Antigens of the erythrocytic stages of the human malaria parasite Plasmodium falciparum detected by monoclonal antibodies

Hall, Roger; McBride, Jana S.; Morgan, Gillian M.; Tait, Andrew; Zolg, J. Werner; Walliker, David; Scaife, John

doi:10.1016/0166-6851(83)90025-7

Cited by 126 publications

(72 citation statements)

References 23 publications

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“…Indirect immunofluorescence assays were performed as described previously (Hall et al 1983). Sodium R. G. Ridley and others 188 dodecyl sulphate polvacrvlamide gel electrophoresis (SDS-PAGE), using the method of Laemmli (1970), together with Western blotting analysis have also been previously described (Takacs & Staehli, 1987).…”

Section: Standard Techniquesmentioning

confidence: 99%

“…Purified mAb 2.13 (Hall et al 1983) was coupled to cyanogen bromide-activated Sepharose 4B (Pharmacia Ltd, Milton Keynes, UK) as recommended by the manufacturer. Cell pellets of bulk cultures of a P. falciparum isolate, Kl from Thailand (Thaithong & Beale, 1981) were harvested as previously described (Goman et al 1982) and stored at -70 °C until required.…”

Section: Affinity-purification Of Rap-1 Antigenmentioning

confidence: 99%

“…In fact, early studies on the rodent malarial parasite Plasmodium yoelii revealed a rhoptry antigen which could partially protect mice against malaria (Holder & Freeman, 1981). We have previously reported two monoclonal antibodies 2.13 and 7.12, which define an antigen, RAP-1 (rhoptry associated protein-1) associated with the rhoptries (Hall et al 1983). They both inhibit parasite growth in vitro (I.…”

Section: Introductionmentioning

confidence: 99%

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A rhoptry antigen ofPlasmodium falciparumis protective inSaimirimonkeys

Ridley¹,

Takács

Etlinger

et al. 1990

Parasitology

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SUMMARYA non-polymorphic antigen associated with the rhoptry organelles of Plasmodium falciparum has been purified by immunoaffinity chromatography. The antigen, RAP-1 (rhoptry associated protein-1), which is defined by monoclonal antibodies which inhibit parasite growth in vitro, is a multi-component antigen consisting of four major proteins of 80, 65, 42 and 40 kDa and two minor proteins of 77 and 70 kDa. These proteins were electro-eluted from preparative sodium dodecyl sulphate polyacrylamide gels and protected Saimiri sciureus monkeys from a lethal blood-stage infection of P. falciparum malaria. Sera from the protected animals recognized only proteins of the RAP-1 antigen when used to probe a Western blot of total parasite protein extract, confirming that RAP-1 is responsible for eliciting the protective immune response.

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Section: Standard Techniquesmentioning

confidence: 99%

Section: Affinity-purification Of Rap-1 Antigenmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A rhoptry antigen ofPlasmodium falciparumis protective inSaimirimonkeys

Ridley¹,

Takács

Etlinger

et al. 1990

Parasitology

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“…Processing occurs about the time merozoites are released from infected erythrocytes, and a series of transitory intermediates with molecular masses of about 153, 150, and 110 kDa appear (2). One of the final products has an Mr of 83 kDa (2,4,5) and possesses serotype-restricted epitopes (4,5). Other products of 50 (1), 42, and 19 kDa (3) have been identified; the 50-kDa antigen is glycosylated (1) and may be homologous with the 42-kDa antigen.…”

mentioning

confidence: 99%

“…Processing of gp195 produces at least three smaller products found on the surface of merozoites (3) and has been observed in at least six P. falciparum strains (1,2,4,5). Processing occurs about the time merozoites are released from infected erythrocytes, and a series of transitory intermediates with molecular masses of about 153, 150, and 110 kDa appear (2).…”

mentioning

confidence: 99%

Epitope map and processing scheme for the 195,000-dalton surface glycoprotein of Plasmodium falciparum merozoites deduced from cloned overlapping segments of the gene.

