Phosphorylated and Nonphosphorylated PfMAP2 Are Localized in the Nucleus, Dependent on the Stage of Plasmodium falciparum Asexual Maturation
| Autor: | Jamaiah Ibrahim, Farah Aida Dahalan, Mohammed Noor Embi, Mogana Das Murtey, Hasidah Mohd Sidek, Lim Fei Tieng, Nurul Aiezzah Zakaria, Noraishah Mydin Abdul-Aziz |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Erythrocytes Article Subject MAP Kinase Signaling System Immunoelectron microscopy Amino Acid Motifs Plasmodium falciparum Protozoan Proteins lcsh:Medicine Bioinformatics General Biochemistry Genetics and Molecular Biology Antibodies Gene Expression Regulation Enzymologic Substrate Specificity 03 medical and health sciences Antimalarials medicine Animals Humans Trophozoites Malaria Falciparum Phosphorylation Fluorescent Antibody Technique Indirect Microscopy Immunoelectron Phylogeny Regulation of gene expression Cell Nucleus General Immunology and Microbiology biology Kinase lcsh:R Computational Biology General Medicine biology.organism_classification Cell biology Cell nucleus 030104 developmental biology medicine.anatomical_structure Microscopy Fluorescence Mitogen-activated protein kinase biology.protein Rabbits Signal transduction Research Article |
| Zdroj: | BioMed Research International, Vol 2016 (2016) BioMed Research International |
| ISSN: | 2314-6133 |
| DOI: | 10.1155/2016/1645097 |
| Popis: | Plasmodium falciparummitogen-activated protein (MAP) kinases, a family of enzymes central to signal transduction processes including inflammatory responses, are a promising target for antimalarial drug development. Our study shows for the first time that theP. falciparumspecific MAP kinase 2 (PfMAP2) is colocalized in the nucleus of all of the asexual erythrocytic stages ofP. falciparumand is particularly elevated in its phosphorylated form. It was also discovered that PfMAP2 is expressed in its highest quantity during the early trophozoite (ring form) stage and significantly reduced in the mature trophozoite and schizont stages. Although the phosphorylated form of the kinase is always more prevalent, its ratio relative to the nonphosphorylated form remained constant irrespective of the parasites’ developmental stage. We have also shown that the TSH motif specifically renders PfMAP2 genetically divergent from the other plasmodial MAP kinase activation sites using Neighbour Joining analysis. Furthermore, TSH motif-specific designed antibody is crucial in determining the location of the expression of the PfMAP2 protein. However, by using immunoelectron microscopy, PPfMAP2 were detected ubiquitously in the parasitized erythrocytes. In summary, PfMAP2 may play a far more important role than previously thought and is a worthy candidate for research as an antimalarial. |
| Databáze: | OpenAIRE |
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