LecA (PA-IL): A Galactose-Binding Lectin from Pseudomonas aeruginosa.
Lectins
Protein-Carbohydrate Interactions
Pseudomonas aeruginosa
Surface Plasmon Resonance
X-ray crystallography
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2020
2020
Historique:
entrez:
20
4
2020
pubmed:
20
4
2020
medline:
9
3
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32306333
doi: 10.1007/978-1-0716-0430-4_25
doi:
Substances chimiques
Adhesins, Bacterial
0
Galectins
0
Globosides
0
LecA protein, bacteria
0
Melibiose
9B1VBE526I
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM