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

Guillaume Bouyer, Luc Reininger, Ghania Ramdani, Lee D. Phillips, Vikram Sharma, Stephane Egee, Gordon Langsley, Edwin Lasonder*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)
8 Downloads (Pure)

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.

Original languageEnglish
Pages (from-to)35-44
Number of pages10
JournalBlood Cells, Molecules, and Diseases
Volume58
Early online date13 Feb 2016
DOIs
Publication statusPublished - 1 May 2016
Externally publishedYes

Fingerprint Dive into the research topics of 'Plasmodium falciparum infection induces dynamic changes in the erythrocyte phospho-proteome'. Together they form a unique fingerprint.

Cite this