Regulation of Adherence and Virulence by the<i>Entamoeba histolytica</i>Lectin Cytoplasmic Domain, Which Contains a β2 Integrin Motif
-
- Richard R. Vines
- Departments of Microbiology,
-
- Girija Ramakrishnan
- Medicine, and
-
- Joshua B. Rogers
- Medicine, and
-
- Lauren A. Lockhart
- Medicine, and
-
- Barbara J. Mann
- Departments of Microbiology,
-
- William A. Petri
- Departments of Microbiology,
-
- W. James Nelson
- editor
説明
<jats:p>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 β2 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.</jats:p>
収録刊行物
-
- Molecular Biology of the Cell
-
Molecular Biology of the Cell 9 (8), 2069-2079, 1998-08
American Society for Cell Biology (ASCB)