The nature of protein modifications, particularly surface glycosylation, in Plasmodium falciparum has long been observed, but in recent times controversial reports appeared. It is considered that the surface modifications, O- and N-glycosylation, have been of particular importance to the malarial parasite itself as well as to the erythrocyte. The modifications in the erythrocytic membranes and changes in the parasitic structure have been the subject of intense investigations in recent years. Comprehensive elaborations resulted in the development of means to describe the extensively modified structural and antigenic properties of the host cell and parasitic molecules that are of vital significance in the understanding of the functions of biologically important molecules such as the merozoite surface protein-1 (MSP-1). A combinatorial behavior of the parasitic and host cell molecules becomes the basis for molecular modifications of the parasite proteins and the events leading to invasion and survival of the parasite. The MSP-1 protein is modified on the surface by a sugar moiety O-glycosidically linked in β-configuration. This β-O-GlcNAc modication of MSP-1 has been predicted by computer assistance and experimentally verified. The Plasmodium falciparum proteins are known to be phosphorylated, and phosphorylation of MSP-1 has been predicted; moreover, there is sufficient experimental evidence to suggest phosphorylation. Computer assisted studies suggest a strong possibility of interplay between glycosylation and phosphorylation in proteins with β-O-GlcNAc modification.