Plasmodium falciparum infection induces dynamic changes in the erythrocyte phospho-proteome

Bouyer, Guillaume, Reininger, Luc, Ramdani, Ghania, D. Phillips, Lee, Sharma, Vikram, Egee, Stephane, Langsley, Gordon and Lasonder, Edwin (2016) Plasmodium falciparum infection induces dynamic changes in the erythrocyte phospho-proteome. Blood Cells, Molecules, and Diseases, 58. pp. 35-44. ISSN 1079-9796

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Official URL: https://doi.org/10.1016/j.bcmd.2016.02.001

Abstract

The phosphorylation status of red blood cell proteins is strongly altered during the infection by the malaria parasite Plasmodium falciparum. We identify the key phosphorylation events that occur in the erythrocyte membrane and cytoskeleton during infection, by a comparative analysis of global phospho-proteome screens between infected (obtained at schizont stage) and uninfected RBCs. The meta-analysis of reported mass spectrometry studies revealed a novel compendium of 495 phosphorylation sites in 182 human proteins with regulatory roles in red cell morphology and stability, with about 25% of these sites specific to infected cells. A phosphorylation motif analysis detected 7 unique motifs that were largely mapped to kinase consensus sequences of casein kinase II and of protein kinase A/protein kinase C. This analysis highlighted prominent roles for PKA/PKC involving 78 phosphorylation sites. We then compared the phosphorylation status of PKA (PKC) specific sites in adducin, dematin, Band 3 and GLUT-1 in uninfected RBC stimulated or not by cAMP to their phosphorylation status in iRBC. We showed cAMP-induced phosphorylation of adducin S59 by immunoblotting and we were able to demonstrate parasite-induced phosphorylation for adducin S726, Band 3 and GLUT-1, corroborating the protein phosphorylation status in our erythrocyte phosphorylation site compendium.

Item Type: Article
Uncontrolled Keywords: CAMP/protein kinase A, Cytoskeleton, Erythrocyte, GLUT-1, P. falciparum, Protein phosphorylation
Subjects: C100 Biology
C900 Others in Biological Sciences
Department: Faculties > Health and Life Sciences > Applied Sciences
Depositing User: Rachel Branson
Date Deposited: 22 Apr 2020 09:22
Last Modified: 22 Apr 2020 09:30
URI: http://nrl.northumbria.ac.uk/id/eprint/42868

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