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Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactosespecific lectins

AuthorsKalograiaki, Ioanna; Euba, Begoña ; Fernández-Alonso, M. Carmen ; Proverbio, Davide; St. Geme, Joseph W.; Aastrup, Teodor; Garmendia, Juncal ; Cañada, F. Javier ; Solís, Dolores
KeywordsLigand-binding characteristics
Ricinus-communis agglutinin
AB-type lectin
Carbohydrate interactions
Protein glycosylation
Issue Date2-Nov-2018
PublisherSpringer Nature
CitationScientific Reports 8:16292 (2018)
AbstractBacterial surfaces are decorated with carbohydrate structures that may serve as ligands for host receptors. Based on their ability to recognize specific sugar epitopes, plant lectins are extensively used for bacteria typing. We previously observed that the galactose-specific agglutinins from Ricinus communis (RCA) and Viscum album (VAA) exhibited differential binding to nontypeable Haemophilus influenzae (NTHi) clinical isolates, their binding being distinctly affected by truncation of the lipooligosaccharide (LOS). Here, we examined their binding to the structurally similar LOS molecules isolated from strains NTHi375 and RdKW20, using microarray binding assays, saturation transfer difference NMR, and molecular dynamics simulations. RCA bound the LOSRdKW20 glycoform displaying terminal Gal beta(1,4) Glc beta, whereas VAA recognized the Gala(1,4) Gal beta(1,4) Glc beta epitope in LOSNTHi375 but not in LOSRdKW20, unveiling a different presentation. Binding assays to whole bacterial cells were consistent with LOSNTHi375 serving as ligand for VAA, and also suggested recognition of the glycoprotein HMW1. Regarding RCA, comparable binding to NTHi375 and RdKW20 cells was observed. Interestingly, an increase in LOSNTHi375 abundance or expression of HMW1 in RdKW20 impaired RCA binding. Overall, the results revealed that, besides the LOS, other carbohydrate structures on the bacterial surface serve as lectin ligands, and highlighted the impact of the specific display of cell surface components on lectin binding.
Description12 p.-4 fig.-4 tab.
Publisher version (URL)https://doi.org/10.1038/s41598-018-34383-x
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