Skip to main content
Journal cover image

Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes.

Publication ,  Journal Article
Atkinson, CT; Aikawa, M; Perry, G; Fujino, T; Bennett, V; Davidson, EA; Howard, RJ
Published in: Eur J Cell Biol
February 1988

The distributions of ankyrin, spectrin, band 3, and glycophorin A were examined in Plasmodium falciparum-infected erythrocytes by immunoelectron microscopy to determine whether movement of parasite proteins and membrane vesicles between the parasitophorous vacuole membrane and erythrocyte surface membrane involves internalization of host membrane skeleton proteins. Monospecific rabbit antisera to spectrin, band 3 and ankyrin and a mouse monoclonal antibody to glycophorin A reacted with these erythrocyte proteins in infected and uninfected human erythrocytes by immunoblotting. Cross-reacting malarial proteins were not detected. The rabbit sera also failed to immunoprecipitate [3H]isoleucine labeled malarial proteins from Triton X-100 and sodium dodecyl sulfate (SDS) extracts of infected erythrocytes. These three antibodies as well as the monoclonal antibody to glycophorin A bound to the membrane skeleton of infected and uninfected erythrocytes. The parasitophorous vacuole membrane was devoid of bound antibody, a result indicating that this membrane contains little, if any, of these host membrane proteins. With ring-, trophozoite- and schizont-infected erythrocytes, spectrin, band 3 and glycophorin A were absent from intracellular membranes including Maurer's clefts and other vesicles in the erythrocyte cytoplasm. In contrast, Maurer's clefts were specifically labeled by anti-ankyrin antibody. There was a slight, corresponding decrease in labeling of the membrane skeleton of infected erythrocytes. A second, morphologically distinct population of circular, vesicle-like membranes in the erythrocyte cytoplasm was not labeled with anti-ankyrin antibody. We conclude that membrane movement between the host erythrocyte surface membrane and parasitophorous vacuole membrane involves preferential sorting of ankyrin into a subpopulation of cytoplasmic membranes.

Duke Scholars

Published In

Eur J Cell Biol

ISSN

0171-9335

Publication Date

February 1988

Volume

45

Issue

2

Start / End Page

192 / 199

Location

Germany

Related Subject Headings

  • Spectrin
  • Plasmodium falciparum
  • Microscopy, Electron
  • Membrane Proteins
  • Immunohistochemistry
  • Glycophorins
  • Erythrocytes
  • Developmental Biology
  • Cytoskeletal Proteins
  • Blood Proteins
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Atkinson, C. T., Aikawa, M., Perry, G., Fujino, T., Bennett, V., Davidson, E. A., & Howard, R. J. (1988). Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes. Eur J Cell Biol, 45(2), 192–199.
Atkinson, C. T., M. Aikawa, G. Perry, T. Fujino, V. Bennett, E. A. Davidson, and R. J. Howard. “Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes.Eur J Cell Biol 45, no. 2 (February 1988): 192–99.
Atkinson CT, Aikawa M, Perry G, Fujino T, Bennett V, Davidson EA, et al. Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes. Eur J Cell Biol. 1988 Feb;45(2):192–9.
Atkinson CT, Aikawa M, Perry G, Fujino T, Bennett V, Davidson EA, Howard RJ. Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes. Eur J Cell Biol. 1988 Feb;45(2):192–199.
Journal cover image

Published In

Eur J Cell Biol

ISSN

0171-9335

Publication Date

February 1988

Volume

45

Issue

2

Start / End Page

192 / 199

Location

Germany

Related Subject Headings

  • Spectrin
  • Plasmodium falciparum
  • Microscopy, Electron
  • Membrane Proteins
  • Immunohistochemistry
  • Glycophorins
  • Erythrocytes
  • Developmental Biology
  • Cytoskeletal Proteins
  • Blood Proteins