The merozoite has landed: reticulocyte-binding-like ligands and the specificity of erythrocyte recognition.
Plasmodium falciparum erythrocyte invasion depends on several imperfectly understood multiprotein families. Two recent papers have shifted our understanding of the P. falciparum reticulocyte-binding-like family to the level of individual amino acids by identifying an erythrocyte-binding domain in one ligand and showing that polymorphisms in another can change the species specificity of erythrocyte binding. Erythrocyte invasion might be even more complex and harder to target than previously thought.
Rayner
Julian C
JC
Sanger Institute Malaria Programme, Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SA, UK. jr9@sanger.ac.uk
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004912:Erythrocytes / Q000469:parasitology*; D006801:Humans; D008024:Ligands; D052940:Merozoites / Q000378:metabolism*; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000254:growth & development / Q000378:metabolism / Q000472:pathogenicity*; D020641:Polymorphism, Single Nucleotide; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012156:Reticulocytes / Q000378:metabolism* / Q000469:parasitology; D012680:Sensitivity and Specificity
D008024:Ligands; D015800:Protozoan Proteins