scholarly journals Proteomic analysis revealed alterations of the Plasmodium falciparum metabolism following salicylhydroxamic acid exposure

2011 ◽  
pp. 109
Author(s):  
Marylin Torrentino-Madamet ◽  
Lionel Almeras ◽  
Travaille ◽  
Sinou ◽  
Pophillat ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Proteomic Analysis ◽  
Acid Exposure ◽  
Salicylhydroxamic Acid

scholarly journals Proteomic analysis of Plasmodium falciparum histone deacetylase 1 complex proteins

2019 ◽  
Vol 198 ◽  
pp. 7-16 ◽  
Author(s):  
Jessica A. Engel ◽  
Emma L. Norris ◽  
Paul Gilson ◽  
Jude Przyborski ◽  
Addmore Shonhai ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Histone Deacetylase ◽  
Proteomic Analysis ◽  
Histone Deacetylase 1

scholarly journals Proteomic analysis of Plasmodium falciparum parasites from patients with cerebral and uncomplicated malaria

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Gwladys I. Bertin ◽  
Audrey Sabbagh ◽  
Nicolas Argy ◽  
Virginie Salnot ◽  
Sem Ezinmegnon ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Proteomic Analysis ◽  
Uncomplicated Malaria

scholarly journals Proteomic analysis of Plasmodium falciparum response to isocryptolepine derivative

PLoS ONE ◽  
2019 ◽  
Vol 14 (8) ◽  
pp. e0220871 ◽  
Author(s):  
Kitiya Rujimongkon ◽  
Mathirut Mungthin ◽  
Jumreang Tummatorn ◽  
Sumate Ampawong ◽  
Poom Adisakwattana ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Proteomic Analysis

scholarly journals Global proteomic analysis of prenylated proteins in Plasmodium falciparum using an alkyne-modified isoprenoid analogue

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Kiall F. Suazo ◽  
Chad Schaber ◽  
Charuta C. Palsuledesai ◽  
Audrey R. Odom John ◽  
Mark D. Distefano
Keyword(s):  
Plasmodium Falciparum ◽  
Proteomic Analysis ◽  
Prenylated Proteins

scholarly journals Alternative Oxidase Inhibitors Potentiate the Activity of Atovaquone against Plasmodium falciparum

1999 ◽  
Vol 43 (3) ◽  
pp. 651-654 ◽  
Author(s):  
Anina D. Murphy ◽  
Naomi Lang-Unnasch
Keyword(s):  
Plasmodium Falciparum ◽  
Oxygen Consumption ◽  
Alternative Oxidase ◽  
Inhibitory Concentration ◽  
Oxidase Inhibitor ◽  
Dependent Manner ◽  
Fractional Inhibitory Concentration ◽  
Respiratory Pathway ◽  
Salicylhydroxamic Acid

ABSTRACT Recent evidence suggests that the malaria parasite Plasmodium falciparum utilizes a branched respiratory pathway including both a cytochrome chain and an alternative oxidase. This branched respiratory pathway model has been used as a basis for examining the mechanism of action of two antimalarial agents, atovaquone and proguanil. In polarographic assays, atovaquone immediately reduced the parasite oxygen consumption rate in a concentration-dependent manner. This is consistent with its previously described role as an inhibitor of the cytochrome bc1complex. Atovaquone maximally inhibited the rate of P. falciparum oxygen consumption by 73% ± 10%. At all atovaquone concentrations tested, the addition of the alternative oxidase inhibitor, salicylhydroxamic acid, resulted in a further decrease in the rate of parasite oxygen consumption. At the highest concentrations of atovaquone tested, the activities of salicylhydroxamic acid and atovaquone appear to overlap, suggesting that at these concentrations, atovaquone partially inhibits the alternative oxidase as well as the cytochrome chain. Drug interaction studies with atovaquone and salicylhydroxamic acid indicate atovaquone’s activity against P. falciparum in vitro is potentiated by this alternative oxidase inhibitor, with a sum fractional inhibitory concentration of 0.6. Propyl gallate, another alternative oxidase inhibitor, also potentiated atovaquone’s activity, with a sum fractional inhibitory concentration of 0.7. Proguanil, which potentiates atovaquone activity in vitro and in vivo, had a small effect on parasite oxygen consumption in polarographic assays when used alone or in the presence of atovaquone or salicylhydroxamic acid. This suggests that proguanil does not potentiate atovaquone by direct inhibition of either branch of the parasite respiratory chain.

Ultrastructural observations on the in vitro cytoadherence of Plasmodium falciparum infected red blood cells

1990 ◽  
Vol 48 (3) ◽  
pp. 914-915
Author(s):  
D.J.P. Ferguson ◽  
A.R. Berendt ◽  
J. Tansey ◽  
K. Marsh ◽  
C.I. Newbold
Keyword(s):  
Plasmodium Falciparum ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Umbilical Vein ◽  
Cell Types ◽  
Amelanotic Melanoma ◽  
Cytoplasmic Process ◽  
Umbilical Vein Endothelial Cells

In human malaria, the most serious clinical manifestation is cerebral malaria (CM) due to infection with Plasmodium falciparum. The pathology of CM is thought to relate to the fact that red blood cells containing mature forms of the parasite (PRBC) cytoadhere or sequester to post capillary venules of various tissues including the brain. This in vivo phenomenon has been studied in vitro by examining the cytoadherence of PRBCs to various cell types and purified proteins. To date, three Ijiost receptor molecules have been identified; CD36, ICAM-1 and thrombospondin. The specific changes in the PRBC membrane which mediate cytoadherence are less well understood, but they include the sub-membranous deposition of electron-dense material resulting in surface deformations called knobs. Knobs were thought to be essential for cytoadherence, lput recent work has shown that certain knob-negative (K-) lines can cytoadhere. In the present study, we have used electron microscopy to re-examine the interactions between K+ PRBCs and both C32 amelanotic melanoma cells and human umbilical vein endothelial cells (HUVEC).We confirm previous data demonstrating that C32 cells possess numerous microvilli which adhere to the PRBC, mainly via the knobs (Fig. 1). In contrast, the HUVEC were relatively smooth and the PRBCs appeared partially flattened onto the cell surface (Fig. 2). Furthermore, many of the PRBCs exhibited an invagination of the limiting membrane in the attachment zone, often containing a cytoplasmic process from the endothelial cell (Fig. 2).

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