Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0024530 (malaria)
 44,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

During the intermonsoon period from mid-September to mid-October 1986, wild-caught Anopheles balabacensis Baisas females were marked and released in a host-choice experiment. Association between capture and recapture of marked mosquitoes from human and bovid hosts and blood meal host identification of recaptured females were determined on a daily basis. Although the mark-recapture and blood meal data indicated behavioral heterogeneity between buffalo and human biters, restriction endonuclease fragment length polymorphism analysis revealed no differences in repeat sequence profiles. Doubly-marked recaptures strongly indicated a "learning" component involved in a separate host preference experiment. In a "habitat loyalty" experiment conducted in January 1987, females of An. balabacensis preferentially returned to the resting sites (indoor surfaces and exit traps) where they were first caught. Of nine isozyme loci found to be polymorphic, the genotypic frequencies of Esterase-3 and Isocitrate dehydrogenase-3 were different in "faithfully" endophilic and exophilic subpopulations. Genetic heterozygosity, as determined by polyacrylamide gel electrophoresis, was greater in exophilic than endophilic population components. These results confirm that genetic and learning components can significantly influence house resting and host seeking behavior and may contribute to local epidemiological patterns of malaria transmission observed in Sabah, Malaysia.
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PMID:Population genetic analysis of host seeking and resting behaviors in the malaria vector, Anopheles balabacensis (Diptera: Culicidae). 168 92

Erythrocytic stages of the malaria parasite Plasmodium falciparum rely on glycolysis for their energy supply and it is unclear whether they obtain energy via mitochondrial respiration albeit enzymes of the tricarboxylic acid (TCA) cycle appear to be expressed in these parasite stages. Isocitrate dehydrogenase (ICDH) is either an integral part of the mitochondrial TCA cycle or is involved in providing NADPH for reductive reactions in the cell. The gene encoding P. falciparum ICDH was cloned and analysis of the deduced amino-acid sequence revealed that it possesses a putative mitochondrial targeting sequence. The protein is very similar to NADP+-dependent mitochondrial counterparts of higher eukaryotes but not Escherichia coli. Expression of full-length ICDH generated recombinant protein exclusively expressed in inclusion bodies but the removal of 27 N-terminal amino acids yielded appreciable amounts of soluble ICDH consistent with the prediction that these residues confer targeting of the native protein to the parasites' mitochondrion. Recombinant ICDH forms homodimers of 90 kDa and its activity is dependent on the bivalent metal ions Mg2+ or Mn2+ with apparent Km values of 13 micro m and 22 micro m, respectively. Plasmodium ICDH requires NADP+ as cofactor and no activity with NAD+ was detectable; the for NADP+ was found to be 90 micro m and that of d-isocitrate was determined to be 40 micro m. Incubation of P. falciparum under exogenous oxidative stress resulted in an up-regulation of ICDH mRNA and protein levels indicating that the enzyme is involved in mitochondrial redox control rather than energy metabolism of the parasites.
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PMID:Isocitrate dehydrogenase of Plasmodium falciparum. 1269 90