SEARCH:   Advanced

Blood, 15 March 2005, Vol. 105, No. 6, pp. 2557-2563. Prepublished online as a Blood First Edition Paper on September 2, 2004; DOI 10.1182/blood-2004-05-1722. This Article Full Text (PDF) All Versions of this Article: 2004-05-1722v1 105/6/2557    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Mayor, A. Articles by Chitnis, C. E Search for Related Content PubMed PubMed Citation Articles by Mayor, A. Articles by Chitnis, C. E Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted May 11, 2004 Accepted August 19, 2004 Receptor-binding residues lie in central regions of Duffy-binding-like domains involved in red cell invasion and cytoadherence by malaria parasites Alfredo Mayor, Nivedita Bir, Ritica Sawhney, Shailja Singh, Priyabrata Pattnaik, Saurabh K Singh, Amit Sharma, and Chetan E Chitnis* Malaria Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), New Delhi, India * Corresponding author; email: cchitnis{at}icgeb.res.in. Erythrocyte invasion by malaria parasites and cytoadherence of Plasmodium falciparum-infected erythrocytes to host capillaries are two key pathogenic mechanisms in malaria. The receptor-binding domains of erythrocyte binding proteins (EBPs) such as Plasmodium falciparum EBA-175, which mediate invasion, and 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 ICAM-1 requires both the central and terminal regions of DBLC2 domains. Determination of functional boundaries within DBL domains is the first step towards understanding the structure-function bases for their interaction with diverse host receptors. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. Mayor, E. Rovira-Vallbona, A. Srivastava, S. K. Sharma, S. S. Pati, L. Puyol, L. Quinto, Q. Bassat, S. Machevo, I. Mandomando, et al. Functional and Immunological Characterization of a Duffy Binding-Like Alpha Domain from Plasmodium falciparum Erythrocyte Membrane Protein 1 That Mediates Rosetting Infect. Immun., September 1, 2009; 77(9): 3857 - 3863. [Abstract] [Full Text] [PDF] J. Normark, D. Nilsson, U. Ribacke, G. Winter, K. Moll, C. E. Wheelock, J. Bayarugaba, F. Kironde, T. G. Egwang, Q. Chen, et al. PfEMP1-DBL1{alpha} amino acid motifs in severe disease states of Plasmodium falciparum malaria PNAS, October 2, 2007; 104(40): 15835 - 15840. [Abstract] [Full Text] [PDF]

	Copyright © 2004 by American Society of Hematology         Online ISSN: 1528-0020