Merozoite surface protein-9 of Plasmodium vivax and related simian malaria parasites is orthologous to p101/ABRA of P. falciparum☆

Vargas-Serrato, Esmeralda; Barnwell, John W.; Ingravallo, Paul; Perler, Francine B.; Galinski, Mary R.

doi:10.1016/s0166-6851(01)00433-9

Cited by 52 publications

(42 citation statements)

References 44 publications

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“…Although a chymotryptic-like protease activity has been reported for MSP9 (21,26) with the implication of autoproteolysis (26), another putative natural substrate for MSP9 is yet to be identified. Interestingly, the serine protease catalytic triad postulated for P. falciparum MSP9 (His-55, Asp-94, and Ser-190 based on 3D7 sequence) is not found in Plasmodium vivax, Plasmodium knowlesi, and Plasmodium cynomolgi orthologues (27), arguing against the physiological relevance of the observed MSP9 protease activity in malaria parasite biogenesis.…”

Section: Discussionmentioning

confidence: 95%

A Co-ligand Complex Anchors Plasmodium falciparum Merozoites to the Erythrocyte Invasion Receptor Band 3

Chen

et al. 2004

Journal of Biological Chemistry

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In Plasmodium falciparum malaria, erythrocyte invasion by circulating merozoites may occur via two distinct pathways involving either a sialic acid-dependent or -independent mechanism. Earlier, we identified two nonglycosylated exofacial regions of erythrocyte band 3 termed 5ABC and 6A as an important host receptor in the sialic acid-independent invasion pathway. 5ABC, a major segment of this receptor, interacts with the 42-kDa processing product of merozoite surface protein 1 (MSP1 42 ) through its 19-kDa C-terminal domain. Here, we show that two regions of merozoite surface protein 9 (MSP9), also known as acidic basic repeat antigen, interact directly with 5ABC during erythrocyte invasion by P. falciparum. Native MSP9 as well as recombinant polypeptides derived from two regions of MSP9 (MSP9/⌬1 and MSP9/⌬2) interacted with both 5ABC and intact erythrocytes. Soluble 5ABC added to the assay mixture drastically diminished the binding of MSP9 to erythrocytes. Recombinant MSP9/⌬1 and MSP9/⌬2 present in the culture medium blocked P. falciparum reinvasion into erythrocytes in vitro. Native MSP9 and MSP1 42 , the two ligands binding to the 5ABC receptor, existed as a stable complex. Our results establish a novel concept wherein the merozoite exploits a specific complex of co-ligands on its surface to target a single erythrocyte receptor during invasion. This new paradigm poses a new challenge in the development of a vaccine for blood stage malaria.

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Section: Discussionmentioning

confidence: 95%

A Co-ligand Complex Anchors Plasmodium falciparum Merozoites to the Erythrocyte Invasion Receptor Band 3

Chen

et al. 2004

Journal of Biological Chemistry

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“…Association between antibody responses to PvMSP-9 and P. vivax PvMSP-9 is associated with the surface of the merozoite and contains a hydrophobic signal sequence, a highly conserved N-terminal domain with a cluster of four cysteines, and a C-terminal region containing two speciesspecific blocks of repeats, designated PvMSP-9 RI and PvMSP-9 RII [57,58]. Recombinant proteins may represent individual blocks or both blocks (PvMSP-9 RIRII ).…”

Section: Cohort Studiesmentioning

confidence: 99%

Immunological markers of Plasmodium vivax exposure and immunity: a systematic review and meta-analysis

Cutts¹,

Powell²,

Agius³

et al. 2014

BMC Medicine

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Background: Identifying Plasmodium vivax antigen-specific antibodies associated with P. vivax infection and protective immunity is key to the development of serosurveillance tools and vaccines for malaria. Antibody targets of P. vivax can be identified by seroepidemiological studies of individuals living in P. vivax-endemic areas, and is an important strategy given the limited ability to culture P. vivax in vitro. There have been numerous studies investigating the association between P. vivax antibody responses and P. vivax infection, but there has been no standardization of results to enable comparisons across populations. Methods: We performed a systematic review with meta-analysis of population-based, cross-sectional, case-control, and cohort studies of individuals living in P. vivax-endemic areas. We searched 6 databases and identified 18 studies that met predefined inclusion and quality criteria, and examined the association between antibody responses to P. vivax antigens and P. vivax malaria.

