Selective association of a fragment of the knob protein with spectrin, actin and the red cell membrane.
The knob protein of Plasmodium falciparum is essential for the formation of knob-like protrusions on the host erythrocyte membrane. A functional domain of the knob protein was identified. This peptide formed stable complexes with the two major red cell skeletal proteins, spectrin and actin. When introduced into resealed normal erythrocytes, the peptide associated selectively with the cytoplasmic surface of the membrane and formed knob-like electron dense deposits. Knobs are thought to play an important role in the immunopathology of P. falciparum infections. Our findings provide a first step towards understanding the molecular basis for selective membrane changes at knobs.
Kilejian
A
A
Public Health Research Institute, New York, NY 10016.
Rashid
M A
MA
Aikawa
M
M
Aji
T
T
Yang
Y F
YF
D000199:Actins / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D010963:Plasmodium falciparum / Q000378:metabolism*; D015800:Protozoan Proteins / Q000378:metabolism*; D013049:Spectrin / Q000378:metabolism*
D000199:Actins; D010446:Peptide Fragments; D010455:Peptides; D015800:Protozoan Proteins; C042968:knob protein, Plasmodium falciparum; D013049:Spectrin