Biomedical subjects
Publications and source records attributed to F Klotz.
The authors report a new case of this rare and not well-know disease, the eosinophilic gastroenteritis. The medical imaging techniques allowed to correlate all the clinical signs to the observed parietal lesions.
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A group of 300 young European adults visiting Gabon for relatively short periods was surveyed monthly for malaria from a parasitological, clinical, immunological, hematological point of view. The regular increase of fevers due to malaria from 1984 to 1988 and the multiplication of cases of amino-4-quinoline resistance in the plasmodial parasites call for new prophylactic considerations for this group residing in this heavily malaria infested area.
The authors report the case of a young 16 year-old woman from Gabon hospitalized because of edemas. The laboratory tests show a hypoproteinemia of 32 g/l with hypoalbuminemia of 9.4 g/l. After ruling out a renal, cardiac or hepatic etiology as well as malnutrition, the endoscopic exploration of the G.I tract, performed because of abdominal pain, enables to make the diagnosis: malignant, non-Hodgkin gastric lymphoma, confirmed by biopsies during the procedure. Edemas and hypoproteinemia were related to an exudative enteropathy secondary to ulcerations of the gastric mucosa.
The profound changes in the morphology, antigenicity, and functional properties of the host erythrocyte membrane induced by intraerythrocytic parasites of the human malaria Plasmodium falciparum are poorly understood at the molecular level. We have used mouse mAbs to identify a very large malarial protein (Mr approximately 300,000) that is exported from the parasite and deposited on the cytoplasmic face of the erythrocyte membrane. This protein is denoted P. falciparum erythrocyte membrane protein 2 (Pf EMP 2). The mAbs did not react with the surface of intact infected erythrocytes, nor was Pf EMP 2 accessible to exogenous proteases or lactoperoxidase-catalyzed radioiodination of intact cells. The mAbs also had no effect on in vitro cytoadherence of infected cells to the C32 amelanotic melanoma cell line. These properties distinguish Pf EMP 2 from Pf EMP 1, the cell surface malarial protein of similar size that is associated with the cytoadherent property of P. falciparum-infected erythrocytes. The mAbs did not react with Pf EMP 1. In one strain of parasite there was a significant difference in relative mobility of the 125I-surface-labeled Pf EMP 1 and the biosynthetically labeled Pf EMP 2, further distinguishing these proteins. By cryo-thin-section immunoelectron microscopy we identified organelles involved in the transit of Pf EMP through the erythrocyte cytoplasm to the internal face of the erythrocyte membrane where the protein is associated with electron-dense material under knobs. These results show that the intraerythrocytic malaria parasite has evolved a novel system for transporting malarial proteins beyond its own plasma membrane, through a vacuolar membrane and the host erythrocyte cytoplasm to the erythrocyte membrane, where they become membrane bound and presumably alter the properties of this membrane to the parasite's advantage.
Immune sera from mice immunized with the 143/140 kDa protein have been shown to partially block erythrocyte invasion by P. knowlesi merozoites. Therefore, immunoelectron microscopy utilizing ultracryomicrotomy, antibody to 143/140 kDa protein, and protein A gold particles were used to determine the precise localization of this protein in malarial parasites. Gold particles were not seen associated with young trophozoites but appeared in the parasite cytoplasm as the parasites grew to multi-nucleate schizonts. In presegmenter-schizonts, gold particles were associated with the well-developed endoplasmic reticulum, the parasite plasma membrane, and the parasitophorous vacuole membrane. The surface of merozoites was covered with gold particles. Maurer's clefts, which appeared in Plasmodium infected erythrocytes, were also associated with gold particles. These observations suggest that 143/140 kDa protective malarial proteins may be synthesized in the endoplasmic reticulum of P. knowlesi schizonts before being transported to the surface of the schizonts and merozoites. Shedding of the merozoite surface coat may be responsible for the presence of the 143/140 kDa proteins in the parasitophorous vacuole and Maurer's clefts.
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