Soluble intercellular adhesion molecule 1-immunoglobulin G1 immunoadhesin mediates phagocytosis of malaria-infected erythrocytes.
We describe an immunoadhesin molecule containing intercellular adhesion molecule 1 (ICAM-1) molecularly fused to hinge and CH2 and CH3 domains of the human immunoglobulin G1 H chain that binds Plasmodium falciparum-infected erythrocytes. This receptor-based immunoadhesin is an effective and specific inhibitor of P. falciparum-infected erythrocyte adhesion to ICAM-1-bearing surfaces, but does not inhibit leukocyte function antigen 1 (LFA-1) interaction with ICAM-1. Furthermore, the immunoadhesin promotes phagocytosis and destruction of parasitized erythrocytes by human monocytes. Each of these modes of action has potential for the therapy of malaria.
Staunton
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DE
Walter Reed Army Institute of Research, Washington, DC 20307.
Ockenhouse
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CF
Springer
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TA
D000818:Animals; D015703:Antigens, CD / Q000502:physiology; D001483:Base Sequence; D018955:CD36 Antigens; D015815:Cell Adhesion Molecules / Q000502:physiology*; D004912:Erythrocytes / Q000469:parasitology*; D006801:Humans; D007074:Immunoglobulin G / Q000502:physiology*; D018799:Intercellular Adhesion Molecule-1; D008969:Molecular Sequence Data; D010587:Phagocytosis; D010963:Plasmodium falciparum / Q000276:immunology*
D015703:Antigens, CD; D018955:CD36 Antigens; D015815:Cell Adhesion Molecules; D007074:Immunoglobulin G; D018799:Intercellular Adhesion Molecule-1