Entamoeba histolytica: lipid rafts are involved in adhesion of trophozoites to host extracellular matrix components.

Lipid microdomains are involved in adhesion of Entamoeba histolytica trophozoites to host extracellular matrix components

Fibronectin-derived fragments as inducers of adhesion and chemotaxis of Entamoeba histolytica trophozoites.

Active migration of Entamoeba histolytica trophozoites through extracellular matrixes might play a role in host tissue destruction. Trophozoites degrade soluble fibronectin (FN) bound to their surface and adhere to substrate-bound FN, producing local degradation. FN proteolytic fragments were used to determine the nature of adhesion and motility-promoting domains within the protein. The 70-kDa ...

The major neutral proteinase of Entamoeba histolytica

FPLC anion-exchange and chromatofocusing chromatography were used to purify the major neutral proteinase from secretions of axenically cultured Entamoeba histolytica trophozoites. HM-1 strain trophozoites, which were more proteolytically active than the less virulent HK-9 strain, were used for purification of the enzyme. It is a thiol proteinase with a subunit Mr of approximately 56,000, a neut...

Localization of phosphatidylinositol 4,5-bisphosphate to lipid rafts and uroids in the human protozoan parasite Entamoeba histolytica.

Entamoeba histolytica is an intestinal protozoan parasite and is the causative agent of amoebiasis. During invasive infection, highly motile amoebae destroy the colonic epithelium, enter the blood circulation, and disseminate to other organs such as liver, causing liver abscess. Motility is a key factor in E. histolytica pathogenesis, and this process relies on a dynamic actomyosin cytoskeleton...

Entamoeba histolytica: a beta 1 integrin-like fibronectin receptor assembles a signaling complex similar to those of mammalian cells.

During tissue invasion, Entamoeba histolytica trophozoites interact with endothelial cells and extracellular matrix (ECM) proteins such as fibronectin (FN), collagen, and laminin. It has been demonstrated that trophozoites interact with FN through a beta1 integrin-like FN receptor (beta 1EhFNR), activating tyrosine kinases. In order to characterize the signaling process triggered by the amoebic...