Characterization of cell surface carbohydrate receptors for Entamoeba histolytica adherence lectin

J. I. Ravdin, Pamela Stanley, C. F. Murphy, W. A. Petri

Research output: Contribution to journalArticle

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Abstract

Binding and cytolysis of Chinese hamster ovary (CHO) cells by Entamoeba histolytica trophozoites is inhibitable by galactose (Gal) or N-acetyl-D-galactosamine (GalNAc). To better define the carbohydrate receptor for E. histolytica, we compared the binding and cytolytic target properties of 10 CHO glycosylation mutants. Each mutant expresses a uniquely altered array of N- and/or O-linked cell surface carbohydrates. Amebic adherence was reduced when lactosamine-containing N-linked carbohydrates were essentially absent (Lec1 mutant), almost undetectable when Gal and GalNAc residues were absent on both N- and O-linked carbohydrates (ldlD.Lec1 mutant), and enhanced for mutants with increased terminal Gal residues (Lec2 and Lec3). Parental CHO cells treated with neuraminidase to expose Gal residues behaved like Lec2 mutants. Binding of purified Gal or GalNAc lectin to parental, Lec1, ldlD.Lec1, and Lec2 mutant CHO cells corroborated the adherence results. The suitability of CHO cell mutants as targets for amebic cytolysis correlated with their glycosylation phenotype: the Lec1 mutants were less susceptible than parental CHO cells, the ldlD.Lec1 mutants were highly resistant, and the Lec2 mutants required higher concentrations of Gal for inhibition. The E. histolytica Gal or GalNAc adherence lectin bound preferentially to β1-6-branched, N-linked carbohydrates lacking terminal sialic acid or fucose residues. However, amebic lectin binding to either N- or O-linked cell surface carbohydrates was sufficient to initiate parasite cytolytic activity.

Original languageEnglish (US)
Pages (from-to)2179-2186
Number of pages8
JournalInfection and Immunity
Volume57
Issue number7
StatePublished - 1989
Externally publishedYes

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Entamoeba histolytica
Cell Surface Receptors
Galactose
Lectins
Cricetulus
Carbohydrates
Ovary
Glycosylation
Acetylgalactosamine
Trophozoites
Fucose
Neuraminidase
N-Acetylneuraminic Acid
Parasites
Phenotype

ASJC Scopus subject areas

  • Immunology

Cite this

Characterization of cell surface carbohydrate receptors for Entamoeba histolytica adherence lectin. / Ravdin, J. I.; Stanley, Pamela; Murphy, C. F.; Petri, W. A.

In: Infection and Immunity, Vol. 57, No. 7, 1989, p. 2179-2186.

Research output: Contribution to journalArticle

Ravdin, J. I. ; Stanley, Pamela ; Murphy, C. F. ; Petri, W. A. / Characterization of cell surface carbohydrate receptors for Entamoeba histolytica adherence lectin. In: Infection and Immunity. 1989 ; Vol. 57, No. 7. pp. 2179-2186.
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