Relative intensities of recognition factors at two combining sites of Ralstonia solanacearum lectin (RSL) for accommodating LFucα1-->, DManα1--> and Galβ1-->3/4GlcNAc glycotopes

FEBS Lett. 2012 May 7;586(9):1294-9. doi: 10.1016/j.febslet.2012.03.024. Epub 2012 Apr 3.

Abstract

Owing to the weak reactivities of monomeric DManα1 and Galβ1-->3/4GlcNAcβ (I(β)/II(β)) glycotopes with Ralstonia solanacearum lectin (RSL), their recognition roles were previously ignored. In this study, the interaction intensities of RSL toward four monomeric glycotopes LFucα1-->, DManα1--> and I(β)/II(β) within two combining sites were established by both enzyme-linked lectinosorbent and inhibition assays. It was found that high density of LFucα1--> complex enhanced the recognition intensities at LFucα1--> site, polyvalent DManα1--> was essential for binding at the DManα1--> site and polyvalent I(β)/II(β) was required at LFucα1--> site. The peculiar recognition systems of RSL are very different from other well known microbial lectins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / chemistry*
  • Acetylglucosamine / metabolism*
  • Animals
  • Binding Sites
  • Carbohydrate Sequence
  • Glycoproteins / metabolism
  • Mannans / metabolism
  • Molecular Sequence Data
  • Protein Binding
  • Ralstonia solanacearum*
  • Receptors, N-Acetylglucosamine / metabolism*

Substances

  • Glycoproteins
  • Mannans
  • Receptors, N-Acetylglucosamine
  • Acetylglucosamine