Volume 30, Issue 6
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645



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 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 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.


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