A Plasmodium falciparum protein located in Maurer's clefts underneath knobs and protein localization in association with Rhop-3 and SERA in the intracellular network of infected erythrocytes |
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| Authors: | T Y Sam-Yellowe H Fujioka M Aikawa T Hall J A Drazba |
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| Institution: | (1) Cleveland State University, Department of Biological, Geological and Environmental Sciences, 2399 Euclid Avenue, SI 219, Cleveland, OH 44115, USA e-mail: ilibot@hotmail.com, US;(2) Case Western Reserve University, Institute of Pathology, 2085 Adelbert Road, Cleveland, OH 44106, USA, US;(3) The Research Institute of Medical Sciences, Tokai University, Boseidai, Isehara, Kanagawa 259-11, Japan, JP;(4) Department of Immunology, The Walter Reed Army Institute of Research, 503 Robert Grant Avenue, Silver Spring, MD 20910, USA, US;(5) The Cleveland Clinic Foundation, Lerner Research Institute, Cleveland, OH 44195, USA, US |
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| Abstract: | We report on the characterization of monoclonal antibodies against Plasmodium falciparum schizonts, which recognize parasite proteins of 130 kDa and 20 kDa. The 130-kDa protein was released by alkaline sodium carbonate
treatment, suggesting that the protein is a peripheral membrane protein, while the 20-kDa protein remained associated with
the membranes following alkali treatment, suggesting it may be an integral membrane protein. Both proteins were localized
to large cytoplasmic vesicles within the cytoplasm of trophozoite and schizont-infected erythrocytes by immunofluorescence
assay and confocal microscopy. Both proteins colocalized with Bodipy-ceramide in trophozoite and immature schizont-infected
erythrocytes, but not in segmenters. The 130-kDa protein was localized by immunoelectron microscopy (IEM) to Maurer's clefts
underneath knobs in a knobby and cytoadherent (K+/C+) P. falciparum strain. No IEM reactivity was obtained in a knobless and non-cytoadherent (K−/C−) parasite strain. We investigated stage-specific protein expression and protein localization by indirect immunofluorescence
assay. Bodipy-ceramide colocalization assays with Rhop-3 and serine-rich antigen (SERA)-specific antibodies were performed.
A similar colocalization in trophozoites and schizonts was obtained using the rhoptry-specific antibody 1B9 reactive with
the 110-kDa Rhop-3 protein. In segmenters, unlike trophozoites and immature schizonts, there was no Bodipy-ceramide colocalization
with antibody 1B9. A difference in protein colocalization was seen using specific antibody 152.3F7.1.1, reactive with SERA.
Antibodies to SERA colocalized with Bodipy-ceramide in schizonts, including segmenters. Collectively the data suggest that
Rhop-3 transits through the intracellular network en route to the rhoptries and both vesicle-specific proteins may function
in the intracellular network.
Received: 4 January 2000 / Accepted: 9 August 2000 |
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| Keywords: | Plasmodium falciparum Cytoplasmic vesicles Knobs Longitudinal clefts Merozoites Malaria Maurer's clefts Parasitophorous vacuole membrane Protein-trafficking Rhoptry Rhop-3 Serine-rich antigen (SERA) Intracellular network |
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