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Phosphorylation of protein 4.1 in Plasmodium falciparum-infected human red
blood cells
AH Chishti, GJ Maalouf, S Marfatia, J Palek, W Wang, D Fisher and SC Liu
Department of Biomedical Research, St. Elizabeth's Hospital, Tufts
University School of Medicine, Boston, MA 02135.
The composition of the erythrocyte plasma membrane is extensively modified
during the intracellular growth of the malaria parasite Plasmodium
falciparum. It has been previously shown that an 80-kD phosphoprotein is
associated with the plasma membrane of human red blood cells (RBCs)
infected with trophozoite/schizont stage malaria parasites. However, the
identity of this 80-kD phosphoprotein is controversial. One line of
evidence suggests that this protein is a phosphorylated form of RBC protein
4.1 and that it forms a tight complex with the mature parasite-infected
erythrocyte surface antigen. In contrast, evidence from another group
indicates that the 80-kD protein is derived from the intracellular malaria
parasite. To resolve whether the 80-kD protein is indeed RBC protein 4.1,
we made use of RBCs obtained from a patient with homozygous 4.1(-) negative
hereditary elliptocytosis. RBCs from this patient are completely devoid of
protein 4.1. We report here that this lack of protein 4.1 is correlated
with the absence of phosphorylation of the 80-kD protein in parasite-
infected RBCs, a finding that provides conclusive evidence that the 80- kD
phosphoprotein is indeed protein 4.1. In addition, we also identify and
partially characterize a casein kinase that phosphorylates protein 4.1 in P
falciparum-infected human RBCs. Based on these results, we suggest that the
maturation of malaria parasites in human RBCs is accompanied by the
phosphorylation of protein 4.1. This phosphorylation of RBC protein 4.1 may
provide a mechanism by which the intracellular malaria parasite alters the
mechanical properties of the host plasma membrane and modulates parasite
growth and survival in vivo.
Volume 83,
Issue 11,
pp. 3339-3345,
06/01/1994
Copyright © 1994 by The American Society of Hematology
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