title: Studies on the glycoprotein modification in erythrocyte membrane during experimental cerebral malaria.
abstract: Plasmodium berghei ANKA (Pb ANKA) is a lethal strain of malaria that causes experimental cerebral malaria (ECM) in rodent models. Pathology of the disease is associated with the sequestration of the infected rbc (irbc) in the micro vessels of brain. In the present study, we analyzed the nature of the glycoprotein modification occurring in irbc membrane during erythrocytic stages of Pb ANKA infection. Titration of naturally occurring glycoproteins with concanavalin A (Con A) and wheat germ agglutinin (WGA) lectins revealed an enhanced lectin binding ability for the irbc membrane preparations. Partial characterization of the Con A specific determinants (alpha-d-methyl mannoside specificity) by lectin affinity chromatography followed by 2D electrophoresis and WGA specific determinants (sialic acid specificity) by Western analysis revealed the association of novel lectin specific determinants in irbc membrane. To correlate the biochemical changes with the morphological changes, SEM of irbc, and TEM of sequestered irbc were performed. These ultra structural studies revealed variable and irregular surface protrusions and deep surface indentations on irbc. These observations implicate that altered glycoprotein profiles may lead to cytoarchitectural changes in irbc membrane and such changes may be essential to establish contact with the host endothelial cells. These observations may be central to the microvascular sequestration and pathology of ECM.
authors.affiliation: Department of Animal Sciences, School of Life Sciences, University of Hyderabad, Hyderabad-500 046, India.
authors.forename: Kota Arun
authors.initials: KA
authors.lastname: Kumar
authors.forename: Sashi
authors.initials: S
authors.lastname: Singh
authors.forename: Phanithi Prakash
authors.initials: PP
authors.lastname: Babu
mesh_terms: D000818:Animals; D015153:Blotting, Western; D001921:Brain / Q000098:blood supply / Q000469:parasitology / Q000473:pathology; D002196:Capillaries / Q000469:parasitology / Q000648:ultrastructure; D003208:Concanavalin A / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000469:parasitology / Q000648:ultrastructure; D007106:Immune Sera / Q000276:immunology; D007074:Immunoglobulin G / Q000276:immunology; D016779:Malaria, Cerebral / Q000097:blood* / Q000473:pathology; D008562:Membrane Glycoproteins / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D010962:Plasmodium berghei / Q000502:physiology*; D011817:Rabbits; D015854:Up-Regulation; D014909:Wheat Germ Agglutinins / Q000378:metabolism
chemical_list: D007106:Immune Sera; D007074:Immunoglobulin G; D008562:Membrane Glycoproteins; D014909:Wheat Germ Agglutinins; D003208:Concanavalin A