Identification of significant variation in the composition of lipophosphoglycan-like molecules of E. histolytica and E. dispar.
Moody S. Becker S. Nuchamowitz Y. Mirelman D.
Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot, Israel.
The lipophosphoglycan-like (LPG-like) molecules of E. histolytica virulent strains are clearly distinct from those of the avirulent E. histolytica and E. dispar strains. Abundant 'LPG' levels are apparently limited to virulent strains, while lipophosphopeptidoglycans ('LPPG's) are common to both virulent and avirulent strains of E. histolytica and E. dispar. It is therefore conceivable that 'LPPG' performs a function that is essential to survival within the host, while the 'LPG' performs a more specific function related to virulence.
Functional heterogeneity of colonic adenocarcinoma mucins for inhibition of Entamoeba histolytica adherence to target cells.
Gottke MU. Keller K. Belley A. Garcia RM. Hollingsworth MA. Mack DR. Chadee K.
Institute of Parasitology, McGill University, Quebec, Canada.
Mucins secreted from the gastrointestinal epithelium from the basis of the adherent mucus layer which is the host's first line of defense against invasion by Entamoeba histolytica. Galactose and N-acetyl-D-galactosamine residues of mucins specifically inhibit binding of the amebic 170 kDa heavy subunit Gal-lectin to target cells, an absolute prerequisite for pathogenesis. Herein we characterized the secretory mucins isolated from the human colon and from three human colonic adenocarcinoma cell lines: two with goblet cell-like (LS174T and T84) and one with absorptive cell-like morphology (Caco-2). By Northern blot analysis the intestinal mucin genes MUC2 and MUC3 were constitutively expressed by confluent LS174T and Caco-2 cells, whereas T84 cells only transcribed MUC2 and not MUC3 mRNA. 3H-glucosamine and 3H-threonine metabolically labeled proteins separated as high M, mucins in the void (Vo > 10(6) Da) of Sepharose-4B column chromatography and remained in the stacking gel of SDS-PAGE as depicted by fluorography. All mucin preparations contained high amounts of N-acetyl-glucosamine, galactose, N-acetyl-galactosamine, fucose and sialic acid, saccharides typical of the O-linked carbohydrate side chains. Mucin samples from the human colon and from LS174T and Caco-2 cells inhibited E. histolytica adherence to chinese hamster ovary cells, whereas mucins from T84 cells did not. These results suggest that genetic heterogeneity and/or posttranslational modification in glycosylation of colonic mucins can affect specific epithelial barrier function against intestinal pathogens.