Selective elimination of malaria infected erythrocytes by a modified phospholipase A2 in vitro.
Pig pancreatic phospholipase A2 does not act on normal erythrocytes, but the membrane penetrating capacity is enhanced by the covalent attachment of one fatty acyl chain to Lys-116 of the enzyme. Taking advantage of the impaired packing of phospholipids in the membrane of Plasmodium infected erythrocytes it was demonstrated that a lauric acid derivative of phospholipase A2 is capable of exclusively attaching the infected erythrocytes in vitro, leaving the uninfected cells undisturbed. The chemically modified phospholipase A2 appeared to cause death of the parasite in cell cultures of infected erythrocytes.
Moll
G N
GN
C.B.L.E., State University of Utrecht, The Netherlands.
Vial
H J
HJ
van der Wiele
F C
FC
Ancelin
M L
ML
Roelofsen
B
B
Slotboom
A J
AJ
de Haas
G H
GH
van Deenen
L L
LL
Op den Kamp
J A
JA
D000818:Animals; D004912:Erythrocytes / Q000469:parasitology*; D006461:Hemolysis; D066298:In Vitro Techniques; D008252:Macaca fascicularis; D008253:Macaca mulatta; D008288:Malaria / Q000097:blood*; D010713:Phosphatidylcholines / Q000494:pharmacology; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2
D010713:Phosphatidylcholines; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2