CarboMet proposal successful!

CarboMet is a Coordination and Support action within the FET-OPEN Horizon 2020 funding schemeand coordinated by the University of Manchester (Prof. Sabine Flitsch) in which Asparia Glycomics a spin-off from our group is participating alongside a number of other stakeholders from industry and academia active in glycoscience research. CarboMet will foster and drive collaboration, cross-fertilisation and communication among stakeholders to facilitate a uniform approach to the metrology and/or measurement of carbohydrates for exploitation in biopharmaceuticals, diagnosis of disease and precision medicine, food and personal care and sustainable material BioIndustries. This will be achieved through a consolidated approach towards the modification of key emerging technologies or identification of radically new technologies currently unforeseen by technology roadmaps.
Carbohydrates and glycoconjugates are especially challenging to analyse due to their high stereochemical diversity which means it is difficult to distinguish between them and fully characterise using standard techniques and methods. Current methodologies to fully solve 3-D structures include NMR and X-Ray Crystallography which are low-throughput, require large samples and have poor sensitivity. Emerging technologies are beginning to address these issues such as Ion Mobility Mass Spectrometry (IM-MS) and the combination of 3 gas phase techniques: IR spectroscopy with IM-MS in-vitro enabling high-throughput with higher sensitivity, small samples, and analysis from mixtures to provide structural detail on each component. These technologies are underpinned by advanced supporting technologies such as automated carbohydrate synthesis, bioinformatics tools and databases, and new suites of enzymes for glycan synthesis and modification. CarboMet will use a range of communication and dissemination tools (meetings, workshops, website, surveys, briefing papers) to engage key stakeholders, to establish the current emerging technologies, limitations, and barriers to implementation. Priority areas, future challenges and a wish list of capabilities will then be defined, culminating in the production of a roadmap for 2030, setting out a Europe-wide vision. These capabilities will lead to new robust metrologies for the exploitation of carbohydrates.

New paper published comparing novel fluoroacetamide NMR tags

toc-chemistry-2016Together with the groups of Jesus Jimenez-Barbero, CIC bioGUNE, Bilbao, Antonio Franconetti, University of Seville, and Javier Cañada, CIB-CSIC, Madrid we have just published a study in the journal Chemistry, A European Journal titled Fluoroacetamide Moieties as NMR Probes for molecular recognition of GlcNAc-containing sugars: Modulation of the CH-π Stacking Interactions by Different Fluorination Patterns. In the paper we propose the use of the fluoroacetamide and difluoroacetamide moieties as sensitive tags for detecting sugar-protein interactions by simple 1H and/or 19F NMR methods. As selected process, we have chosen the binding of N,N’-diacetyl chitobiose, a ubiquitous disaccharide fragment in glycoproteins, by wheat germ agglutinin (WGA), a model lectin. Using STD-NMR, we experimentally demonstrate that, under solution conditions, the molecule containing the CHF2-CO-NH- moiety is the stronger aromatic binder, followed by the analogue with the CH2F-CO-NH- group and the natural molecule (with the CH3-CO-NH- fragment). In contrast, the molecule with the CF3-CO-NH- isoster displays the weakest intermolecular interaction (one order of magnitude weaker). Since sugar-aromatic CH-π interactions are at the origin of these observations, these results further contribute to the characterization and exploration of these forces and offer an opportunity to use them to unravel complex recognition processes.

Spin-off company Asparia Glycomics founded to commercialize our glycan analysis technology


CIC biomaGUNE and private investors have come together to set up Asparia Glycomics, a company specialized in the production and marketing of reagents, reference standards, kits and software for glycan analysis in clinical diagnosis and for quality control of biopharmaceuticals.

The new company is commercializing state of the art technology developed in our laboratory during the last 5 years to quantify protein glycosylation with higher precision and higher throughput than existing solutions. Asparia Glycomics is offering unique stable isotope labeled glycans as internal standards, custom made quantification software and reagents for glycan analysis by mass spectrometry.

The company is led by Dr. Juan Echevarria, a co-developer of the technology, who moved to Asparia Glycmics from the glycotechnology laboratory. The standards and kit solutions offered by Asparia Glycomics find multiple applications in clinical glycomics research, biopharmaceutical glycan analysis and glycobiology in general. For more information visit

Paper on the use of glycans for dendritic cell targeting accepted in ACS Chemical Biology

TOC ACS Chem Bio 2016After a first publication of the synthesis and microarray binding analysis of xylosylated N-glycans we have just published a second paper in ACS Chemical Biology describing the effect of core xylosylation on carbohydrate based dendritic cell targeting.

Abstract: Targeting antigens to dendritic cell subsets is a promising strategy to enhance the efficacy of vaccines. C-type lectin receptors (CLRs) expressed by dendritic cells are particularly attractive candidates since CLR engagement may promote cell uptake and may further stimulate antigen presentation and subsequent T cell activation. While most previous approaches have involved antibody-mediated CLR-targeting, glycan-based CLR targeting has become more and more attractive in recent years. In the present study, we show that small structural glycan modifications may markedly influence CLR recognition, dendritic cell targeting, and subsequent T cell activation. A biantennary N-glycan (G0) and its analogous O-2 core xylosylated N-glycan (XG0) were synthesized, covalently conjugated to the model antigen ovalbumin, and analyzed for binding to a set of murine CLR-Fc fusion proteins using lectin microarray. To evaluate whether the differential binding of G0 and XG0 to CLRs impacted dendritic cell targeting, uptake studies using murine dendritic cells were performed. Finally, effects of the ovalbumin glycoconjugates on T cell activation were measured in a dendritic cell/T cell cocultivation assay. Our results highlight the utility of glycan-based dendritic cell targeting and demonstrate that small structural differences may have a major impact on dendritic cell targeting efficacy.