Plasmodium falciparum sialic acid

Among the fungal and protozoal lectins only a few have been studied in detail. One of these is the galactose-specific lectin of the protozoa Entamoeba histolytica. It mediates adhesion of the parasite to human colonic mucin glycoproteins and has a central role in the contact-dependent cytolysis or histolysis for which the parasite is named. A sialic-acid-speeific lectin has been isolated from merozoites of the human malarial parasite, Plasmodium falciparum. An unusual lectin is that of the protozoan Giardia lamblia, specific for mannose-6-phosphate, which is activated by trypsinization. 

Duraisingh, M. T., Maier, A. G., Triglia, T., and Cowman, A. F. (2003). Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways. Proc. Natl. Acad. Sci. USA 100,4796 801. 

Templeton, T. J., Keister, D. B., Muratova, O., Procter, J. L., and Kaslow, D. C. (1998). Adherence of erythrocytes during exflagellation of Plasmodium falciparum microgametes is dependent on erythrocyte surface sialic acid and glycophorins. ]. Exp. Med. 187, 1599-1609. 

Perkins, M. E., and Rocco, L. J., 1988, Sialic acid-dependent binding of Plasmodium falciparum merozoite surface antigen, Pf200, to human erythrocytes, J. Immunol. 141 3190-3196. 

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