Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth

Antonella Pantaleo, Emanuela Ferru, Franco Carta, Franca Mannu, Giuliana Giribaldi, Rosa Vono, Antonio J. Lepedda, Proto Pippia, Francesco Turrini

Research output: Contribution to journalArticle

Abstract

Phosphorylation of erythrocyte membrane proteins has been previously documented following infection and intracellular growth of the malarial parasite, Plasmodium falciparum in red cells. Much of this data dealt with phosphorylation of serine residues. In this study, we report detailed characterization of phosphorylation of serine and tyrosine residues of red cell membrane proteins following infection by P falciparum. Western blot analysis using anti-phosphotyrosine and antiphosphoserine antibodies following 2-DE in conjunction with double channel laser-induced infrared fluorescence enabled accurate assessment of phosphorylation changes. Tyrosine phosphorylation of band 3 represented the earliest modification observed during parasite development. Band 3 tyrosine phosphorylation observed at the ring stage appears to be under the control of Syk kinase. Serine and tyrosine phosphorylation of additional cytoskeletal, trans-membrane and membrane associated proteins was documented as intracellular development of parasite progressed. Importantly, during late schizont stage of parasite maturation, we observed widespread protein dephosphorylation. In vitro treatments that caused distinct activation of red cell tyrosine and serine kinases elicited phosphorylative patterns similar to what observed in parasitized red blood cell, suggesting primary involvement of erythrocyte kinases. Identification of tyrosine phosphorylations of band 3, band 4.2, catalase and actin which have not been previously described in P. falciparum infected red cells suggests new potential regulatory mechanisms that could modify the functions of the host cell membrane.

Original languageEnglish
Pages (from-to)3469-3479
Number of pages11
JournalProteomics
Volume10
Issue number19
DOIs
Publication statusPublished - Oct 2010

Fingerprint

Phosphorylation
Serine
Tyrosine
Membrane Proteins
Growth
Parasites
Cells
Plasmodium falciparum
Phosphotransferases
Erythrocytes
Schizonts
Phosphotyrosine
Protein-Serine-Threonine Kinases
Erythrocyte Membrane
Cell membranes
Infection
Protein-Tyrosine Kinases
Catalase
Actins
Lasers

Keywords

  • 2-D electrophoresis
  • Band 3
  • Cell biology
  • Erythrocyte membrane
  • Plasmodium falciparum
  • Protein phosphorylation

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

Cite this

Pantaleo, A., Ferru, E., Carta, F., Mannu, F., Giribaldi, G., Vono, R., ... Turrini, F. (2010). Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth. Proteomics, 10(19), 3469-3479. https://doi.org/10.1002/pmic.201000269

Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth. / Pantaleo, Antonella; Ferru, Emanuela; Carta, Franco; Mannu, Franca; Giribaldi, Giuliana; Vono, Rosa; Lepedda, Antonio J.; Pippia, Proto; Turrini, Francesco.

In: Proteomics, Vol. 10, No. 19, 10.2010, p. 3469-3479.

Research output: Contribution to journalArticle

Pantaleo, A, Ferru, E, Carta, F, Mannu, F, Giribaldi, G, Vono, R, Lepedda, AJ, Pippia, P & Turrini, F 2010, 'Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth', Proteomics, vol. 10, no. 19, pp. 3469-3479. https://doi.org/10.1002/pmic.201000269
Pantaleo, Antonella ; Ferru, Emanuela ; Carta, Franco ; Mannu, Franca ; Giribaldi, Giuliana ; Vono, Rosa ; Lepedda, Antonio J. ; Pippia, Proto ; Turrini, Francesco. / Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth. In: Proteomics. 2010 ; Vol. 10, No. 19. pp. 3469-3479.
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