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Prepublished online as a Blood First Edition Paper on November 14, 2002; DOI 10.1182/blood-2002-07-2016. This Article Full Text (PDF) Erratum (v104,p3910) All Versions of this Article: 2002-07-2016v1 101/6/2405    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 Vogt, A. M Articles by Wahlgren, M. Search for Related Content PubMed PubMed Citation Articles by Vogt, A. M Articles by Wahlgren, M. Social Bookmarking                   What's this? Submitted July 5, 2002 Accepted October 23, 2002 Heparan sulfate on endothelial cells mediates the binding of Plasmodium falciparum-infected erythrocytes via the DBL1 domain of PfEMP1 Anna M Vogt, Antonio Barragan, Qijun Chen, Fred Kironde, Dorothe Spillmann, and Mats Wahlgren* Department of Microbiology and Tumor Biology Centre (MTC), Karolinska Institutet, Stockholm, Sweden; Swedish Institute for Infectious Disease Control (SMI), Stockholm, Sweden Department of Medical Biochemistry and Microbiology, Biomedical Centre, Uppsala University, Uppsala, Sweden Department of Biochemistry, University of Makerere, Kampala, Uganda * Corresponding author; email: mats.wahlgren{at}smi.ki.se. Plasmodium falciparum may cause severe forms of malaria when excessive sequestration of infected and uninfected erythrocytes occurs in vital organs. The capacity of wild isolates of P. falciparum-infected erythrocytes (pRBC) to bind glycosamoinoglycans (GAG) such as heparin has been identified as a marker for severe disease. Here we report that pRBC of the parasite FCR3S1.2 and wild clinical isolates from Uganda adhere to heparan sulfate (HS) on endothelial cells. Binding to human umbilical vein endothelial cells (HUVEC) and to human lung endothelial cells (HLEC) was found to be inhibited by HS/heparin or enzymes that remove HS from cell surfaces.35S-labeled HS extracted from HUVECs bound directly to the pRBCs membrane. Using recombinant proteins corresponding to the different domains of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) we identified Duffy-binding-like domain-1 (DBL1) as the ligand for HS. DBL1 bound in a HS dependent way to endothelial cells and blocked the adherence of pRBC in a dose-dependent manner. 35S-labeled HS bound to DBL1-columns and eluted as a distinct peak at 0.4 mM NaCl. 35S-labeled chondroitin sulfate (CS) of HUVECs did not bind to PfEMP1 or to the pRBCs membrane. Adhesion of pRBC of FCR3S1.2 to PECAM-1/CD31, mediated by the cystein-rich-interdomain region 1 (CIDR1), was found to be co-operative with but independent of the binding to HS. HS and the previously identified HS-like GAG on uninfected erythrocytes may act as co-receptors in endothelial and erythrocyte binding of rosetting parasites causing excessive sequestration of both pRBC and RBC. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. Normark, D. Nilsson, U. Ribacke, G. Winter, K. Moll, C. E. Wheelock, J. Bayarugaba, F. Kironde, T. G. Egwang, Q. Chen, et al. 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