Merozoite surface protein 8 of Plasmodium falciparum contains two epidermal growth factor-like domains

Black, Casilda Gabrielle; Wu, Tieqiao; Wang, Lina; Hibbs, Alan R.; Coppel, Ross L.

doi:10.1016/s0166-6851(01)00265-1

Cited by 75 publications

(72 citation statements)

References 33 publications

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“…Parasite extracts (Black et al, 2001) and synchronised cultures (Lambros and Vanderberg, 1979) were prepared as described and sampled at various time points for analysis of stage-specific expression.…”

Section: Plasmodium Falciparum Parasitesmentioning

confidence: 99%

“…The underlined sequences encode restriction endonuclease sites and the capitalised sequence is Pf34 gene-specific. DNA cloning and characterisation procedures were performed as previously described (Black et al, 2001). …”

Section: Genomic Sequences Molecular Cloning and Analysismentioning

confidence: 99%

“…Recombinant Pf34-GST fragments were expressed in Escherichia coli BL21 (DE3) (Invitrogen) and purified as described previously (Black et al, 2001). Polyclonal antisera were raised in 6-8-weeks-old female BALB/C mice (Monash Animal Services, Clayton Vic, Australia).…”

Section: Recombinant Protein Expression and Production Of Polyclonal mentioning

confidence: 99%

“…GPIanchored proteins have emerged as important candidates for inclusion in a blood-stage subunit vaccine. At least nine GPI-anchored merozoite proteins have been described (Merozoite Surface Protein (MSP)-1, -2, -4, -5, -8, -10, Pf92, Pf38 and Pf12) and two others (RAMA and ASP) have been localised to apical organelles (Holder and Freeman, 1982;Smythe et al, 1988;Marshall et al, 1997Marshall et al, , 1998Black et al, 2001Black et al, , 2003Topolska et al, 2004a;O'Keeffe et al, 2005;Sanders et al, 2005;Gilson et al, 2006;). GPI-anchored proteins are preferentially incorporated into detergent resistant microdomains (DRMs) where they are proposed to function as distinct components within lipid bilayers and are thought to participate in receptor signaling, signal transduction and membrane sorting in a variety of eukaryotic cells.…”

Section: Introductionmentioning

confidence: 99%

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Plasmodium falciparum Pf34, a novel GPI-anchored rhoptry protein found in detergent-resistant microdomains

Proellocks

Kovacevic

Ferguson

et al. 2007

International Journal for Parasitology

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Apicomplexan parasites are characterised by the presence of specialised organelles, such as rhoptries, located at the apical end of invasive forms that play an important role in invasion of the host cell and formation of the parasitophorous vacuole. In this study, we have characterised a novel Plasmodium falciparum rhoptry protein, Pf34, encoded by a single exon gene located on chromosome 4 and expressed as a 34 kDa protein in mature asexual stage parasites. Pf34 is expressed later in the life cycle than the previously described rhoptry protein, Rhoptry Associated Membrane Antigen (RAMA). Orthologues of Pf34 are present in other Plasmodium species and a potential orthologue has also been identified in Toxoplasma gondii. Indirect immunofluorescence assays show that Pf34 is located at the merozoite apex and localises to the rhoptry neck. Pf34, previously demonstrated to be glutathione-S-transferase (GPI)-anchored (Gilson et al., 2006, Identification and stoichiometry of GPI-anchored membrane proteins of the human malaria parasite Plasmodium falciparum. Mol Cell Proteomics, 1286-1299), is associated with parasite-derived detergent-resistant microdomains (DRMs). Pf34 is carried into the newly invaded ring, consistent with a role for Pf34 in the formation of the parasitophorous vacuole. Pf34 is exposed to the human immune system during infection and is recognised by human immune sera collected from residents of malaria endemic areas of Vietnam and Papua New Guinea.

