| Literature DB >> 1383388 |
D E Staunton1, C F Ockenhouse, T A Springer.
Abstract
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.Entities:
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Year: 1992 PMID: 1383388 PMCID: PMC2119430 DOI: 10.1084/jem.176.5.1471
Source DB: PubMed Journal: J Exp Med ISSN: 0022-1007 Impact factor: 14.307