Sequence and structure of the galactose adherence lectin of Entamoeba histolytica
Mann, B.J.; Young, C.Y.; Petri, W.A.
Archives of Medical Research 23(2): 55-56
1992
ISSN/ISBN: 0188-4409 PMID: 1285085 Document Number: 402128
Entamoeba histolytica adheres to human colonic mucin, epithelial cells and other target cells via a galactose-inhibitable lectin. The purified lectin is a heterodimeric protein consisting of a 170 000 and a 35 000 MW subunit. Monoclonal antibodies (mAb), specific for 7 non-overlapping epitopes on the 170 000 MW subunit, have been shown to inhibit, enhance, or have no effect on amoebic adherence. The purpose of this study was to map the linear epitopes recognized by these 170 000 MW-specific mAbs. Fusion protein lecA was found to react with 6 of these 7 mAbs. The results indicate that these 6 epitopes were contained within 538 amino acids of the cysteine-rich domain of the 170 000 MW subunit.