Nutritional Requirements for in vitro Cultivation of a Simian Malarial Parasite, Plasmodium knowlesi

1969 ◽  
Vol 134 (9) ◽  
pp. 927-938 ◽  
Author(s):  
W. A. Siddiqui ◽  
J. V. Schnell ◽  
Q. M. Geiman
Keyword(s):  
Plasmodium Knowlesi ◽  
Malarial Parasite ◽  
Nutritional Requirements ◽  
In Vitro Cultivation ◽  
Parasite Plasmodium

scholarly journals Localization of ferrochelatase in Plasmodium falciparum

2004 ◽  
Vol 384 (2) ◽  
pp. 429-436 ◽  
Author(s):  
Sundaramurthy VARADHARAJAN ◽  
B. K. Chandrashekar SAGAR ◽  
Pundi N. RANGARAJAN ◽  
Govindarajan PADMANABAN
Keyword(s):  
Plasmodium Falciparum ◽  
De Novo ◽  
Enzymic Activity ◽  
Malarial Parasite ◽  
Parasite Genome ◽  
Marker Proteins ◽  
Parasite Plasmodium ◽  
Theoretical Predictions ◽  
Parasite Plasmodium Falciparum

Our previous studies have demonstrated de novo haem biosynthesis in the malarial parasite (Plasmodium falciparum and P. berghei). It has also been shown that the first enzyme of the pathway is the parasite genome-coded ALA (δ-aminolaevulinate) synthase localized in the parasite mitochondrion, whereas the second enzyme, ALAD (ALA dehydratase), is accounted for by two species: one species imported from the host red blood cell into the parasite cytosol and another parasite genome-coded species in the apicoplast. In the present study, specific antibodies have been raised to PfFC (parasite genome-coded ferrochelatase), the terminal enzyme of the haem-biosynthetic pathway, using recombinant truncated protein. With the use of these antibodies as well as those against the hFC (host red cell ferrochelatase) and other marker proteins, immunofluorescence studies were performed. The results reveal that P. falciparum in culture manifests a broad distribution of hFC and a localized distribution of PfFC in the parasite. However, PfFC is not localized to the parasite mitochondrion. Immunoelectron-microscopy studies reveal that PfFC is indeed localized to the apicoplast, whereas hFC is distributed in the parasite cytoplasm. These results on the localization of PfFC are unexpected and are at variance with theoretical predictions based on leader sequence analysis. Biochemical studies using the parasite cytosolic and organellar fractions reveal that the cytosol containing hFC accounts for 80% of FC enzymic activity, whereas the organellar fraction containing PfFC accounts for the remaining 20%. Interestingly, both the isolated cytosolic and organellar fractions are capable of independent haem synthesis in vitro from [4-14C]ALA, with the cytosol being three times more efficient compared with the organellar fraction. With [2-14C]glycine, most of the haem is synthesized in the organellar fraction. Thus haem is synthesized in two independent compartments: in the cytosol, using the imported host enzymes, and in the organellar fractions, using the parasite genome-coded enzymes.

Nuclear and mitochondrial DNA of the primate malarial parasite Plasmodium knowlesi

1985 ◽  
Vol 14 (2) ◽  
pp. 199-209 ◽  
Author(s):  
Donald H. Williamson ◽  
Robert J.M. Wilson ◽  
Paul A. Bates ◽  
Shirley McCready ◽  
Francine Perler ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Plasmodium Knowlesi ◽  
Malarial Parasite ◽  
Parasite Plasmodium

scholarly journals An intracellular simian malarial parasite (Plasmodium knowlesi) induces stage-dependent alterations in membrane phospholipid organization of its host erythrocyte

1987 ◽  
Vol 246 (1) ◽  
pp. 103-108 ◽  
Author(s):  
P Joshi ◽  
G P Dutta ◽  
C M Gupta
Keyword(s):  
Developmental Stages ◽  
Plasmodium Knowlesi ◽  
Membrane Phospholipid ◽  
Malarial Parasite ◽  
Merocyanine 540 ◽  
Parasite Plasmodium ◽  
Normal Monkey ◽  
Infected Cells ◽  
Membrane Isolation ◽  
Different Sources

