A novel core 1 O-linked glycan-specific binding lectin from the fruiting body of Hericium erinaceus

Int J Biol Macromol. 2018 Feb;107(Pt B):1528-1537. doi: 10.1016/j.ijbiomac.2017.10.018. Epub 2017 Oct 6.


Mucin-type O-glycans are involved in biological functions on the cell surface as well as the glycoproteins and can also be used as specific carbohydrate biomarkers of many diseases. In this study, I purified a novel core 1 O-linked glycan specific lectin, Hericium erinaceus lecin (HeL), from the fruiting body of the mushroom Hericium erinaceus, which is known as the natural source for a sialic acid-binding lectin. Upon optimization of the purification conditions, a sequence of ion exchange, affinity, ion exchange, and size-exclusion chromatography resulted in the highest yield and best quality of lectin without protease activity. The resulting purified HeL is an apparent hexameric protein with a subunit molecular weight of 15kDa, and a pI of 4.3. In hemagglutination inhibition assay, the purified lectin was only inhibited by glycoproteins containing mucin-type O-glycans and reacted weakly with Galβ(1,3)GalNAc. Glycan array analyses showed that HeL specifically interacts with core 1 O-linked glycans as well as extended O-glycan structures containing sialylation or fucosylation. The glycan binding specificity of HeL is comparable to that of peanut agglutinin for detection of a broader range of extended core 1 O-glycan structures. Taken together, these results provide an efficient and optimized procedure for the purification of HeL from the fruiting body of the mushroom Hericium erinaceus. Moreover, HeL represents a powerful tool for analyzing core 1 and extended core 1 O- glycan structures in diagnosis assays.

Keywords: Core 1 O-linked glycan; Galβ(1,3)GalNAc; Hericium erinaceus; Lectin; Mushroom.

MeSH terms

  • Animals
  • Basidiomycota / chemistry*
  • Carbohydrates / chemistry
  • Chromatography, Affinity
  • Fruiting Bodies, Fungal / chemistry*
  • Fungal Proteins / chemistry
  • Fungal Proteins / isolation & purification
  • Fungal Proteins / metabolism*
  • Glycosylation
  • Hemagglutination
  • Lectins / chemistry
  • Lectins / isolation & purification
  • Lectins / metabolism*
  • Peptide Hydrolases / metabolism
  • Polysaccharides / chemistry
  • Polysaccharides / isolation & purification
  • Polysaccharides / metabolism*
  • Protein Binding
  • Sus scrofa


  • Carbohydrates
  • Fungal Proteins
  • Lectins
  • Polysaccharides
  • Peptide Hydrolases