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DC-SIGN对R1型核心脂寡糖的分子识别

Molecular recognition of R1-type core lipooligosaccharide by DC-SIGN.

作者信息

Nieto-Fabregat Ferran, Marseglia Angela, Thépaut Michel, Kleman Jean-Philippe, Abbas Massilia, Le Roy Aline, Ebel Christine, Maalej Meriem, Simorre Jean-Pierre, Laguri Cedric, Molinaro Antonio, Silipo Alba, Fieschi Franck, Marchetti Roberta

机构信息

Department of Chemical Science, University of Naples Federico II Via Cinthia 4, 80126 Naples, Italy.

University Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, France.

出版信息

iScience. 2024 Jan 4;27(2):108792. doi: 10.1016/j.isci.2024.108792. eCollection 2024 Feb 16.

DOI:10.1016/j.isci.2024.108792
PMID:38299112
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10828809/
Abstract

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 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.

摘要

由于凝集素能够识别碳水化合物结构，它们成为细菌脂多糖（LPS）的潜在受体。尽管人们对研究宿主受体凝集素与外源性聚糖配体之间的关联兴趣日增，但人类凝集素识别细菌的分子机制仍未完全明了。我们通过揭示[具体细菌名称]的脂寡糖与树突状细胞特异性细胞内粘附分子（ICAM）-3结合非整合素（DC-SIGN）之间相互作用的分子基础，为填补这一空白做出了贡献。具体而言，包括荧光显微镜、表面等离子体共振、核磁共振光谱和计算研究在内的多种技术相结合，证明DC-SIGN主要通过识别其外核五糖与纯化的脱酰化R1脂寡糖结合，该五糖充当DC-SIGN两个不同四聚体单元之间的交联剂。我们的结果有助于更好地理解DC-SIGN-LPS相互作用，并可能为细菌感染的药理学和免疫刺激策略的开发、预防及治疗提供支持。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/1ee231edb1b4/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/9a741c390ed9/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/908b54488a2a/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/3041e1762dac/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/4e26487605d2/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/da6c5fcf4d16/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/2bab96975ce0/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/5145aea44500/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/85deaeac8cf2/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/1ee231edb1b4/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/9a741c390ed9/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/908b54488a2a/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/3041e1762dac/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/4e26487605d2/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/da6c5fcf4d16/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/2bab96975ce0/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/5145aea44500/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/85deaeac8cf2/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e6/10828809/1ee231edb1b4/gr8.jpg

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