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“…The completion of the Plasmodium falciparum genome has provided the basis for the identification of many proteins in sporozoites (5, 12), but very few of these proteins are characterized for their function in sporozoite infectivity and development in the liver. Proteomic and transcript analyses have identified a number of apical organelle and membraneassociated proteins expressed both in sporozoites and merozoites, with many belonging to molecular families conserved among the diverse species of Plasmodium (3,5,7,19,(22)(23)(24).The circumsporozoite protein (CSP) and to a lesser extent the thrombospondin-related anonymous protein (TRAP, or sporozoite surface protein 2 [SSP2]) have been the focus of most research on the sporozoite stages. CSP and TRAP are major sporozoite proteins that are functionally important for sporozoite development in the mosquito stage and are widely considered as important targets for vaccine development.…”

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confidence: 99%

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confidence: 99%

Antibodies against MAEBL Ligand Domains M1 and M2 Inhibit Sporozoite Development In Vitro

Preiser¹,

Rénia

Singh

et al. 2004

Infect Immun

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MAEBL is a type 1 membrane protein that is implicated in the merozoite invasion of erythrocytes and sporozoite invasion of mosquito salivary glands. This apical organelle protein is structurally similar to the ebl erythrocyte binding proteins, such as EBA-175, except that the tandem ligand domains of MAEBL are similar to part of the extracellular domain of apical membrane antigen 1 and not the Duffy binding-like domain. Although midgut and salivary gland sporozoites are morphologically similar, salivary gland sporozoites undergo a period of new gene expression after infecting the salivary glands, display distinct phenotypic differences, and are more infectious for the mammalian host. The objectives of this project were to determine the molecular form of MAEBL in the infectious salivary gland sporozoites and whether the ligand has a role in the sporozoite development to exoerythrocytic stages in hepatocytes. We determined that MAEBL is newly expressed in salivary gland sporozoites and in a form distinct from what is present in the midgut sporozoites or present in erythrocytic stages. Both ligand domains (M1 and M2) were expressed as part of a full-length membrane form of MAEBL in the salivary gland sporozoites in contrast to the other stages that retain only the M2 ligand domain as part of the membrane form of the protein. Antisera developed against the cysteine-rich regions of the extracellular portion of MAEBL inhibited sporozoite development to exoerythrocytic forms in vitro. Together these data indicate that MAEBL has a role in this third developmental stage in the life cycle of the malaria parasite. Thus, MAEBL is another target for pre-erythrocytic-stage vaccine development against malaria parasites.Malaria is one of the most serious human diseases, causing several million deaths and clinical illness in hundreds of millions of people every year. Infection is spread from person to person by the bite of a Plasmodium-infected anopheline mosquito. Sporozoites injected by the mosquito must infect and develop in a hepatocyte, which can then initiate the bloodstage infection that causes the severe pathogenesis of malaria. Molecules in the apical organelles and on the surface of malaria sporozoites play a role in sporozoite motility and target this infective stage to the liver. The completion of the Plasmodium falciparum genome has provided the basis for the identification of many proteins in sporozoites (5, 12), but very few of these proteins are characterized for their function in sporozoite infectivity and development in the liver. Proteomic and transcript analyses have identified a number of apical organelle and membraneassociated proteins expressed both in sporozoites and merozoites, with many belonging to molecular families conserved among the diverse species of Plasmodium (3,5,7,19,(22)(23)(24).The circumsporozoite protein (CSP) and to a lesser extent the thrombospondin-related anonymous protein (TRAP, or sporozoite surface protein 2 [SSP2]) have been the focus of most research on the sporozoite stages. CSP ...

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Merozoite surface protein-9 of Plasmodium vivax and related simian malaria parasites is orthologous to p101/ABRA of P. falciparum☆

Cited by 52 publications

References 44 publications

A Co-ligand Complex Anchors Plasmodium falciparum Merozoites to the Erythrocyte Invasion Receptor Band 3

A Co-ligand Complex Anchors Plasmodium falciparum Merozoites to the Erythrocyte Invasion Receptor Band 3

Immunological markers of Plasmodium vivax exposure and immunity: a systematic review and meta-analysis

Antibodies against MAEBL Ligand Domains M1 and M2 Inhibit Sporozoite Development In Vitro

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