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Prepublished online as a Blood First Edition Paper on May 1, 2003; DOI 10.1182/blood-2002-11-3513. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-11-3513v1 102/5/1911    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 Waller, K. L. Articles by Coppel, R. L. Search for Related Content PubMed PubMed Citation Articles by Waller, K. L. Articles by Coppel, R. L. Related Collections Red Cells Cytoskeleton Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 September 2003, Vol. 102, No. 5, pp. 1911-1914 RED CELLS Brief report Mature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells Karena L. Waller, Wataru Nunomura, Xiuli An, Brian M. Cooke, Narla Mohandas, and Ross L. Coppel From the Department of Microbiology and the Victorian Bioinformatics Consortium, Monash University, Melbourne, Victoria, Australia; Department of Biochemistry, School of Medicine, Tokyo Women's Medical University, Tokyo, Japan; and New York Blood Center, New York, NY. The Plasmodium falciparum mature parasite-infected erythrocyte surface antigen (MESA) is exported from the parasite to the infected red blood cell (IRBC) membrane skeleton, where it binds to protein 4.1 (4.1R) via a 19-residue MESA sequence. Using purified RBC 4.1R and recombinant 4.1R fragments, we show MESA binds the 30-kDa region of RBC 4.1R, specifically to a 51-residue region encoded by exon 10 of the 4.1R gene. The 3D structure of this region reveals that the MESA binding site overlaps the region of 4.1R involved in the p55, glycophorin C, and 4.1R ternary complex. Further binding studies using p55, 4.1R, and MESA showed competition between p55 and MESA for 4.1R, implying that MESA bound at the IRBC membrane skeleton may modulate normal 4.1R and p55 interactions in vivo. Definition of minimal binding domains involved in critical protein interactions in IRBCs may aid the development of novel therapies for falciparum malaria. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: F. K. Glenister, K. M. Fernandez, L. M. Kats, E. Hanssen, N. Mohandas, R. L. Coppel, and B. M. Cooke Functional alteration of red blood cells by a megadalton protein of Plasmodium falciparum Blood, January 22, 2009; 113(4): 919 - 928. [Abstract] [Full Text] [PDF] X. Pei, X. Guo, R. Coppel, N. Mohandas, and X. An Plasmodium falciparum Erythrocyte Membrane Protein 3 (PfEMP3) Destabilizes Erythrocyte Membrane Skeleton J. Biol. Chem., September 14, 2007; 282(37): 26754 - 26758. [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] X. Pei, X. An, X. Guo, M. Tarnawski, R. Coppel, and N. Mohandas Structural and Functional Studies of Interaction between Plasmodium falciparum Knob-associated Histidine-rich Protein (KAHRP) and Erythrocyte Spectrin J. Biol. Chem., September 2, 2005; 280(35): 31166 - 31171. [Abstract] [Full Text] [PDF]

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