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Divergent binding sites on intercellular adhesion molecule-1 (ICAM-1) for variant Plasmodium falciparum isolates

Tse, M. T., Chakrabarti, K., Gray, Carolyn, Chitnis, C. E. and Craig, Alister ORCID: https://orcid.org/0000-0003-0914-6164 (2004) 'Divergent binding sites on intercellular adhesion molecule-1 (ICAM-1) for variant Plasmodium falciparum isolates'. Molecular Microbiology, Vol 51, Issue 4, pp. 1039-1049.

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Abstract

Adhesion of human erythrocytes infected with the malaria parasite Plasmodium falciparum to host endothelium has been associated with severe forms of this disease. A number of endothelial receptors have been identified, and there is evidence that one of these, intercellular adhesion molecule-1 (ICAM-1), may play an important role in the pathology of cerebral malaria. Mutagenesis of domain 1 of ICAM-1, which is involved in parasite adhesion, shows that the binding sites for different parasite variants overlap to a large extent, but that there are subtle differences between them that correlate with their adhesive phenotypes. This suggests that the ability to bind to ICAM-1 has arisen from a common variant, but that subsequent changes have led to differences in binding avidity, which may affect pathogenesis. The definition of common binding determinants and the elucidation of links between ICAM-1 binding phenotype and disease will provide new leads in the design of therapeutic interventions.

Item Type: Article
Uncontrolled Keywords: microvascular endothelial-cells infected erythrocytes cerebral malaria membrane glycoprotein var genes receptor cd36 identification cytoadherence adherence
Subjects: QW Microbiology and Immunology > Immunity by Type > QW 568 Cellular immunity. Immunologic cytotoxicity. Immunocompetence. Immunologic factors (General)
WC Communicable Diseases > Tropical and Parasitic Diseases > WC 750 Malaria
WC Communicable Diseases > Tropical and Parasitic Diseases > WC 770 Therapy
WH Hemic and Lymphatic Systems > Hematologic Diseases. Immunologic Factors. Blood Banks > WH 150 Erythrocytes
Faculty: Department: Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group
Digital Object Identifer (DOI): https://doi.org/10.1046/j.1365-2958.2003.03895.x
Depositing User: Martin Chapman
Date Deposited: 21 Mar 2012 20:42
Last Modified: 06 Feb 2018 13:03
URI: https://archive.lstmed.ac.uk/id/eprint/2207

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