LecA (PA-IL): A Galactose-Binding Lectin from Pseudomonas Aeruginosa
Overview
Affiliations
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.
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PMID: 39809740 PMC: 11733155. DOI: 10.1038/s41467-025-55845-7.
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PMID: 39226360 PMC: 11406247. DOI: 10.1073/pnas.2408716121.
Photoswitchable glycoligands targeting LecA.
Fan Y, El Rhaz A, Maisonneuve S, Gillon E, Fatthalla M, Le Bideau F Beilstein J Org Chem. 2024; 20:1486-1496.
PMID: 38978747 PMC: 11228623. DOI: 10.3762/bjoc.20.132.
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Sanchez H, OToole G, Berwin B Microbiol Spectr. 2023; 11(4):e0166723.
PMID: 37470715 PMC: 10434018. DOI: 10.1128/spectrum.01667-23.
Assessment of the Glycan-Binding Profile of PAO1.
Sanchez H, OToole G, Berwin B bioRxiv. 2023; .
PMID: 37131708 PMC: 10153242. DOI: 10.1101/2023.04.20.537720.