Related Experiment Video
Updated: Sep 14, 2025

Author Spotlight: Studying Behavior of Acanthamoeba to Develop Targeted Strategies for Preventing Acanthamoeba Keratitis
Published on: September 20, 2024
Density-dependent cell migration in the absence of social interactions: a case study of Acanthamoeba castellanii
Nasser Ghazi1, Mete Demircigil2, Olivier Cochet-Escartin1
1UMR5306, Université Claude Bernard Lyon 1, CNRS, Institut Lumière Matière, Villeurbanne, France.
Abstract:
Cell migration is often influenced by intercellular or social interactions, ranging from long-range diffusive cues to direct contacts that can trigger biochemical signaling within the cell and affect the cell protruding activity or direction of turns. Here we study the density-dependent migration of the amoeba Acanthamoeba castellanii (Ac), a unicellular eukaryote that moves without social interactions. Using experiments and mean free path theory, we characterize how collisions affect motility parameters in crowded environments. We identify the collision rate as a key parameter linking cell density to the collision-induced reorientation rate, and we show its consistency across multiple independent approaches. Our findings reveal that the intrinsic migration speed remains constant, while persistence time and effective diffusion are entirely governed by collisions. At high densities, cells exhibit nearly ballistic trajectories between collisions, a behavior rarely reported in eukaryotes. These results establish Ac as a minimal model for motility in the absence of biochemical signaling, with implications for testing behaviors in complex crowded environments and pre-jamming dynamics.
Related Concept Videos
Cell Migration
Actin Polymerization and Cell Motility
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
Chemotaxis and Direction of Cell Migration
Cytoskeletal Coordination in Cell Migration
Diversity of Protists IV
Role of Myosin in Cell Migration
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....

