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Monoclonal antibody OKM5 inhibits the in vitro binding of Plasmodium falciparum-infected erythrocytes to monocytes, endothelial, and C32 melanoma cells.

J W Barnwell, C F Ockenhouse and D M Knowles 2nd
J Immunol November 1, 1985, 135 (5) 3494-3497;
J W Barnwell
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C F Ockenhouse
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D M Knowles 2nd
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Abstract

Plasmodium falciparum-infected erythrocytes bind in vitro to human endothelial cells, monocytes, and a certain melanoma cell line. Evidence suggests that this interaction is mediated by similar mechanisms which lead to the sequestration of parasitized erythrocytes in vivo through their attachment to endothelial cells of small blood vessels. We show here that monoclonal antibody OKM5, previously shown to react with the membranes of endothelial cells, monocytes, and platelets, also reacts with the C32 melanoma cell line which also binds P. falciparum-infected erythrocytes. At relatively low concentrations, OKM5 inhibits and reverses the in vitro adherence of infected erythrocytes to target cells. As with monocytes, OKM5 antibody recognizes an 125I-labeled protein of approximately 88 Kd on the surface of C32 melanoma cells. It seems likely, therefore, that the 88 Kd polypeptide plays a role in cytoadherence, possibly as the receptor or part of a receptor for a ligand on the surface of infected erythrocytes.

  • Copyright © 1985 by American Association of Immunologists

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The Journal of Immunology
Vol. 135, Issue 5
1 Nov 1985
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Monoclonal antibody OKM5 inhibits the in vitro binding of Plasmodium falciparum-infected erythrocytes to monocytes, endothelial, and C32 melanoma cells.
J W Barnwell, C F Ockenhouse, D M Knowles
The Journal of Immunology November 1, 1985, 135 (5) 3494-3497;

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Monoclonal antibody OKM5 inhibits the in vitro binding of Plasmodium falciparum-infected erythrocytes to monocytes, endothelial, and C32 melanoma cells.
J W Barnwell, C F Ockenhouse, D M Knowles
The Journal of Immunology November 1, 1985, 135 (5) 3494-3497;
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Print ISSN 0022-1767        Online ISSN 1550-6606