Entamoeba histolytica: molecules involved in the target cell-parasite relationship

Mol Biochem Parasitol. 1989 Nov;37(1):87-99. doi: 10.1016/0166-6851(89)90105-9.

Abstract

To detect molecules of Entamoeba histolytica involved in the trophozoite-target cell interaction, three different antisera were generated: (a) two rabbit antisera, one against total amebic proteins and another directed specifically to the 112-kDa adhesin; and (b) a mouse antiserum against amebic molecules adhering to the red blood cell (RBC) surface after incubation of RBCs with total soluble protein from trophozoites (anti-adhesion serum). All three antisera recognized the 112-kDa adhesion. Adhesion of this molecule to the RBC surface was temperature-dependent. More of the 112-kDa adhesion was found on the surface of RBCs incubated with trophozoites at 37 degrees C than on RBCs incubated at room temperature or at 0 degree C. Experiments using both anti-adhesin and anti-total ambebic protein sera revealed the presence of 210, 160, 112, 90, 70, 50, and 24-kDa proteins on RBC incubated with trophozoites. Surface proteins obtained from iodinated MDCK cells recognized amebic proteins of 112, 90, and 48-50 kDa. Virulence-deficient mutants presented a similar amount of the 112-kDa adhesin to the wild-type strain. However, in mutants, the adhesion was not functional, since they did not adhere to RBCs. 90- and 24-kDa proteins were also found to be altered in mutants.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Adhesion
  • Cell Adhesion
  • Entamoeba histolytica / analysis*
  • Entamoeba histolytica / immunology
  • Entamoeba histolytica / pathogenicity
  • Epithelial Cells
  • Erythrocytes / analysis
  • Fluorescent Antibody Technique
  • Host-Parasite Interactions*
  • Membrane Proteins / analysis*
  • Membrane Proteins / immunology
  • Phagocytosis
  • Protozoan Proteins / analysis*
  • Protozoan Proteins / immunology
  • Rabbits
  • Virulence

Substances

  • Membrane Proteins
  • Protozoan Proteins