LecA (PA-IL): A Galactose-Binding Lectin from Pseudomonas aeruginosa

Methods Mol Biol. 2020:2132:257-266. doi: 10.1007/978-1-0716-0430-4_25.

Abstract

LecA/PA-IL (Pfam PF07828) is a soluble galactose-binding lectin from bacterium Pseudomonas aeruginosa. The lectin is specific for α-galactose present on glycosphingolipids of the globoside family and has therefore been proposed to play a role in cell adhesion and in internalization of bacteria in epithelial cells. The lectin has also direct toxic activity. Search for high-affinity inhibitors can be performed on the recombinant lectin, with use of surface plasmon resonance assays and structural studies.

Keywords: Lectins; Protein-Carbohydrate Interactions; Pseudomonas aeruginosa; Surface Plasmon Resonance; X-ray crystallography.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Adhesins, Bacterial / metabolism*
  • Bacterial Adhesion
  • Binding Sites
  • Crystallography, X-Ray
  • Galectins / chemistry
  • Galectins / metabolism
  • Globosides / metabolism
  • Melibiose / metabolism*
  • Models, Molecular
  • Protein Conformation
  • Pseudomonas aeruginosa / chemistry
  • Pseudomonas aeruginosa / metabolism*
  • Surface Plasmon Resonance

Substances

  • Adhesins, Bacterial
  • Galectins
  • Globosides
  • LecA protein, bacteria
  • Melibiose