Glycosylation in malaria parasites: what do we know?

Trends Parasitol. 2024 Feb;40(2):131-146. doi: 10.1016/j.pt.2023.12.006. Epub 2024 Jan 22.

Abstract

In malaria parasites, although post-translational modification of proteins with N-. O-, and C-glycosidic bond-linked glycans is limited, it is confined to relatively fewer proteins in which the glycans are present at significant levels and may have important functions. Furthermore, several proteins are modified with glycosylphosphatidylinositols (GPIs) which represent the predominant glycan synthesized by parasites. Modification of proteins with GPIs is obligatory for parasite survival as GPI-anchored proteins (GPI-APs) play essential roles in all life cycle stages of the parasites, including development, egress, gametogenesis, motility, and host cell adhesion and invasion. Here, we discuss the current knowledge on the structures and potential functions of the glycan moieties of parasite proteins. The knowledge has important implications for the development of drugs and vaccines for malaria.

Keywords: Plasmodium parasites; glycan structure and function; glycosylation; malaria.

Publication types

  • Review

MeSH terms

  • Animals
  • Glycosylation
  • Glycosylphosphatidylinositols / chemistry
  • Glycosylphosphatidylinositols / metabolism
  • Parasites* / metabolism
  • Plasmodium falciparum
  • Polysaccharides / metabolism
  • Protein Processing, Post-Translational
  • Protozoan Proteins / metabolism

Substances

  • Glycosylphosphatidylinositols
  • Polysaccharides
  • Protozoan Proteins