Caenorhabditis elegans galectins LEC-1-LEC-11: Structural features and sugar-binding properties

Yoko Nemoto-Sasaki, Ko Hayama, Hiroyuki Ohya, Yoichiro Arata, Mika Kato Kaneko, Naruya Saitou, Jun Hirabayashi, Ken ichi Kasai

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)


Galectins form a large family of β-galactoside-binding proteins in metazoa and fungi. This report presents a comparative study of the functions of potential galectin genes found in the genome database of Caenorhabditis elegans. We isolated full-length cDNAs of eight potential galectin genes (lec-2-5 and 8-11) from a λZAP cDNA library. Among them, lec-2-5 were found to encode 31-35-kDa polypeptides containing two carbohydrate-recognition domains similar to the previously characterized lec-1, whereas lec-8-11 were found to encode 16-27-kDa polypeptides containing a single carbohydrate-recognition domain and a C-terminal tail of unknown function. Recombinant proteins corresponding to lec-1-4, -6, and 8-10 were expressed in Escherichia coli, and their sugar-binding properties were assessed. Analysis using affinity adsorbents with various β-galactosides, i.e., N-acetyllactosamine (Galβ1-4GlcNAc), lacto-N-neotetraose (Galβ1-4GlcNAcβ1-3Galβ1-4Glc), and asialofetuin, demonstrated that LEC-1-4, -6, and -10 have a significant affinity for β-galactosides, while the others have a relatively lower affinity. These results indicate that the integrity of key amino acid residues responsible for recognition of lactose (Galβ1-4Glc) or N-acetyllactosamine in vertebrate galectins is also required in C. elegans galectins. However, analysis of their fine oligosaccharide-binding properties by frontal affinity chromatography suggests their divergence towards more specialized functions.

Original languageEnglish
Pages (from-to)1131-1142
Number of pages12
JournalBiochimica et Biophysica Acta - General Subjects
Issue number10
Publication statusPublished - 2008 Oct
Externally publishedYes


  • Caenorhabditis elegans
  • Carbohydrate-binding property
  • Frontal affinity chromatography
  • Galectin
  • Lectin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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