Infectious Diseases & Glycans

Glycan-Based Antigens for Vaccines

Asparia supports vaccine development with custom synthesis of glycopeptides and viral glycan shields for antiviral vaccines, and polysaccharide fragment libraries for antibacterial vaccines. We also provide conjugation to the carrier of your choice, enabling the design of authentic, effective glycan-based immunogens.

Mimicking Host Receptors for Pathogen Binding Studies:

Asparia provides custom synthesis of specific glycans, such as sialylated or high-mannose structures, to replicate host cell receptors. These glycans make it possible to study how viruses and bacteria recognize and attach to host cells, and how they interact with designed antibodies.

They help define detailed receptor–pathogen and pathogen–antibody binding interactions, supporting the development of entry inhibitors and vaccines. The compounds can also be applied in glycan arrays to test receptor binding specificities or used as reagents in biological assays.

Because individual glycan–protein interactions are weak, we also offer multivalent presentation formats that enhance binding strength. This enables more effective targeting strategies and the design of anti-adhesive approaches against pathogens

Generating Glycan Standards for Biomarker Discovery:

Asparia produces custom glycan standards with precisely defined structures, including isotope-labeled variants for quantitative analysis. These standards are essential for monitoring infection-related serum biomarkers, where subtle changes in glycosylation can reflect disease state or immune status.

A key example is the IgG glycan profile, which shifts during viral infections. Alterations in sialylation, galactosylation, or fucosylation can indicate pro-inflammatory or anti-inflammatory immune responses, making IgG glycans valuable readouts for patient monitoring. By providing robust reference standards, we enable accurate identification and quantification of these glycan signatures in complex biological samples.

This approach supports the discovery and validation of glycan-based biomarkers for infectious disease diagnostics, prognosis, and therapeutic monitoring.

Glycan profiling

Asparia provides a broad glycan profiling service portfolio aimed at the analysis of patient biofluids and tissues to support biomarker discovery. By monitoring disease-associated changes in glycosylation, we help identify signatures that can be used for diagnostics or therapeutic monitoring. Our services include N-glycan profiling, O-glycan profiling, and glycolipid analysis from samples such as serum proteins, IgG, and tissue extracts.

• LPS Extraction and Purification: Isolation of lipopolysaccharides from bacterial biomass using established chemical protocols (e.g., Westphal/Jahn). The crude extract is subjected to nuclease and protease treatments to remove nucleic acids and proteins, followed by multiple chromatographic separations. Product integrity and purity are confirmed by SDS-PAGE and carbohydrate-specific assays.
• Monosaccharide Composition: Quantitative and qualitative profiling of constituent sugars (GC-MS). The polysaccharide is hydrolyzed into monomers, reduced to alditols, derivatized to acetates, and analyzed by GC–MS. Fatty acid content is determined by hydrolysis and methylation, with selective release of ester-linked species under alkaline conditions.
• Absolute Configuration of Sugars: Assignment of D- or L- stereochemistry of each monosaccharide via chiral derivatization (e.g., 2-butanolysis). Resulting glycosides are acetylated and compared against authenticated standards using GC–MS.
• Glycosidic Linkage and Ring Size: Determination of inter-residue linkages through permethylation analysis. Hydrolyzed, reduced, and acetylated fragments are examined by GC–MS, and fragmentation patterns are used to identify glycosidic positions and ring forms.
• Anomeric Configuration: Nuclear Magnetic Resonance spectroscopy is employed to define α/β anomeric forms. Diagnostic 2D NMR experiments (e.g., 13C–1H HSQC with coupling analysis) provide insight into stereochemistry at the glycosidic centers.
• Identification of Non-Carbohydrate Moieties: Detection and characterization of lipid A, phosphate groups, acetylations, or other substituents using MALDI-TOF, ESI-MS, and complementary NMR spectra.
• Repeating Unit Structure: Comprehensive elucidation of the polysaccharide repeating unit. Sequential assignment of signals in 2D NMR spectra (COSY, TOCSY, HSQC, NOESY/ROESY, HMBC) combined with MS provides complete residue connectivity and substitution patterns.
• Molecular Size and Homogeneity: Determination of the absolute molecular weight and size distribution of polysaccharides or LPS by size-exclusion chromatography coupled to multi-angle light scattering. Provides information on aggregation, polydispersity, and sample uniformity.

Microarray Technology

• Lectin Arrays which employ panels of plant and animal lectins with defined glycan-binding specificities, are powerful tools for profiling global glycosylation changes in biological samples. In infectious disease research, they are mainly applied to detect host glycosylation alterations in biofluids, tissues, or immune proteins during infection, which can reveal disease-associated signatures and potential biomarkers. For bacterial infections, lectin arrays can highlight shifts in host glycan patterns linked to inflammation or altered immunoglobulin glycosylation. In viral infections, they are useful for monitoring changes in sialylation or fucosylation that accompany immune modulation or tissue remodeling. While lectin arrays do not directly define pathogen–host binding interactions (which require glycan arrays or pathogen-binding assays), they provide a rapid and comparative method to identify infection-driven glycosylation phenotypes that inform diagnostics, therapeutic monitoring, and vaccine evaluation

• Glycan Arrays provide an unparalleled platform to analyze host–pathogen interactions and immune recognition. By presenting defined glycans on a solid surface, they allow systematic exploration of how pathogen lectins bind to human glycans, and how host immune receptors such as DC-SIGN, Siglecs, TLRs, or antibodies recognize pathogen-derived structures. This is particularly valuable for understanding mechanisms of adhesion, immune evasion, and host defense. Glycan arrays are also critical for studying the specificity of antibody responses against bacterial polysaccharides, for example in evaluating glycoconjugate vaccines. Arrays composed of synthetic polysaccharide fragments enable detailed epitope mapping with high sensitivity and precision.

At Asparia, we offer a comprehensive glycan array of more than 150 N-glycan and O-glycan structures derived from mammalian, parasite, and plant origins, as well as custom fragment libraries of pure synthetic glycans. These platforms support in-depth characterization of immune responses, biomarker discovery, and vaccine development in infectious disease research.