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Blood, 1 July 2006, Vol. 108, No. 1, pp. 370-378. Prepublished online as a Blood First Edition Paper on February 28, 2006; DOI 10.1182/blood-2005-11-4624. This Article Full Text Full Text (PDF) Supplemental Table All Versions of this Article: 2005-11-4624v1 108/1/370    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Rug, M. Articles by Cowman, A. F. Search for Related Content PubMed PubMed Citation Articles by Rug, M. Articles by Cowman, A. F. Related Collections Red Cells Cell Adhesion and Motility Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS The role of KAHRP domains in knob formation and cytoadherence of P falciparum-infected human erythrocytes Melanie Rug, Stuart W. Prescott, Kate M. Fernandez, Brian M. Cooke, and Alan F. Cowman From the Walter and Eliza Hall Institute of Medical Research, Melbourne; Particulate Fluids Processing Centre, School of Chemistry, University of Melbourne, Melbourne; and Department of Microbiology, Monash University, Clayton, Victoria, Australia. Surface protrusions of Plasmodium falciparum-infected erythrocytes, called knobs, display focal aggregates of P falciparum erythrocyte membrane protein 1 (PfEMP1), the adhesion ligand binding endothelial-cell receptors. The resulting sequestration of infected erythrocytes in tissues represents an important factor in the course of fatalities in patients with malaria. The main component of knobs is the knob-associated histidine-rich protein (KAHRP), and it contributes to altered mechanical properties of parasite-infected erythrocytes. The role of KAHRP domains in these processes is still elusive. We generated stable transgenic P falciparum-infected erythrocytes expressing mutant versions of KAHRP. Using atomic force and electron microscopy we show that the C-terminal repeat region is critical for the formation of functional knobs. Elasticity of the membrane differs dramatically between cells with different KAHRP mutations. We propose that the 5' repeat region of KAHRP is important in cross-linking to the host-cell cytoskeleton and this is required for knob protrusion and efficient adhesion under physiologic flow conditions. (Blood. 2006;108:370-378) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. Gill, M. Yogavel, A. Kumar, H. Belrhali, S. K. Jain, M. Rug, M. Brown, A. G. Maier, and A. Sharma Crystal Structure of Malaria Parasite Nucleosome Assembly Protein: DISTINCT MODES OF PROTEIN LOCALIZATION AND HISTONE RECOGNITION J. Biol. Chem., April 10, 2009; 284(15): 10076 - 10087. [Abstract] [Full Text] [PDF] Z. Bozdech, S. Mok, G. Hu, M. Imwong, A. Jaidee, B. Russell, H. Ginsburg, F. Nosten, N. P. J. Day, N. J. White, et al. The transcriptome of Plasmodium vivax reveals divergence and diversity of transcriptional regulation in malaria parasites PNAS, October 21, 2008; 105(42): 16290 - 16295. [Abstract] [Full Text] [PDF] X. Pei, X. Guo, R. Coppel, S. Bhattacharjee, K. Haldar, W. Gratzer, N. Mohandas, and X. An The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion Blood, August 1, 2007; 110(3): 1036 - 1042. [Abstract] [Full Text] [PDF]

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