A repetitive antigen of Plasmodium falciparum that is homologous to heat shock protein 70 of Drosophila melanogaster.

Bianco, A. E.; Favaloro, Jenny M.; Burkot, Thomas R.; Culvenor, Janetta G.; Crewther, Pauline E.; Brown, Graham V.; Anders, Robin F.; Coppel, Ross L.; Kemp, David J.

doi:10.1073/pnas.83.22.8713

Cited by 109 publications

(50 citation statements)

References 28 publications

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“…A number of highly immunogenic proteins with repeating elements have been described in parasitic protozoa (2,8,9,15,20,28,32,34,37,42). cDNAs for some of these proteins have been isolated by using sera from infected hosts.…”

Section: Discussionmentioning

confidence: 99%

Tandemly repeated exons encode 81-base repeats in multiple, developmentally regulated Schistosoma mansoni transcripts.

Davis¹,

Davis²,

Carroll³

et al. 1988

Mol. Cell. Biol.

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The adult Schistosoma mansoni cDNA clone 10-3 encodes an antigen that is recognized by sera from infected humans. We characterized multiple developmentally regulated transcripts homologous to the 10-3 cDNA and portions of the complex genomic loci encoding those transcripts. Transcripts of approximately 950, 870, and 780 nucleotides were expressed in adults, whereas only the 780-nucleotide transcript was observed in the larval stage. These transcripts were highly similar, containing variable numbers of identical direct tandem repeats of 81 bases. Although the sequence of the repeating elements and sequences 3' to them were identical in ali the transcripts, sequences 5' of the repeating elements exhibited variations, including a 27-base insertion, alternative start sites for transcription, and alternate 5' exon usage. These transcripts appeared to be derived in part by the developmentally controlled alternative splicing of small exons and the use of alternative transcription initiation sites from the one or two complex loci of at least 40 kilobase pairs. Each 81-base repeat in the transcripts was encoded by three dispersed 27-base-pair exons. These 27-base-pair exons were contained within highly conserved, reiterated 3-kilobase-pair genomic tandem arrays.

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Section: Discussionmentioning

confidence: 99%

Tandemly repeated exons encode 81-base repeats in multiple, developmentally regulated Schistosoma mansoni transcripts.

Davis¹,

Davis²,

Carroll³

et al. 1988

Mol. Cell. Biol.

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“…Rabbit antisera were purified on affinity columns using the recombinant protein as ligand. Other antibodies used in immuno-detection were rabbit anti-EBA-175 (7) and anti-HSP70 antibodies (27).…”

Section: Methodsmentioning

confidence: 99%

A Novel Erythrocyte Binding Antigen-175 Paralogue fromPlasmodium falciparum Defines a New Trypsin-resistant Receptor on Human Erythrocytes

Gilberger¹,

Thompson

Triglia

et al. 2003

Journal of Biological Chemistry

178

149

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Plasmodium falciparum is the causative agent of the most lethal form of malaria in humans and is responsible for more than 2 million deaths per year. Because of the increasing resistance of this parasite toward the commonly used antimalarial drugs there is an urgent need for the development of a vaccine (1, 2). P. falciparum invades erythrocytes and develops and expands within this host cell followed by release of invasive merozoite forms into the blood stream. The merozoite is exposed to the host immune system, and proteins involved in the invasion process are potential vaccine candidates.

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“…Dual-color fluorescence images were captured using a digital camera and fluorescence microscope (Zeiss, Gottingen, Germany). The DNA stain DAPI (4Ј,6Ј-diamidino-2-phenylindole) was included in the second antibody incubation step (8).…”

Section: Methodsmentioning

confidence: 99%

Independent Translocation of Two Micronemal Proteins in Developing Plasmodium falciparum Merozoites

et al. 2002

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Apical membrane antigen 1 of Plasmodium falciparum (PfAMA1) contains an N-terminal propeptide that is removed prior to the translocation of the mature protein onto the merozoite surface. We localized unprocessed PfAMA1 to the microneme organelles of the intraerythrocytic schizont. The results have suggested that the processed form of PfAMA1 translocates from the microneme compartment independently of another microneme protein, EBA175, which is also involved in the invasion of human erythrocytes.The clinical symptoms of malaria infection result from exponential expansion of parasite numbers during the asexual erythrocytic phase of the Plasmodium life cycle. The precise molecular events mediating erythrocyte invasion are not fully understood, but its rapid nature indicates that it is a tightly controlled process involving specific receptor-ligand interactions between host and parasite (reviewed in reference 7). Molecules located in the apical organelles, as well as those found on the merozoite surface, are believed to play crucial roles.Extracellular merozoites form an initially reversible attachment to circulating erythrocytes through molecules in the surface coat filaments of the parasite (18). Attached merozoites then reorient to bring the anterior apical pole into alignment with the erythrocyte plasma membrane. Next, an irreversible adhesion, the tight junction, forms between host and parasite membranes, coinciding with an indentation in the erythrocyte membrane and extrusion of the contents of the apical organelles (2, 6). Entry into the host cell is accomplished by posterior movement of the tight junction around the merozoite circumference. When the newly formed parasitophorous vacuole is sealed around the body of the merozoite, invasion is complete.In Plasmodium falciparum, proteins belonging to the erythrocyte binding protein family have been identified in the micronemes of developing and free merozoites. The best characterized of these is EBA175, which binds to sialic acid residues present on glycophorin A, a highly abundant erythrocyte surface protein (38).Proteins found in association with the merozoite surface and apical organelles offer considerable potential as components in a malaria vaccine (4). One of the leading candidates for inclusion in a subunit vaccine is apical membrane antigen 1 (AMA1). This molecule has been demonstrated to induce protection against parasite challenge in various animal model systems (3,12,15).P. falciparum AMA1 (PfAMA1) is synthesized in segmenting schizonts as a precursor protein of around 83 kDa, which is then processed N terminally to a 62-kDa form (13). This protein has the structural features of a type 1 integral membrane protein, with short transmembrane and cytoplasmic tail domains. It has previously been localized by immunofluorescence microscopy to the apical organelles and the surface of the merozoite (32), and immunoelectron microscopy (immuno-EM) suggested it to be resident in the rhoptry neck (13). The processed form of AMA1 is thought to translocate to the m...

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A repetitive antigen of Plasmodium falciparum that is homologous to heat shock protein 70 of Drosophila melanogaster.

Cited by 109 publications

References 28 publications

Tandemly repeated exons encode 81-base repeats in multiple, developmentally regulated Schistosoma mansoni transcripts.

Tandemly repeated exons encode 81-base repeats in multiple, developmentally regulated Schistosoma mansoni transcripts.

A Novel Erythrocyte Binding Antigen-175 Paralogue fromPlasmodium falciparum Defines a New Trypsin-resistant Receptor on Human Erythrocytes

Independent Translocation of Two Micronemal Proteins in Developing Plasmodium falciparum Merozoites

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