Molecular and functional characterization of a tandem-repeat galectin from the freshwater snail Biomphalaria glabrata, intermediate host of the human blood fluke Schistosoma mansoni.
Gene, 2008/3/31;411(1-2):46-58.
Yoshino TP[1], Dinguirard N, Kunert J, Hokke CH
Affiliations
PMID: 18280060DOI: 10.1016/j.gene.2008.01.003
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Abstract
In the present study, a tandem-repeat type galectin was characterized from an embryonic cell line (Bge) and circulating hemocytes of the snail Biomphalaria glabrata, intermediate host of the human blood fluke Schistosoma mansoni. The predicted B. glabrata galectin (BgGal) protein of 32 kDa possessed 2 carbohydrate recognition domains, each displaying 6 of 8 conserved amino acids involved in galactoside-binding activity. A recombinant BgGal (rBgGal) demonstrated hemagglutinating activity against rabbit erythrocytes, which was specifically inhibited by galactose-containing sugars (lacNAc/lac>galNAc/gal). Although native galectin was immunolocalized in the cytoplasm of Bge cells and the plasma membrane of a subset of snail hemocytes (60%), it was not detected in cell-free plasma by Western blot analysis. The findings that rBgGal selectively recognizes the schistosome-related sugar, lacNAc, and strongly binds to hemocytes and the tegument of S. mansoni sporocysts in a sugar-inhibitable fashion suggest that hemocyte-bound galectin may be serving as a pattern recognition receptor for this, or other pathogens possessing appropriate sugar ligands. Based on molecular and functional features, BgGal represents an authentic galectin, the first to be fully characterized in the medically-important molluscan Class Gastropoda.
MeSH terms
Amino Acid Sequence; Animals; Antibodies; Base Sequence; Biomphalaria; Cell Line; Cloning, Molecular; Disease Vectors; Galectins; Hemocytes; Host-Parasite Interactions; Humans; Molecular Sequence Data; Recombinant Proteins; Schistosoma mansoni; Sequence Analysis, Protein; Tandem Repeat Sequences
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