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PMID: 2532219 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Red cell membrane protein distribution during malarial invasion.

Journal of cell science ·Vol. 92 ( Pt 4) ·1989-04-00 ·Pages 691-9

Dluzewski AR, Fryer PR, Griffiths S, Wilson RJ, Gratzer WB

Abstract

Immuno-gold labelling electron microscopy of thin sections was used to determine the distribution of red cell membrane and membrane skeleton proteins in the vicinity of internalized malaria parasites. When examined immediately after invasion (young ring-stage parasites), the parasitophorous vacuole membranes of both Plasmodium falciparum and P. knowlesi were found to be characterized by the essentially complete absence of spectrin, ankyrin and the most abundant transmembrane protein, band 3. P. knowlesi merozoites were trapped in the attached but not internalized state by pretreatment with cytochalasin B. In this merozoite-red cell complex antibody labelling showed that band 3 had been eliminated from the region of the host cell membrane in contact with the parasite. Internal vesicles, originating apparently from the site of attachment, were often observed in the red cell. Opposite the attached parasite a cavity was also sometimes seen in the host cell, presumably representing an incipient internal vesicle. The membrane was intact, as judged by the absence of protein (haemoglobin) in the cavity, and, like the membranes surrounding the internal vesicles, was devoid of membrane proteins. A large multilamellar body was sometimes seen in the merozoite close to its point of attachment. The lamellar spacing was about 50 nm. The electron microscope images suggest a diffusion of electron-dense material from the lamellar body into the cavity in the host cell.

MeSH Terms
Animals Anion Exchange Protein 1, Erythrocyte/analysis Ankyrins Blood Proteins/analysis Cytochalasin B/pharmacology Erythrocyte Membrane/analysis,ultrastructure Erythrocytes/parasitology Haplorhini Humans Immunohistochemistry Membrane Proteins/analysis Microscopy, Electron Plasmodium/physiology Plasmodium falciparum/physiology Spectrin/analysis Vacuoles/analysis
Chemicals
Anion Exchange Protein 1, Erythrocyte Ankyrins Blood Proteins Membrane Proteins Spectrin Cytochalasin B
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Dluzewski A R
Medical Research Council Cell Biophysics Unit, King's College, London, UK.
Fryer P R
Griffiths S
Wilson R J
Gratzer W B
Article Info
Journal
Journal of cell science
Abbr.
J Cell Sci
ISSN
0021-9533
Published
1989-04-00
Pages
691-9
Language
English
Region
England
NLM ID
0052457
Subset
IM
Grants
Medical Research Council · MC_U117532072 · United Kingdom
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