, RBP1b, RBP2a, RBP2b, RBP2c, and RBP2-P2) were recently characterized and found to have erythrocyte binding capacity and various degrees of reticulocyte selectivity (3,4,(12)(13)(14). Human antibodies to some of these proteins are associated with reduced parasitemia (15) or protection against clinical disease (13).…”

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The Blood Stage Antigen RBP2-P1 of Plasmodium vivax Binds Reticulocytes and Is a Target of Naturally Acquired Immunity

et al. 2020

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The interactions between Plasmodium parasites and human erythrocytes are prime targets of blood stage malaria vaccine development. The reticulocyte binding protein 2-P1 (RBP2-P1) of Plasmodium vivax, a member of the reticulocyte binding protein family, has recently been shown to be highly antigenic in several settings endemic for malaria. Yet, its functional characteristics and the relevance of its antibody response in human malaria have not been examined. In this study, the potential function of RBP2-P1 as an invasion ligand of P. vivax was evaluated. The protein was found to be expressed in schizonts, be localized at the apical end of the merozoite, and preferentially bind reticulocytes over normocytes. Human antibodies to this protein also exhibit erythrocyte binding inhibition at physiologically relevant concentrations. Furthermore, RBP2-P1 antibodies are associated with lower parasitemia and tend to be higher in asymptomatic carriers than in patients. This study provides evidence supporting a role of RBP2-P1 as an invasion ligand and its consideration as a vaccine target.

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“…The level of DARC on mature RBCs is reduced compared to that on reticulocytes 25 , which possibly explains the predilection of P. knowlesi for reticulocytes. Besides Duffy binding protein, the reticulocyte binding-like proteins (RBLs), another important ligand family, also contribute to the successful invasion of human RBCs 49,59 .…”

Section: Cryopreservation Of Reticulocytes and Malariamentioning

confidence: 99%

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2019

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Plasmodium knowlesi, a simian malaria parasite, is widely used as a malaria model and now characterized as a clinically significant parasite that can lead to outbreaks throughout most countries in Southeast Asia. Despite its importance, both fundamental and clinical studies of P. knowlesi have been impeded by the lack of a convenient in-vitro culture system partly due to the parasite's preference for reticulocytes. Due to a limited number of reticulocytes that could be collected from fresh sources such as umbilical cord, bone marrow, and peripheral blood, scientists have opted reticulocytes generated from CD34 + hematopoietic stem cells (HSCs) that have been cultured in an in-vitro system. With sufficient growth factors (GFs) and differentiation factors (DFs), a higher number and more homogenous populations of reticulocytes could be obtained from HSCs invitro. Here, we review an approach to produce massive expansion of CD34 + HSCs and their differentiation into reticulocytes that could be used for the establishment of a continuous in-vitro culture of P. knowlesi or P. vivax. The successful development of the long-term in-vitro culture of this parasite could ultimately provide an ideal system for forwarding diagnostic, antimalarial drug and vaccine studies in malaria.

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Identification of a reticulocyte-specific binding domain of Plasmodium vivax reticulocyte-binding protein 1 that is homologous to the PfRh4 erythrocyte-binding domain

Cited by 43 publications

References 50 publications

Plasmodium vivax Merozoite Surface Protein 1 Paralog as a Mediator of Parasite Adherence to Reticulocytes

Plasmodium vivax Merozoite Surface Protein 1 Paralog as a Mediator of Parasite Adherence to Reticulocytes

The Blood Stage Antigen RBP2-P1 of Plasmodium vivax Binds Reticulocytes and Is a Target of Naturally Acquired Immunity

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