Lyon¹,

Geller²,

Haynes³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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DNA fragments from human malaria parasites were cloned into Xgtll to produce a genomic DNA expression library. A pool of monoclonal antibodies (mAbs) recognizing three domains of the 195-kDa major merozoite surface glycoprotein (gp195) reacted with seven clones expressing malaria antigens. mAbs recognizing the 83-kDa product of gp195 reacted with the clones, but mAbs recognizing a glycosylated 45-kDa and a nonglycosylated 45-kDa domain did not.Restriction enzyme mapping revealed that the clones contained overlapping segments encoding about 70% of the gene beginning at the 5' end and ending at an EcoRI restriction enzyme site 3.3 kilobase pairs downstream. The mAbs recognizing the 83-kDa domain reacted differently with the clones, allowing the mapping of three epitopes, one of which was repetitive. Affinity-purified antibodies were selected from immune monkey serum with recombinant expression proteins adsorbed to nitrocellulose filters. When used to probe electrophoretic immunoblots of parasite extracts, these antigen-selected antibodies reacted with specific sets of processed products of gp195, including those associated with the 83-and the nonglycosylated 45-kDa domains. This information, combined with the mAb epitope map, allowed a tentative scheme for processing gp195 from the Camp strain to be proposed.Merozoites from Plasmodium falciparum malaria parasites have, as major components of their surface, a 195-kDa glycoprotein (gp195) (1) and polypeptides derived from this protein as a result of processing by proteases (2, 3). Processing of gp195 produces at least three smaller products found on the surface of merozoites (3) and has been observed in at least six P. falciparum strains (1,2,4,5). Processing occurs about the time merozoites are released from infected erythrocytes, and a series of transitory intermediates with molecular masses of about 153, 150, and 110 kDa appear (2). One of the final products has an Mr of 83 kDa (2, 4, 5) and possesses serotype-restricted epitopes (4, 5). Other products of 50 (1), 42, and 19 kDa (3) have been identified; the 50-kDa antigen is glycosylated (1) and may be homologous with the 42-kDa antigen. gp195 and its proteolytic products are recognized on intact merozoites by growth-inhibitory immune sera (6) and may be good candidates for vaccine development (1, 7-10).The molecular cloning and expression of parasite antigens in bacterial systems allows the preparation of sufficient amounts of pure antigen to conduct immunological and immunochemical studies. The cloning from cDNA of the complete structural gene encoding gp195 has been reported (11), and cDNA clones encoding 0.21 (7) and 1.1 (12) kilobase pairs (kb) of the gp195 gene have been reported as well. We report the cloning of a 3.6-kb portion of gp195 genomic DNA from the Camp strain and propose a scheme for processing the Camp strain protein, locating major proteolytic products and the positions of epitopes recognized by monoclonal antibodies (mAbs).MATERIALS AND METHODS Culture of P. falciparum. Camp strain...

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Plasmodium falciparum‐specific human T cell clones: recognition of different parasite antigens

et al. 1987

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T lymphocyte clones specific for malarial (Plasmodium falciparum) blood stage antigens were obtained from acutely infected patients or from donors living in a malaria-endemic area of West Africa. Thirty-four clones carrying the CD4 antigen, and one CD8+ clone, were tested in a proliferation assay for their capacity to recognize P. falciparum isolates of different geographical origins. Only one clone distinguished between different parasite isolates (it failed to react with a parasite isolate originating from East Africa, but did recognize West African and Asian isolates). All of the clones responded well to intact erythrocytes containing viable parasites, but some responded poorly to extracts of parasitized cells. Eight of 19 clones studied (all CD4+) recognized parasite antigens which had characteristic mobilities in sodium dodecyl sulfate-containing polyacrylamide gels. The antigens had apparent molecular weights of about 20,000, 35,000, 40,000, 120,000, 150,000-200,000 and 200,000. These results (together with a previous report of two clones recognizing an antigen of molecular weight about 50,000, Sinigaglia and Pink, EMBO J. 1985. 4:3819) show that T cells in infected individuals react with at least 6 different parasite proteins.

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Antigens of the erythrocytic stages of the human malaria parasite Plasmodium falciparum detected by monoclonal antibodies

Cited by 126 publications

References 23 publications

A rhoptry antigen ofPlasmodium falciparumis protective inSaimirimonkeys

A rhoptry antigen ofPlasmodium falciparumis protective inSaimirimonkeys

Epitope map and processing scheme for the 195,000-dalton surface glycoprotein of Plasmodium falciparum merozoites deduced from cloned overlapping segments of the gene.

Plasmodium falciparum‐specific human T cell clones: recognition of different parasite antigens

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