Receptor-binding residues lie in central regions of Duffy-binding-like domains involved in red cell invasion and cytoadherence by malaria parasites
In: Blood, Jg. 105 (2004-09-04), Heft 6
Online
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Zugriff:
Erythrocyte invasion by malaria parasites and cytoadherence of Plasmodium falciparum-infected erythrocytes to host capillaries are 2 key pathogenic mechanisms in malaria. The receptor-binding domains of erythrocyte-binding proteins (EBPs) such as Plasmodium falciparum EBA-175, which mediate invasion, and P falciparum erythrocyte membrane protein 1 (PfEMP-1) family members, which are encoded by var genes and mediate cytoadherence, have been mapped to conserved cysteine-rich domains referred to as Duffy-binding–like (DBL) domains. Here, we have mapped regions within DBL domains from EBPs and PfEMP-1 that contain receptor-binding residues. Using biochemical and molecular methods we demonstrate that the receptor-binding residues of parasite ligands that bind sialic acid on glycophorin A for invasion as well as complement receptor-1 and chondroitin sulfate A for cytoadherence map to central regions of DBL domains. In contrast, binding to intercellular adhesion molecule 1 (ICAM-1) requires both the central and terminal regions of DBLβC2 domains. Determination of functional regions within DBL domains is the first step toward understanding the structure-function bases for their interaction with diverse host receptors.
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Receptor-binding residues lie in central regions of Duffy-binding-like domains involved in red cell invasion and cytoadherence by malaria parasites
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Autor/in / Beteiligte Person: | Pattnaik, Priyabrata ; Singh, Saurabh ; Bir, Nivedita ; Sharma, Amit ; Mayor, Alfredo ; Singh, Shailja ; Sawhney, Ritica ; Chitnis, Chetan E. |
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Zeitschrift: | Blood, Jg. 105 (2004-09-04), Heft 6 |
Veröffentlichung: | 2004 |
Medientyp: | unknown |
ISSN: | 0006-4971 (print) |
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