scholarly journals Plasmodium falciparum Protein Exported in Erythrocyte and Mechanism Resistance to Malaria

Malaria ◽  
2019 ◽  
Author(s):  
Neyder Contreras-Puentes
Keyword(s):  
Plasmodium Falciparum ◽  
Falciparum Protein

Dynamical Basis of Allosteric Activation for the Plasmodium falciparum Protein Kinase G

2021 ◽  
Author(s):  
Jinfeng Huang ◽  
Jung Ah Byun ◽  
Bryan VanSchouwen ◽  
Philipp Henning ◽  
Friedrich W. Herberg ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Kinase ◽  
Protein Kinase G ◽  
Allosteric Activation ◽  
Falciparum Protein

Cloning of a Ca(2+)-ATPase gene of Plasmodium falciparum and comparison with vertebrate Ca(2+)-ATPases

1993 ◽  
Vol 104 (4) ◽  
pp. 1129-1136 ◽  
Author(s):  
M. Kimura ◽  
Y. Yamaguchi ◽  
S. Takada ◽  
K. Tanabe
Keyword(s):  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phosphorylation Site ◽  
Genomic Libraries ◽  
Atpase Gene ◽  
Binding Regions ◽  
Cloned Gene ◽  
Falciparum Protein

A Ca(2+)-ATPase gene was cloned from the genomic libraries of Plasmodium falciparum. From the deduced amino acid sequence of the gene, a 139 kDa protein with a total of 1228 amino acids was predicted. Sequence of a partial cDNA clone of the gene identified two introns near the 3′-end at the regions identical to the regions assumed for the Ca(2+)-ATPase gene of P. yoelii, a rodent malaria species. As compared with a variety of Ca(2+)-ATPases, the P. falciparum Ca(2+)-ATPase had the highest amino acid sequence homology (78%) to the P. yoelii Ca(2+)-ATPase, moderate homology (45-50%) to vertebrate sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPases (SERCAs), and lowest homology (20%) to a plasma membrane Ca(2+)-ATPase. The P. falciparum protein conserved sequences and residues that are important for the function and/or structure of the organellar type Ca(2+)-ATPase, such as high affinity Ca(2+)-binding sites, fluorescein isothiocyanate (FITC)-binding regions, and the phosphorylation site, but the protein did not contain calmodulin-binding regions that occur in the plasma membrane type Ca(2+)-ATPase. Thus we concluded the cloned gene was the organellar type Ca(2+)-ATPase of P. falciparum. In a region between the phosphorylation site and FITC-binding region, the P. falciparum protein was about 200 residues longer than the rabbit SERCA and lacked a sequence that binds to phospholamban, a protein that regulates the activity of the rabbit SERCA.(ABSTRACT TRUNCATED AT 250 WORDS)

Characterization of Plasmodium falciparum protein kinase 2

2008 ◽  
Vol 162 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Kentaro Kato ◽  
Atsushi Sudo ◽  
Kyousuke Kobayashi ◽  
Yukinobu Tohya ◽  
Hiroomi Akashi
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Kinase ◽  
Falciparum Protein

scholarly journals Kelch Mutations in Plasmodium falciparum Protein K13 Do Not Modulate Dormancy after Artemisinin Exposure and Sorbitol Selection In Vitro

2018 ◽  
Vol 62 (5) ◽  
Author(s):  
Kimberly F. Breglio ◽  
Rifat S. Rahman ◽  
Juliana M. SÃ ◽  
Amanda Hott ◽  
David J. Roberts ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Single Site ◽  
Ring Stage ◽  
Content Type ◽  
Isogenic Lines ◽  
Falciparum Protein

ABSTRACT Some Kelch mutations of the Plasmodium falciparum K13 protein confer increased survival to dihydroartemisinin (DHA)-treated ring-stage parasites. Here, we asked if K13 mutations affect a dormancy phenotype allowing parasites to survive DHA exposure and then sorbitol selection. Although recrudescence from dormancy differed between two distinct parasite lines, it was similar for isogenic lines carrying single-site substitutions in K13. Therefore, K13 mutations do not alter the DHA-sorbitol combined dormancy phenotype; rather, traits from other loci likely determine this phenotype.

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