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Vol. 9, Issue 8, 2069-2079, August 1998

Regulation of Adherence and Virulence by the Entamoeba histolytica Lectin Cytoplasmic Domain, Which Contains a beta 2 Integrin Motif

Richard R. Vines,*dagger Girija Ramakrishnan,dagger Dagger Joshua B. Rogers,Dagger Lauren A. Lockhart,Dagger Barbara J. Mann,*Dagger and William A. Petri Jr.*Dagger §parallel

Departments of  *Microbiology,  Dagger Medicine, and  §Pathology, University of Virginia, Charlottesville, Virginia 22908

Killing of human cells by the parasite Entamoeba histolytica requires adherence via an amebic cell surface lectin. Lectin activity in the parasite is regulated by inside-out signaling. The lectin cytoplasmic domain has sequence identity with a region of the beta 2 integrin cytoplasmic tail implicated in regulation of integrin-mediated adhesion. Intracellular expression of a fusion protein containing the cytoplasmic domain of the lectin has a dominant negative effect on extracellular lectin-mediated cell adherence. Mutation of the integrin-like sequence abrogates the dominant negative effect. Amebae expressing the dominant negative mutant are less virulent in an animal model of amebiasis. These results suggest that inside-out signaling via the lectin cytoplasmic domain may control the extracellular adhesive activity of the amebic lectin and provide in vivo demonstration of the lectin's role in virulence.


Molecular Biology of the Cell
Vol. 9, 2069-2079, August 1998
Copyright © 1998 by The American Society for Cell Biology



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