Document Type

Article

Publication Date

10-2008

Publication Title

Experimental Parasitology

Volume

120

Issue

2

Publisher

Elsevier

Abstract

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-β-cyclodextrin (MβCD), resulted in inhibition of adhesion to collagen, and to a lesser extent, to fibronectin. Replenishment of cholesterol in MβCD-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.

Comments

This manuscript has been published in the journal Experimental Parasitology. Please find the published version here (note that a subscription is necessary to access this version):

http://www.sciencedirect.com/science/article/pii/S001448940800146X

Elsevier holds the copyright in this article

Download

Included in

Microbiology Commons

Share

COinS