Regular paper
Phospholipid organization in monkey erythrocytes upon Plasmodium knowlesi infection

https://doi.org/10.1016/0005-2736(87)90250-1Get rights and content

Abstract

The phospholipid organization in monkey erythrocytes upon Plasmodium knowlesi infection has been studied. Parasitized and nonparasitized erythrocytes from malaria-infected blood were separated and pure erythrocyte membranes from parasitized cells were isolated using Affi-Gel beads. In this way, the phospholipid content and composition of (i) the membrane of nonparasitized cells, (ii) the erythrocyte membrane of parasitized cells and (iii) the parasite could be determined. The phospholipid content and composition of the erythrocyte membranes of nonparasitized and parasitized cells and erythrocytes from chloroquine-treated monkeys cured from malaria, were the same as in normal erythrocytes. The phospholipid content of the parasite increased during its development, but its composition remained unchanged. Three independent techniques, i.e., treatment of intact cells with phospholipase A2 and sphingomyelinase C, fluorescamine labeling of aminophospholipids and a phosphatidylcholine-transfer protein-mediated exchange procedure have been applied to assess the disposition of phospholipids in: (i) erythrocytes from healthy monkeys, (ii) nonparasitized and parasitized erythrocytes from monkeys infected with Plasmodium knowlesi, and (iii) erythrocytes from monkeys that had been cured from malaria by chloroquine treatment. The results obtained by these experiments do not show any abnormality in phospholipid asymmetry in the erythrocyte from malaria-infected (splenectomized) monkeys, neither in the nonparasitized cells, nor in the parasitized cells at any stage of parasite development. Nevertheless, a considerable degree of lipid bilayer destabilization in the membrane of the parasitized cells is apparent from the enhanced exchangeability of the PC from those cells, as well as from their increased permeability towards fluorescamine.

References (53)

  • H.J. Vial et al.

    Mol. Biochem. Parasitol.

    (1984)
  • B.D. Beaumelle et al.

    Biochim. Biophys. Acta

    (1986)
  • Y. Yuthavong et al.

    Comp. Biochem. Physiol.

    (1979)
  • P.F.H. Franck et al.

    Biochim. Biophys. Acta

    (1982)
  • P.F.H. Franck et al.

    Biochim. Biophys. Acta

    (1985)
  • P. Joshi et al.

    Biochim. Biophys. Acta

    (1986)
  • R.M. Kramer et al.

    Biochim. Biophys. Acta

    (1979)
  • R.F.A. Zwaal et al.

    Biochim. Biophys. Acta

    (1975)
  • J. Westerman et al.

    Methods Enzymol.

    (1983)
  • A.W. Rowe et al.

    Cryobiology

    (1968)
  • C.D. Mitchell et al.

    Biochim. Biophys. Acta

    (1965)
  • M.E. Aberlin et al.

    Biochim. Biophys. Acta

    (1979)
  • H.G. Rose et al.

    J. Lipid Res.

    (1965)
  • R.M. Broekhuyse

    Clin. Chim. Acta

    (1969)
  • A. Rawyler et al.

    Biochim. Biophys. Acta

    (1984)
  • F.A. Kuypers et al.

    Biochim. Biophys. Acta

    (1984)
  • H. Kamp et al.

    Methods Enzymol.

    (1974)
  • R.C. Rock et al.

    Comp. Biochem. Physiol.

    (1971)
  • S. McClean et al.

    Anal. Chim. Acta

    (1976)
  • C.W.M. Haest et al.

    Biochim. Biophys. Acta

    (1978)
  • A.J. Rawyler et al.

    Biochim. Biophys. Acta

    (1983)
  • J.P.J. Boegheim et al.

    Biochim. Biophys. Acta

    (1983)
  • L. Tilley et al.

    FEBS Lett.

    (1986)
  • E. Mulder et al.

    Biochim. Biophys. Acta

    (1965)
  • E. Mulder et al.

    Biochim. Biophys. Acta

    (1965)
  • I.W. Sherman

    Microbiol. Rev.

    (1979)
  • Cited by (0)

    View full text