AFM investigation of Pseudomonas aeruginosa lectin LecA (PA-IL) filaments induced by multivalent glycoclusters

Sicard, Delphine; Cecioni, Samy; Iazykov, Maksym; Chevolot, Yann; Matthews, Susan E.; Praly, Jean‐Pierre; Souteyrand, Éliane; Imberty, Anne; Vidal, Sébastien; Phaner‐Goutorbe, Magali

doi:10.1039/c1cc13097h

Cited by 63 publications

(73 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…37, 53–55 Binding of PA-IL to glycoconjugates on surfaces or membranes has also been demonstrated to be more efficient than to monovalent compounds in solution. 56 The data obtained from the ITC experiment on porphyrin 2a /PA-IL were in the range of 100 nM for both the solution and FET experiments, in agreement with the chelating effect since compound 2a is tetravalent.…”

Section: Resultssupporting

confidence: 62%

Electronic Detection of Lectins Using Carbohydrate-Functionalized Nanostructures: Graphene versus Carbon Nanotubes

et al. 2011

Self Cite

View full text Add to dashboard Cite

Here we investigated the interactions between lectins and carbohydrates using field-effect transistor (FET) devices comprised of chemically converted graphene (CCG) and single-walled carbon nanotubes (SWNTs). Pyrene- and porphyrin-based glycoconjugates were functionalized noncovalently on the surface of CCG-FET and SWNT-FET devices, which were then treated with 2 µM of nonspecific and specific lectins. In particular, three different lectins (PA-IL, PA-IIL and ConA) and three carbohydrate epitopes (galactose, fucose and mannose) were tested. The responses of 36 different devices were compared and rationalized using computer-aided models of carbon nanostructure/glycoconjugate interactions. Glycoconjugates surface coverage in addition to one-dimensional structures of SWNTs resulted in optimal lectin detection. Additionally, lectin titration data of SWNT- and CCG-based biosensors were used to calculate lectin dissociation constants (Kd) and compare them to the values obtained from the isothermal titration microcalorimetry (ITC) technique.

show abstract

Section: Resultssupporting

confidence: 62%

Electronic Detection of Lectins Using Carbohydrate-Functionalized Nanostructures: Graphene versus Carbon Nanotubes

et al. 2011

Self Cite

View full text Add to dashboard Cite

show abstract

“…The design of glycoclusters based on aromatic scaffolds has attracted much attention recently taking advantage of the intrinsic physico‐chemical properties of the different cores . We have recently designed a series of multivalent scaffolds based on calixarenes, resorcinarenes, porphyrins, and fullerenes . In all cases, the grafting of carbohydrate residues onto these central cores yielded glycoclusters displaying improved lectin binding properties in comparison to their monovalent natural ligands …”

Section: Introductionmentioning

confidence: 99%

Pillar[5]arene‐Based Glycoclusters: Synthesis and Multivalent Binding to Pathogenic Bacterial Lectins

Buffet

Nierengarten

Galanos

et al. 2016

Chemistry A European J

Self Cite

View full text Add to dashboard Cite

The synthesis of pillar[5]arene-based glycoclusters has been readily achieved by CuAAC conjugations of azido- and alkyne-functionalized precursors. The lectin binding properties of the resulting glycosylated multivalent ligands have been studied by at least two complementary techniques to provide a good understanding. Three lectins were selected from bacterial pathogens based on their potential therapeutic applications as anti-adhesives, namely LecA and LecB from Pseudomonas aeruginosa and BambL from Burkholderia ambifaria. As a general trend, multivalency improved the binding to lectins and a higher affinity can be obtained by increasing to a certain limit the length of the spacer arm between the carbohydrate subunits and the central macrocyclic core.

show abstract

“…As shown in in Figure 4, as the concentration of the ligand on the surface is reduced (hybridizing from 2.5 to 0.03 mm of library, 3-fold dilution), the signal ratio between the fittest divalent ligand and its monomeric version increases. [21] At lower ligand concentration and hence surface density, the binding to the divalent ligand is preferred compared to the [21] At lower ligand concentration and hence surface density, the binding to the divalent ligand is preferred compared to the …”

mentioning

confidence: 99%

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

et al. 2014

Self Cite

View full text Add to dashboard Cite

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.

show abstract

AFM investigation of Pseudomonas aeruginosa lectin LecA (PA-IL) filaments induced by multivalent glycoclusters

Cited by 63 publications

References 28 publications

Electronic Detection of Lectins Using Carbohydrate-Functionalized Nanostructures: Graphene versus Carbon Nanotubes

Electronic Detection of Lectins Using Carbohydrate-Functionalized Nanostructures: Graphene versus Carbon Nanotubes

Pillar[5]arene‐Based Glycoclusters: Synthesis and Multivalent Binding to Pathogenic Bacterial Lectins

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

Contact Info

Product

Resources

About