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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
Sakonwan Kuhaudomlarp 1 , Emilie Gillon 1 , Annabelle Varrot 1 , Anne Imberty 2
Sakonwan Kuhaudomlarp 1 , Emilie Gillon 1 , Annabelle Varrot 1 , Anne Imberty 2

[No authors listed]

Author information
  • 1 Univ. Grenoble Alpes, CNRS, CERMAV, Grenoble, Alpes, France.
  • 2 Univ. Grenoble Alpes, CNRS, CERMAV, Grenoble, Alpes, France. anne.imberty@cermav.cnrs.fr.

摘要


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