Homology between a histidine-rich protein from Plasmodium lophurae and a protein associated with the knob-like protrusions on membranes of erythrocytes infected with Plasmodium falciparum.
The incorporation of several radioactive amino acids into the knob protein of Plasmodium falciparum was compared. Histidine showed better incorporation than proline. A protein hydrolysate, which had all major amino acids except histidine and methionine, showed relatively poor incorporation as compared with proline, and no labeling could be detected with methionine or leucine. These results strongly suggest that the amino acid composition of the knob protein has the same peculiarities as that of a histidine-rich protein characterized from P. lophurae. Immunoelectron microscopy suggested possible immunological cross-reactivity between these two proteins.
D000818:Animals; D001798:Blood Proteins / Q000032:analysis; D003429:Cross Reactions; D004910:Erythrocyte Membrane / Q000032:analysis; D004912:Erythrocytes / Q000469:parasitology; D006639:Histidine / Q000378:metabolism; D008288:Malaria / Q000378:metabolism*; D008565:Membrane Proteins / Q000032:analysis* / Q000276:immunology; D008970:Molecular Weight; D010961:Plasmodium / Q000032:analysis* / Q000276:immunology; D010963:Plasmodium falciparum / Q000032:analysis* / Q000276:immunology
D001798:Blood Proteins; D008565:Membrane Proteins; D006639:Histidine