Present-day catarrhines (old world monkeys and hominoids) lack Gal α1-3 Gal β1-4 GlcNAc-R structures (α-galactosyl epitopes) and produce the corresponding anti-galactosyl antibodies (anti-gal), while platyrrhines (new world monkeys) and non-primate mammals possess α-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 α-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 α1-3 galactosyl transferase in catarrhines. The implications of the results for the development of clinical immunity to falciparum malaria are briefly discussed.
Ramasamy, R., & Rajakaruna, R. (1997). Association of malaria with inactivation of α1,3-galactosyl transferase in catarrhines. Biochimica et Biophysica Acta - Molecular Basis of Disease, 1360(3), 241–246. https://doi.org/10.1016/S0925-4439(97)00005-7