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Section: Plasmodium Falciparum Parasitesmentioning

confidence: 99%

Section: Genomic Sequences Molecular Cloning and Analysismentioning

confidence: 99%

Section: Recombinant Protein Expression and Production Of Polyclonal mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Plasmodium falciparum Pf34, a novel GPI-anchored rhoptry protein found in detergent-resistant microdomains

Proellocks

Kovacevic

Ferguson

et al. 2007

International Journal for Parasitology

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“…Recombinant proteins (100 ng) were fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) on 12% polyacrylamide gels and blotted as described previously (2). Recombinant fragments A and B of merozoite surface protein 4 (MSP4) were kindly provided by Lina Wang.…”

Section: Ethical Committeesmentioning

confidence: 99%

Associations between Responses to the Rhoptry-Associated Membrane Antigen of Plasmodium falciparum and Immunity to Malaria Infection

et al. 2004

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Rhoptry proteins participate in the invasion of red blood cells by merozoites during the malaria parasite's asexual-stage cycle. Interference with the rhoptry protein function has been shown to prevent invasion, and three rhoptry proteins have been suggested as potential components of a vaccine against malaria. Rhoptryassociated membrane antigen (RAMA) is a 170-kDa protein of Plasmodium falciparum which is processed to a 60-kDa mature form in the rhoptries. p60/RAMA is discharged from rhoptries of free merozoites and binds to the red-cell membrane before being internalized to form part of the parasitophorous vacuole of the newly developing ring. We examined the range of anti-RAMA responses in individuals living in an area of endemicity for malaria and determined its association with clinical immunity. RAMA is immunogenic during infections, and at least three epitopes within RAMA are recognized by hyperimmune sera in immunoblots. Sera from individuals living in a region of Vietnam where malaria is endemic possessed strong antibody responses toward two C-terminal regions of RAMA. Cytophilic antibody isotypes (immunoglobulin G1 [IgG1] and IgG3) predominated in humoral responses to both C-terminal epitopes. Acute episodes of P. falciparum infection result in significant boosting of levels of antibody to an epitope at the extreme C terminus of RAMA that harbors the red-cell-binding domain. Immunity to P. falciparum infection was linked to elevated levels of IgG3 responses to this functional domain of RAMA, suggesting that the region may contain a protective epitope useful for inclusion in a multiepitope vaccine against malaria.Plasmodium falciparum malaria is responsible for Ͼ2 million deaths each year. With the increasing resistance of Plasmodium parasites to antimalarial drugs and of the Anopheles mosquito vector to commonly available insecticides, an effective vaccine that would protect nonimmune individuals from death would be valuable. The life cycle of malaria parasites is quite complex and provides a number of potential vaccine targets. Several proteins expressed by P. falciparum during the erythrocytic stages are being investigated as candidates for a subunit vaccine, among them rhoptry-associated proteins. The most important immune response for immunity to asexual-stage infection is believed to be humoral, although cell-mediated responses may also contribute to immunity.Rhoptries are intracellular organelles of malaria parasites involved in the invasion of red blood cells (RBCs) by Plasmodium merozoites. Although their contents are only transiently accessible to antibodies, seroepidemiological studies have demonstrated the development of antibody responses to the rhoptry proteins RhopH3, RAP1, and RAP2 following infection (8,12,20,23). In vitro growth inhibition assays have indicated that antibodies directed against the RAP1 and RAP2 proteins have inhibitory effects on P. falciparum growth in in vitro culture (6,9,14,18). Moreover, immunization of Saimiri monkeys with RAP1 protected the animals from a lethal...

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Molecular basis of erythrocyte invasion byPlasmodiummerozoites

Gaur

Chitnis

Chauhan

2016

Advances in Malaria Research

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Merozoite surface protein 8 of Plasmodium falciparum contains two epidermal growth factor-like domains

Cited by 75 publications

References 33 publications

Plasmodium falciparum Pf34, a novel GPI-anchored rhoptry protein found in detergent-resistant microdomains

Plasmodium falciparum Pf34, a novel GPI-anchored rhoptry protein found in detergent-resistant microdomains

Associations between Responses to the Rhoptry-Associated Membrane Antigen of Plasmodium falciparum and Immunity to Malaria Infection

Molecular basis of erythrocyte invasion byPlasmodiummerozoites

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