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Infection and Immunity, September 2001, p. 5892-5898, Vol. 69, No. 9
Department of Infectious Diseases, Tokai
University School of Medicine, Bohseidai, Isehara, Kanagawa 259-1193, Japan1; Departments of Medicine,
Microbiology, and Pathology, University of Virginia,
Charlottesville, Virginia 22908-13402; and
The Institute for Genomic Research, Rockville, Maryland
208503
Received 27 February 2001/Returned for modification 23 April
2001/Accepted 4 June 2001
Killing by Entamoeba histolytica requires parasite
adherence to host galactose- and
N-acetyl-D-galactosamine
(Gal/GalNAc)-containing cell surface receptors. A 260-kDa heterodimeric
E. histolytica Gal/GalNAc lectin composed of heavy (Hgl)
and light (Lgl) subunits has been previously described. Here we present
the cloning and characterization of Igl, a 150-kDa intermediate subunit
of the Gal/GalNAc lectin. Igl, Hgl, and Lgl colocalized on the surface membrane of trophozoites. Two unlinked copies of genes encoding Igl
shared 81% amino acid sequence identity (GenBank accession no.
AF337950 and AF337951). They encoded cysteine-rich proteins with amino-
and carboxy-terminal hydrophobic signal sequences characteristic of
glycosylphosphatidylinositol (GPI)-anchored membrane proteins.
The igl genes lacked carbohydrate recognition domains but
were members of a large family of amebic genes containing CXXC and CXC
motifs. These data indicate that Igl is part of the parasite's
multimolecular Gal/GalNAc adhesin required for host interaction.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.9.5892-5898.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Intermediate Subunit of the Gal/GalNAc Lectin of Entamoeba
histolytica Is a Member of a Gene Family Containing Multiple
CXXC Sequence Motifs
*
Corresponding author. Present address: Room 2115 MR4,
Division of Infectious Diseases, P.O. Box 801340, University of
Virginia Health System, Charlottesville, VA 22908-1340. Phone: (434)
924-5621. Fax: (434) 924-0075. E-mail: wap3g{at}virginia.edu.
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