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Background  The infectious and diagnostic form of  Entamoeba histolytica  (Eh), cause of amebic dysentery and liver abscess, is the quadranucleate cyst. The cyst wall of  Entamoeba invadens  (Ei), a model for Eh, is composed of chitin fibrils and three sets of chitin-binding lectins that cross-link chitin fibrils (multivalent Jacob lectins), self-aggregate (Jessie lectins), and remodel chitin (chitinase). The goal here was to determine how well the Ei model applies to  Entamoeba  cysts from humans.    Methods/Results  An Eh Jacob lectin (EhJacob2) has three predicted chitin-binding domains surrounding a large, Ser-rich spacer. Recombinant EhJacob2 made in transfected Eh trophozoites binds to particulate chitin. Sequences of PCR products using primers flanking the highly polymorphic spacer of EhJacob2 may be used to distinguish  Entamoeba  isolates. Antibodies to the EhJacob2, EhJessie3, and chitinase each recognize cyst walls of clinical isolates of  Entamoeba . While numerous sera from patients with amebic intestinal infections and liver abscess recognize recombinant EhJacob1 and EhJessie3 lectins, few of these sera recognize recombinant EhJacob2.    Conclusions/Significance  The EhJacob2 lectin binds chitin and is polymorphic, and Jacob2, Jessie3, and chitinase are present in cyst walls of clinical isolates of  Entamoeba . These results suggest there are substantial similarities between cysts of the human pathogen (Eh) and the  in vitro  model (Ei), even though there are quantitative and qualitative differences in their chitin-binding lectins.

The Jacob2 Lectin of the Entamoeba histolytica Cyst Wall Binds Chitin and Is Polymorphic