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TitleStructural basis for carbohydrate recognition by the Gal/GalNAc lectin of Entamoeba histolytica involved in host cell adhesion.
Journal, issue, pagesPLoS Pathog, Vol. 22, Issue 2, Page e1013948, Year 2026
Publish dateFeb 24, 2026
AuthorsSamuel F Gérard / Christina Redfield / Matthew K Higgins /
PubMed AbstractIntestinal amoebiasis is caused by Entamoeba histolytica, one of the deadliest human-infective parasites. Central to its pathogenicity is its binding to mucosal carbohydrates, which precedes tissue ...Intestinal amoebiasis is caused by Entamoeba histolytica, one of the deadliest human-infective parasites. Central to its pathogenicity is its binding to mucosal carbohydrates, which precedes tissue damage by trogocytosis. Carbohydrate binding is mediated by a single adhesin, the galactose/N-acetylgalactosamine (Gal/GalNAc) lectin, which is the leading vaccine candidate for amoebiasis. We present the structure of the native heterodimeric lectin, revealing an ordered core containing the light chain and the N-terminal region of the heavy chain. Structures obtained in the presence of ligand show that the Gal/GalNAc binding site is in the light chain, which adopts a β-trefoil fold found in other lectins. An elongated arm emerges from the heavy chain, which adopts multiple positions and may be modulated by sugar binding. This study reveals the molecular basis for sugar binding by the Entamoeba histolytica Gal/GalNAc lectin, a prerequisite for parasite invasion and development of intestinal disease.
External linksPLoS Pathog / PubMed:41734235 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.818 - 3.9 Å
Structure data

51385

9gja

EMDB-51385, PDB-9gja:
Entamoeba histolytica Gal/GalNAc lectin, mode 1
Method: EM (single particle) / Resolution: 3.7 Å

51386

9gjb

EMDB-51386, PDB-9gjb:
Entamoeba histolytica Gal/GalNAc lectin, mode 2
Method: EM (single particle) / Resolution: 3.5 Å

51387

9gjc

EMDB-51387, PDB-9gjc:
Entamoeba histolytica Gal/GalNAc lectin, mode 3
Method: EM (single particle) / Resolution: 3.9 Å

51392

9gjh

EMDB-51392, PDB-9gjh:
Entamoeba histolytica Gal/GalNAc lectin bound to galactose, mode 1
Method: EM (single particle) / Resolution: 3.0 Å

51393

9gji

EMDB-51393, PDB-9gji:
Entamoeba histolytica Gal/GalNAc lectin bound to galactose, mode 2
Method: EM (single particle) / Resolution: 3.4 Å

51394

9gjj

EMDB-51394, PDB-9gjj:
Entamoeba histolytica Gal/GalNAc lectin bound to galactose, mode 3
Method: EM (single particle) / Resolution: 3.9 Å

51395

9gjk

EMDB-51395, PDB-9gjk:
Entamoeba histolytica Gal/GalNAc lectin bound to LacNAc, mode 1
Method: EM (single particle) / Resolution: 3.3 Å

51396

9gjl

EMDB-51396, PDB-9gjl:
Entamoeba histolytica Gal/GalNAc lectin bound to LacNAc, mode 2
Method: EM (single particle) / Resolution: 3.4 Å

51397

9gjm

EMDB-51397, PDB-9gjm:
Entamoeba histolytica Gal/GalNAc lectin bound to LacNAc, mode 3
Method: EM (single particle) / Resolution: 3.9 Å

PDB-9ged:
Entamoeba histolytica Gal/GalNAc lectin heavy chain residues 808-992
Method: X-RAY DIFFRACTION / Resolution: 2.484 Å

PDB-9gee:
Entamoeba histolytica Gal/GalNAc lectin heavy chain residues 808-992 in the presence of galactose
Method: X-RAY DIFFRACTION / Resolution: 1.818 Å

PDB-9geg:
Entamoeba histolytica Gal/GalNAc lectin heavy chain residues 808-992 in the presence of GalNAc
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-9geh:
Entamoeba histolytica Gal/GalNAc lectin heavy chain residues 808-992 in the presence of LacNAc
Method: X-RAY DIFFRACTION / Resolution: 2.319 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-GAL:
beta-D-galactopyranose

Source
  • entamoeba histolytica hm-1:imss (eukaryote)
  • entamoeba histolytica (eukaryote)
KeywordsCELL ADHESION / Entamoeba histolytica / lectin / Gal/GalNAc / trogocytosis

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