Chinese hamster ovary cells deficient in N-acetylglucosaminyltransferase I activity are resistant to Entamoeba histolytica-mediated cytotoxicity

Infect Immun. 1989 Jan;57(1):8-12. doi: 10.1128/iai.57.1.8-12.1989.

Abstract

To study the relationship between carbohydrate-specific amebic cytoadherence and ameba-mediated cytotoxicity, we measured Entamoeba histolytica trophozoite-mediated cytolysis directed against a panel of four Chinese hamster ovary (CHO) cell lines that have defined alterations in their glycosylation patterns. We recently measured amebic trophozoite adherence to this panel of CHO cells and showed that trophozoites bind variant cells (RICR 15B), which are deficient in Asn-linked N-acetyllactosamine units, at 12% of the level observed for wild-type cells (E. Li, A. Becker, and S. L. Stanley, J. Exp. Med 167:1725-1730, 1988). Using a 51Cr release assay to measure trophozoite-mediated cytolysis, we demonstrate in this study that RICR 15B cells are less susceptible to trophozoite-mediated cytolysis than are wild-type cells. In addition, we found that N-acetyllactosamine, which inhibits trophozoite adherence to CHO cells, also inhibited trophozoite-mediated cytolysis of wild-type cells. These studies indicate that surface carbohydrates on target cells can influence susceptibility to ameba-mediated cytotoxicity. This panel of CHO cells provides a useful model system for investigating the role of glycoconjugates in mediating amebic interactions with mammalian cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosaminidase / deficiency*
  • Adhesiveness
  • Amino Sugars / pharmacology
  • Animals
  • Cell Line
  • Cricetinae
  • Cricetulus
  • Cytotoxicity, Immunologic* / drug effects
  • Entamoeba histolytica / growth & development
  • Entamoeba histolytica / immunology*
  • Entamoeba histolytica / physiology
  • Female
  • Hexosaminidases / deficiency*
  • Immunity, Innate
  • Lactose / pharmacology
  • Ovary / enzymology
  • Ovary / immunology*
  • Ovary / microbiology

Substances

  • Amino Sugars
  • N-acetyllactosamine
  • Hexosaminidases
  • Acetylglucosaminidase
  • Lactose