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Blood, 1 March 2004, Vol. 103, No. 5, pp. 1920-1928. Prepublished online as a Blood First Edition Paper on October 30, 2003; DOI 10.1182/blood-2003-09-3165. This Article Full Text (PDF) Supplemental Figures All Versions of this Article: 2003-09-3165v1 103/5/1920    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 Murphy, S. C Articles by Haldar, K. Search for Related Content PubMed PubMed Citation Articles by Murphy, S. C Articles by Haldar, K. Social Bookmarking                   What's this? Submitted September 15, 2003 Accepted October 20, 2003 Erythrocyte detergent-resistant membrane proteins: their characterization and selective uptake during malarial infection Sean C Murphy, Benjamin U Samuel, Travis Harrison, Kaye D Speicher, David W Speicher, Marion E Reid, Rainer Prohaska, Philip S Low, Michael J Tanner, Narla Mohandas, and Kasturi Haldar* Departments of Pathology and Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA Proteomics Facility, The Wistar Institute, Philadelphia, PA, USA New York Blood Center, New York, NY, USA Institute of Medical Biochemistry, University of Vienna, Vienna, Austria Department of Chemistry, Purdue University, West Lafayette, IN, USA Department of Biochemistry, University of Bristol, Bristol, United Kingdom * Corresponding author; email: k-haldar{at}northwestern.edu. Infection of human erythrocytes by the apicomplexan malaria parasite Plasmodium falciparum results in endovacuolar uptake of four host proteins that reside in erythrocyte detergent resistant membranes (DRMs). Whether this vacuolar transport reflects selective uptake of host DRM proteins remains unknown. A further complication is that DRMs of vastly different protein and cholesterol contents have been isolated from erythrocytes. Here we show that isolated DRMs containing the highest cholesterol-to-protein ratio have low protein mass. Liquid chromatography, mass spectrometry and antibody-based studies reveal that the major DRM proteins are band 3, flotillin-1 and -2, peroxiredoxin-2 and stomatin. Band 3 and stomatin, which reflect the bulk mass of erythrocyte DRM proteins, and all tested non-DRM proteins, are excluded from the vacuolar parasite. In contrast, flotillin-1 and -2 and eight minor DRM proteins are recruited to the vacuole. These data suggest that DRM association is necessary but not sufficient for vacuolar recruitment and there is active, vacuolar uptake of a subset of host DRM proteins. Finally, the ten internalized DRM proteins show varied lipid and peptidic anchors indicating that, contrary to the prevailing model of apicomplexan vacuole formation, DRM-association, rather than lipid anchors, provides the preferred criteria for protein recruitment to the malarial vacuole. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: N. Mohandas and P. G. Gallagher Red cell membrane: past, present, and future Blood, November 15, 2008; 112(10): 3939 - 3948. [Abstract] [Full Text] [PDF] M. D. Lazarus, T. G. Schneider, and T. F. Taraschi A new model for hemoglobin ingestion and transport by the human malaria parasite Plasmodium falciparum J. Cell Sci., June 1, 2008; 121(11): 1937 - 1949. [Abstract] [Full Text] [PDF] S. C. Murphy, S. Fernandez-Pol, P. H. Chung, S. N. Prasanna Murthy, S. B. Milne, M. Salomao, H. A. Brown, J. W. Lomasney, N. Mohandas, and K. Haldar Cytoplasmic remodeling of erythrocyte raft lipids during infection by the human malaria parasite Plasmodium falciparum Blood, September 15, 2007; 110(6): 2132 - 2139. [Abstract] [Full Text] [PDF] D. Mandal, A. Mazumder, P. Das, M. Kundu, and J. Basu Fas-, Caspase 8-, and Caspase 3-dependent Signaling Regulates the Activity of the Aminophospholipid Translocase and Phosphatidylserine Externalization in Human Erythrocytes J. Biol. Chem., November 25, 2005; 280(47): 39460 - 39467. [Abstract] [Full Text] [PDF] G. H.H. Borner, D. J. Sherrier, T. Weimar, L. V. Michaelson, N. D. Hawkins, A. MacAskill, J. A. Napier, M. H. Beale, K. S. Lilley, and P. Dupree Analysis of Detergent-Resistant Membranes in Arabidopsis. Evidence for Plasma Membrane Lipid Rafts Plant Physiology, January 1, 2005; 137(1): 104 - 116. [Abstract] [Full Text] [PDF]

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