PMID: 7034559Nov 1, 1981Paper

Competitive inhibition by soluble erythrocyte glycoproteins of penetration by Plasmodium falciparum

The American Journal of Tropical Medicine and Hygiene
J E Deas, L T Lee

Abstract

Glycophorin, the major sialoglycoprotein of the erythrocyte membrane, was extracted from human erythrocyte ghosts by the lithium diiodosalicylate phenol (LIS) or chloroform-methanol (CM) methods. The products (LISgp and CMgp) were examined for their capacity to inhibit invasion of erythrocytes by Plasmodium falciparum in vitro. In the presence of either glycoprotein, parasitemia was significantly less than in control cultures, indicating competitive inhibition of attachment. Desialylation resulted in only partial loss of this inhibitory potency. Neither crystalline NANA nor the dialyzates of either hydrolyzed glycoprotein had any inhibitory effect. We conclude that the receptor for merozoites of P. falciparum probably resides in the protein portion of glycophorin, in which NANA plays a secondary role, possibly related to hydration of the cell surface. The parasite itself contains no detectable neuraminidase activity.

Citations

Jan 1, 1985·Transactions of the Royal Society of Tropical Medicine and Hygiene·M Jungery
Jul 28, 2011·Cellular Microbiology·José A Stoute
Jan 1, 1989·Parasitology·G H Mitchell
Jan 1, 1983·Transactions of the Royal Society of Tropical Medicine and Hygiene·C A Facer
Feb 26, 2011·Immunological Reviews·Julius Clemence HafallaKai Matuschewski
Apr 11, 2018·Scientific Reports·Gordon A AwandareJosé A Stoute
Apr 4, 2015·The Journal of Infectious Diseases·Henrietta E Mensah-BrownGordon A Awandare
Jan 1, 1984·Molecular and Biochemical Parasitology·M E Perkins
Apr 1, 1984·Molecular and Biochemical Parasitology·C I Newbold
Jan 1, 1987·Infection and Immunity·M H Rodriguez, M Jungery
Dec 1, 1984·Experimental Parasitology·P HermentinB Enders
Jan 1, 1988·Critical Reviews in Oncology/hematology·G H Mitchell, L H Bannister
Jun 1, 1993·Baillière's Clinical Haematology·G PasvolB Clough

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