Cell polarization and adhesion in a motile pathogenic protozoan: role and fate of the Entamoeba histolytica Gal/GalNAc lectin.
The human pathogenic protozoan Entamoeba histolytica is a motile cell polarized into a front pseudopod and a rear uroid. The amoebic Gal/GalNAc surface lectin is a major adhesion molecule composed of an immunodominant 170-kDa heavy subunit, mostly extracellular except for a short cytoplasmic tail, and of an extracellular light subunit. The binding of multivalent ligands triggers lectin capping and recruitment to the uroid. The properties of the Gal/GalNAc lectin and its role in amoeba adhesion and uroid polarization are reviewed in the context of the molecular mechanisms underlying cell polarization and locomotion.
Tavares
P
P
Unité de pathogénie microbienne moléculaire et Inserm U389, Institut Pasteur, Rue du Dr. Roux 28, F-75724 cedex 15, Paris, France.
Sansonetti
P
P
Guillén
N
N
D000116:Acetylgalactosamine / Q000378:metabolism; D000818:Animals; D002448:Cell Adhesion; D002465:Cell Movement; D016764:Cell Polarity; D004748:Entamoeba histolytica / Q000166:cytology / Q000502:physiology*; D004749:Entamoebiasis / Q000469:parasitology*; D005690:Galactose / Q000378:metabolism; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D015800:Protozoan Proteins / Q000737:chemistry / Q000378:metabolism
D037102:Lectins; D015800:Protozoan Proteins; C078014:N-acetylgalactosamine inhibitable lectin 35-kDa subunit, Entamoeba histolytica; D000116:Acetylgalactosamine; D005690:Galactose