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

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Lectin Purification and Analysis

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2132))

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.

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Acknowledgments

The authors acknowledge support by the ANR PIA Glyco@Alps (ANR-15-IDEX-02), Labex ARCANE and CBH-EUR-GS (ANR-17-EURE-0003), and the French Cystic Fibrosis Association Vaincre la Mucoviscidose.

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Correspondence to Anne Imberty .

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Kuhaudomlarp, S., Gillon, E., Varrot, A., Imberty, A. (2020). LecA (PA-IL): A Galactose-Binding Lectin from Pseudomonas aeruginosa. In: Hirabayashi, J. (eds) Lectin Purification and Analysis. Methods in Molecular Biology, vol 2132. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0430-4_25

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  • DOI: https://doi.org/10.1007/978-1-0716-0430-4_25

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-0429-8

  • Online ISBN: 978-1-0716-0430-4

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