Abstract
GPI-anchored proteins are ubiquitously expressed on eukaryotic cell surfaces and are involved in a variety of vital functions ranging from adhesion to enzymatic catalysis. This review focuses on GPI-anchored proteins in malaria and the role of carbohydrate moieties in malarial proteins. Malaria remains a formidable threat to human beings even in the twenty-first century. Malaria vaccine development to prevent morbidity and mortality has generated comprehensive molecular information on many immunologically-relevant malarial antigens but an effective anti-malaria vaccine is still unavailable. Several malarial antigenic proteins have been considered as promising vaccine candidates. Merozoite surface protein 1 (MSP-1) and merozoite surface protein 2 (MSP-2) from the asexual stages of the malarial life cycle are prominent amongst malarial antigens. Modifications of MSPs are significantly important as the natural MSPs offer better protection against malaria compared to recombinant proteins that lack post-translational modifications. Development of viable vaccine(s) against malaria has met considerable difficulties and it is likely that the lack of post-translational modification may have been a contributory factor. The role of galactose residues in MSP-1 is reviewed in this article.
Keywords: Terminal galactose, GPI-anchored proteins, merozoite surface proteins, Trypanosoma brucei, mannosyl glucosamine
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