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Probing DC-SIGN-glycan multivalent interaction and dendritic cell immune regulation using polyvalent multifunctional glycan-gold nanoparticles

Project description

Structural insight into dendritic cell antigen recognition

Dendritic cells (DCs) express on their surface the receptor DC-SIGN, which binds and discriminates self and pathogen polysaccharide (glycan) patterns, thereby driving immune responses. The scope of the EU-funded Glycan-PMN project is to shed light on the structural determinants of this binding as well as the underlying immune regulation mechanism. Scientists will use nanoparticles functionalised with different glycans on their surface to determine the optimal structure for DC-SIGN binding. With the help of in vitro infection models, they will also evaluate the potential of targeting DC-SIGN with specific glycans to block infection or develop effective immunotherapies.

Objective

Multivalent lectin-glycan interactions is central to pathogen infection and immune response regulation. Dendritic cell (DC) surface tetrameric lectin, DC-SIGN, is particularly important in discriminating self- and foreign (pathogen) glycan patterns and regulates DC immune response. The underlying structural and immune regulation mechanisms remain poorly understood. As various lectins have overlapping glycan specificity, this greatly limits our ability to design glycoconjugates that can specifically target DC-SIGN to block infection or exploit its powerful immune regulation to develop effective immunotherapies.

Here we will address this challenge by developing polyvalent glycan-gold nanoparticles (GNPs) & multiple GNP assemblies to enhance binding affinity and specificity by exploiting multivalency. By tuning GNP surface glycan structure, valency, inter-glycan spacing, size and shape and study their binding with DC-SIGN/R, we will reveal the optimal glycan structure for DC-SIGN binding. By exploiting GNP’s fluorescence quenching, we will develop a new lectin-glycan affinity quantifying method. We will use glycan-GNPs to block pseudo-Ebola virus infection of DC-SIGN expressing cells and correlate the affinity and inhibition potency. We will study how glycan-GNP binding controls DC surface DC-SIGN clustering, binding to intracellular proteins & regulating cytokine production to reveal the .

This research is extremely timely & important because it will, 1) establish a design rule for potent, highly specific DC-SIGN targeting; 2) develop a new lectin-glycan affinity quantification method; 3) reveal correlation between DC-SIGN/R binding affinity & viral inhibition potency; 4) elucidate how DC-SIGN-glycan binding signal is transduced to regulate DC immune function, paving way to develop effective immunotherapies against deadly immune-dysregulation diseases (e.g. cancer, allergy, & auto-immune diseases) by exploiting DC-SIGN’s powerful immune regulation function.

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MSCA-IF - Marie Skłodowska-Curie Individual Fellowships (IF)

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Call for proposal

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(opens in new window) H2020-MSCA-IF-2019

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Coordinator

UNIVERSITY OF LEEDS
Net EU contribution

Net EU financial contribution. The sum of money that the participant receives, deducted by the EU contribution to its linked third party. It considers the distribution of the EU financial contribution between direct beneficiaries of the project and other types of participants, like third-party participants.

€ 224 933,76
Address
WOODHOUSE LANE
LS2 9JT Leeds
United Kingdom

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Region
Yorkshire and the Humber West Yorkshire Leeds
Activity type
Higher or Secondary Education Establishments
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Total cost

The total costs incurred by this organisation to participate in the project, including direct and indirect costs. This amount is a subset of the overall project budget.

€ 224 933,76
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