Related Experiment Video
Updated: Aug 15, 2026

Analysis of the Epithelial Damage Produced by Entamoeba histolytica Infection
Published on: June 12, 2014
Characterization of Entamoeba histolytica alpha-actinin
1Biochemistry, Umeå University, SE-901 87 Umeå, Sweden.
Abstract:
We have cloned, expressed and characterized a alpha-actinin-like protein of Entamoeba histolytica. Analysis of the primary structure reveals that the essential domains of the alpha-actinin protein family are conserved: an N-terminus actin-binding domain, a C-terminus calcium-binding domain and a central helical rod domain. However, the rod domain of this Entamoeba protein is considerably shorter than the rod domain in alpha-actinins of higher organisms. The cloned Entamoeba 63 kDa protein is recognized by conventional alpha-actinin antibodies as well as binds and cross-links filamentous actin and calcium ions in the same manner as alpha-actinins. Despite the shorter rod domain this protein has conserved the most important functions of alpha-actinins. Therefore, it is suggested that this 63 kDa protein is an atypical and ancestral alpha-actinin.
Related Concept Videos
Introduction to Actin
Actin Polymerization and Cell Motility
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Amebiasis
The Sarcomere
Each myosin...
Cytoskeletal Proteins in Bacteria
The Role of Actin and Myosin in Non-muscle Cells

