Association of malaria with inactivation of alpha1,3-galactosyl transferase in catarrhines.
Present-day catarrhines (old world monkeys and hominoids) lack Gal alpha1-3 Gal beta1-4 GlcNAc-R structures (alpha-galactosyl epitopes) and produce the corresponding anti-galactosyl antibodies (anti-gal), while platyrrhines (new world monkeys) and non-primate mammals possess alpha-galactosyl epitopes and lack anti-gal. Anti-gal is shown to inhibit Plasmodium falciparum growth in culture in a concentration dependent manner. probably by binding to alpha-galactosyl epitopes on merozoite surface molecules and causing complement mediated damage. A P. falciparum-like malaria parasite may therefore have selected for the inactivation of an alpha 1-3 galactosyl transferase in catarrhines. The implications of the results for the development of clinical immunity to falciparum malaria are briefly discussed.
Ramasamy
R
R
Division of Life Sciences, Institute of Fundamental Studies, Kandy, Sri Lanka. ranjan@ifs.ac.lk
Rajakaruna
R
R
D000818:Animals; D000913:Antibodies, Protozoan / Q000276:immunology; D005700:Galactosyltransferases / Q000037:antagonists & inhibitors* / Q000276:immunology; D000882:Haplorhini; D006801:Humans; D007106:Immune Sera; D016778:Malaria, Falciparum / Q000201:enzymology* / Q000517:prevention & control; D009844:Oligosaccharides / Q000276:immunology; D010963:Plasmodium falciparum / Q000235:genetics / Q000276:immunology
D000913:Antibodies, Protozoan; D007106:Immune Sera; D009844:Oligosaccharides; D005700:Galactosyltransferases; C047006:N-acetyllactosaminide alpha-1,3-galactosyltransferase