Hot, sweet and sticky: the glycobiology of Plasmodium falciparum.
Carbohydrate structures that decorate the surface of cells are increasingly recognized as playing important roles in the biology of host-pathogen interactions. Plasmodium species have undergone a process of gene loss that has removed much of their capacity to produce complex glycoconjugates or glycosylated proteins other than the glycosylphosphatidyinositol (GPI) moiety that anchors the surface proteins of infective stages, including the merozoite. Instead, these parasites have elaborated a set of proteins with lectin-like properties that interact with mammalian and insect cell surfaces. An overview of this and other aspects of the glycobiology of Plasmodium is presented here.
von Itzstein
Mark
M
Monash University, VIC 3800, Australia.
Plebanski
Magdalena
M
Cooke
Brian M
BM
Coppel
Ross L
RL
D000818:Animals; D002240:Carbohydrate Sequence; D018503:Genome, Protozoan; D017261:Glycosylphosphatidylinositols / Q000378:metabolism*; D008288:Malaria / Q000469:parasitology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D015800:Protozoan Proteins / Q000378:metabolism
D017261:Glycosylphosphatidylinositols; D015800:Protozoan Proteins