A novel immune-tolerable and permeable lectin-like protein from mushroom Agaricus bisporus

Biochem Biophys Res Commun. 2016 May 13;473(4):1090-1093. doi: 10.1016/j.bbrc.2016.04.020. Epub 2016 Apr 6.

Abstract

A lectin like protein designated as LSMT is recently discovered in Agaricus bisporus. The protein adopts very similar structure to Ricin-B like lectin from Clitocybe nebularis (CNL) and HA-33 from Clostridium botulinum (HA-33), which both recognize sugar molecules that decorate the surface of the epithelial cells of the intestine. A preliminary study in silico pointed out potential capability of LSMT to perform such biological activity. Following that hypothesis, we demonstrated that LSMT is indeed capable of penetrating out from a dialysis tube of the mice intestine origin. Furthermore, the protein appeared not to evoke the immune response upon introduction into mice, unlike its structural homologs. This is the first report on the biological implication of LSMT that might lead to its application.

Keywords: Agaricus bisporus lectin-like protein; Mushroom tyrosinase light subunit; ORF239342.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Computer Simulation
  • Female
  • Immune Tolerance / immunology*
  • Intestinal Absorption / immunology*
  • Lectins / chemistry*
  • Lectins / classification
  • Lectins / immunology*
  • Mice
  • Models, Chemical
  • Models, Immunological*
  • Permeability
  • Sequence Analysis, Protein
  • Sequence Homology, Amino Acid

Substances

  • Agaricus lectins
  • Lectins