title: Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth.
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 anti-phosphoserine 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.
authors.affiliation: Department of Genetics, Biology and Biochemistry, University of Turin, Turin, Italy. antonella.pantaleo@unito.it
authors.forename: Antonella
authors.initials: A
authors.lastname: Pantaleo
authors.forename: Emanuela
authors.initials: E
authors.lastname: Ferru
authors.forename: Franco
authors.initials: F
authors.lastname: Carta
authors.forename: Franca
authors.initials: F
authors.lastname: Mannu
authors.forename: Giuliana
authors.initials: G
authors.lastname: Giribaldi
authors.forename: Rosa
authors.initials: R
authors.lastname: Vono
authors.forename: Antonio J
authors.initials: AJ
authors.lastname: Lepedda
authors.forename: Proto
authors.initials: P
authors.lastname: Pippia
authors.forename: Francesco
authors.initials: F
authors.lastname: Turrini
mesh_terms: D004910:Erythrocyte Membrane / Q000378:metabolism / Q000469:parasitology*; D006790:Host-Parasite Interactions; D006801:Humans; D016778:Malaria, Falciparum / Q000469:parasitology / Q000503:physiopathology; D008565:Membrane Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D010963:Plasmodium falciparum / Q000254:growth & development / Q000502:physiology*; D012694:Serine / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*
chemical_list: D008565:Membrane Proteins; D010750:Phosphoproteins; D014443:Tyrosine; D012694:Serine