The membrane phospholipid organization in monkey erythrocytes harbouring different developmental stages of the simian malarial parasite Plasmodium knowlesi was studied using phospholipase A2 from two different sources and Merocyanine 540 as the external-membrane probes. Experiments were done to confirm that the phospholipases did not penetrate into the infected cells or hydrolyse phospholipids during membrane isolation. The parasite-free erythrocyte membrane was isolated by differential centrifugation or by using the cationic beads Affi-Gel 731. The purity of the membranes was established by optical and electron microscopy, and by assaying the parasite-specific enzyme glutamate dehydrogenase. About 10% of the phosphatidylethanolamine and none of phosphatidylserine were hydrolysed by the phospholipases in intact normal monkey erythrocytes. However, accessibility of these aminophospholipids to the enzymes was significantly enhanced in the infected cells under identical conditions. The degree of this enhancement depended on the developmental stage of the intracellular parasite, but not on the parasitaemia levels in the infected monkeys, and increased with the parasite growth inside the cells. Analogously, Merocyanine 540 was found to label the trophozoite- or schizont-infected erythrocytes, but not the ring-infected or normal cells. These results demonstrate that the intracellular malarial parasite produces stage-dependent alterations in the membrane phospholipid organization of its host erythrocyte.

scholarly journals STUDIES ON MALARIAL PARASITES

1946 ◽  
Vol 84 (6) ◽  
pp. 583-606 ◽  
Author(s):  
Quentin M. Geiman ◽  
Christian B. Anfinsen ◽  
Ralph W. McKee ◽  
Richard A. Ormsbee ◽  
Eric G. Ball
Keyword(s):  
Host Cell ◽  
Macaca Mulatta ◽  
Blood Cells ◽  
Plasmodium Knowlesi ◽  
Average Rate ◽  
In Vitro Cultivation ◽  
Biochemical Studies ◽  
Differential Sedimentation ◽  
Physical And Chemical

1. Methods of recovering adequate amounts of Plasmodium knowlesi from the monkey (Macaca, mulatta) for biochemical studies and in vitro cultivation are described. Concentrates of red blood cells parasitized with P. knowlesi can be obtained by differential sedimentation of parasitized blood because of physical and chemical changes produced by the parasites in the host cell and the plasma of the blood. 2. Two different techniques, the rocker-dilution and the rocker-perfusion methods, are described for the cultivation of malarial parasites. Details of the apparatus, assembly, and sterilization are given, as well as methods of counting and evaluating parasites. 3. In a series of 235 control experiments for 20 to 24 hours using three types of apparatus, the average rate of multiplication was 3.9. Each technique has specific value for studying the various aspects of metabolism, nutrition, and the action of antimalarial drugs.

In vitro Ookinete Development of the Rodent Malarial Parasite, Plasmodium berghei

1974 ◽  
Vol 60 (5) ◽  
pp. 819 ◽  
Author(s):  
Maria C. Rosales-Ronquillo ◽  
Paul H. Silverman
Keyword(s):  
Plasmodium Berghei ◽  
Malarial Parasite ◽  
Parasite Plasmodium

scholarly journals THE AGGLUTINATION OF PLASMODIUM KNOWLESI BY IMMUNE SERUM

1938 ◽  
Vol 67 (6) ◽  
pp. 857-870 ◽  
Author(s):  
Monroe D. Eaton
Keyword(s):  
Plasmodium Knowlesi ◽  
Immune Serum ◽  
Malarial Parasite ◽  
Passive Immunity ◽  
Malarial Infection ◽  
Parasite Plasmodium ◽  
Plasmodium Inui

A specific agglutination of Plasmodium knowlesi detectable both by macroscopic and by microscopic methods is described. Agglutinins for Plasmodium knowlesi appear in the sera of monkeys between 15 and 45 days after the onset of the infection and become progressively stronger as the malarial infection gradually subsides. Agglutinins persist in the sera of chronically infected animals for a year or longer. The sera of animals which have been repeatedly superinfected agglutinate parasites at dilutions as high as 1:1,000. Sera from normal monkeys, from monkeys acutely ill with malaria, and from monkeys chronically infected with a different species of malarial parasite (Plasmodium inui) do not agglutinate Plasmodium knowlesi. Immune serum agglutinates mature intracellular or extracellular parasites but does not agglutinate unparasitized cells or cells containing immature parasites. The relation of these observations to the mechanism of active and passive immunity in monkey malaria is discussed.

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