title: Red cell membrane protein distribution during malarial invasion.
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.
authors.affiliation: Medical Research Council Cell Biophysics Unit, King's College, London, UK.
authors.forename: A R
authors.initials: AR
authors.lastname: Dluzewski
authors.forename: P R
authors.initials: PR
authors.lastname: Fryer
authors.forename: S
authors.initials: S
authors.lastname: Griffiths
authors.forename: R J
authors.initials: RJ
authors.lastname: Wilson
authors.forename: W B
authors.initials: WB
authors.lastname: Gratzer
mesh_terms: D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000032:analysis; D017487:Ankyrins; D001798:Blood Proteins / Q000032:analysis*; D003571:Cytochalasin B / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000032:analysis* / Q000648:ultrastructure; D004912:Erythrocytes / Q000469:parasitology*; D000882:Haplorhini; D006801:Humans; D007150:Immunohistochemistry; D008565:Membrane Proteins / Q000032:analysis*; D008854:Microscopy, Electron; D010961:Plasmodium / Q000502:physiology*; D010963:Plasmodium falciparum / Q000502:physiology; D013049:Spectrin / Q000032:analysis; D014617:Vacuoles / Q000032:analysis
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D017487:Ankyrins; D001798:Blood Proteins; D008565:Membrane Proteins; D013049:Spectrin; D003571:Cytochalasin B