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A LecA Ligand Identified from a Galactoside-Conjugate Array Inhibits Host Cell Invasion by Pseudomonas aeruginosa

Authors
Eierhoff, Thorsten
Topin, Jérémie
Varrot, Annabelle
Imberty, Anne
Römer, Winfried
Published in Angewandte Chemie: International Edition. 2014, vol. 53, no. 34, p. 8885-8889
Abstract Lectin LecA is a virulence factor of Pseudomonas aeruginosa involved in lung injury, mortality, and cellular invasion. Ligands competing with human glycoconjugates for LecA binding are thus promising candidates to counteract P. aeruginosa infections. We have identified a novel divalent ligand from a focused galactoside(Gal)-conjugate array which binds to LecA with very high affinity (Kd=82 nm). Crystal structures of LecA complexed with the ligand together with modeling studies confirmed its ability to chelate two binding sites of LecA. The ligand lowers cellular invasiveness of P. aeruginosa up to 90 % when applied in the range of 0.05–5 μm. Hence, this ligand might lead to the development of drugs against P. aeruginosa infection.
Keywords Bacterial invasionGlycan arrayLecALectinsP. aeruginosa
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Other version: http://doi.wiley.com/10.1002/anie.201402831
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NOVOA, Alexandre et al. A LecA Ligand Identified from a Galactoside-Conjugate Array Inhibits Host Cell Invasion by Pseudomonas aeruginosa. In: Angewandte Chemie: International Edition, 2014, vol. 53, n° 34, p. 8885-8889. https://archive-ouverte.unige.ch/unige:39381

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Deposited on : 2014-08-13

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