Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN

Bibliographic Details
Title: Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN
Authors: Ferran Nieto-Fabregat, Angela Marseglia, Michel Thépaut, Jean-Philippe Kleman, Massilia Abbas, Aline Le Roy, Christine Ebel, Meriem Maalej, Jean-Pierre Simorre, Cedric Laguri, Antonio Molinaro, Alba Silipo, Franck Fieschi, Roberta Marchetti
Source: iScience, Vol 27, Iss 2, Pp 108792- (2024)
Publisher Information: Elsevier, 2024.
Publication Year: 2024
Collection: LCC:Science
Subject Terms: Microbiology, Structural biology, Science
More Details: Summary: Due to their ability to recognize carbohydrate structures, lectins emerged as potential receptors for bacterial lipopolysaccharides (LPS). Despite growing interest in investigating the association between host receptor lectins and exogenous glycan ligands, the molecular mechanisms underlying bacterial recognition by human lectins are still not fully understood. We contributed to fill this gap by unveiling the molecular basis of the interaction between the lipooligosaccharide of Escherichia coli and the dendritic cell-specific intracellular adhesion molecules (ICAM)-3 grabbing non-integrin (DC-SIGN). Specifically, a combination of different techniques, including fluorescence microscopy, surface plasmon resonance, NMR spectroscopy, and computational studies, demonstrated that DC-SIGN binds to the purified deacylated R1 lipooligosaccharide mainly through the recognition of its outer core pentasaccharide, which acts as a crosslinker between two different tetrameric units of DC-SIGN. Our results contribute to a better understanding of DC-SIGN-LPS interaction and may support the development of pharmacological and immunostimulatory strategies for bacterial infections, prevention, and therapy.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2589-0042
Relation: http://www.sciencedirect.com/science/article/pii/S2589004224000130; https://doaj.org/toc/2589-0042
DOI: 10.1016/j.isci.2024.108792
Access URL: https://doaj.org/article/b0db4208477b44db88da22e26245f019
Accession Number: edsdoj.b0db4208477b44db88da22e26245f019
Database: Directory of Open Access Journals
More Details
ISSN:25890042
DOI:10.1016/j.isci.2024.108792
Published in:iScience
Language:English