Journal
EXPERIMENTAL PARASITOLOGY
Volume 120, Issue 2, Pages 127-134Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.exppara.2008.06.003
Keywords
adhesion; cholesterol; collagen; Entamoeba histolytica; extracellular matrix; fibronectin; lipid raft
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Funding
- National Institute of Allergy and Infectious Diseases [R01AI046414]
- South Carolina IDeA Network of Biomedical Research Excellence (INBRE)
- CSREES/USDA [SC-1700312]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI046414] Funding Source: NIH RePORTER
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Adhesion is an important virulence function for Entamoeba histolytica, the causative agent of amoebic dysentery. Lipid rafts, cholesterol-rich domains, function in compartmentalization of cellular processes. In E. histolytica, rafts participate in parasite-host cell interactions; however, their role in parasite-host extracellular matrix (ECM) interactions has not been explored. Disruption of rafts with a cholesterol extracting agent, methyl-beta-cyclodextrin (M beta CD), resulted in inhibition of adhesion to collagen, and to a lesser extent, to fibronectin. Replenishment of cholesterol in M beta CD-treated cells, using a lipoprotein-cholesterol concentrate, restored adhesion to collagen. Confocal microscopy revealed enrichment of rafts at parasite-ECM interfaces. A raft-resident adhesin, the galactose/N-acetylgalactosamine-inhibitable lectin, mediates interaction to host cells by binding to galactose or N-acetylgalactosamine moieties on host glycoproteins. In this study, galactose inhibited adhesion to collagen, but not to fibronectin. Together these data suggest that rafts participate in E. histolytica-ECM interactions and that raft-associated Gal/GalNAc lectin may serve as a collagen receptor. (C) 2008 Elsevier Inc. All rights reserved.
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