Immune and Inflammatory Diseases & Glycans

Immune Cell Targeting

ustom-synthesized glycans  or glycomimitics tailored to selectively bind immune receptors (e.g., Siglecs, galectins, C-type lectins) for precision modulation of immune responses. Selective targetings of lectins restricted to a defined immune cell subtype substantially enhances the specificity of therapeutic delivery to that cell population. For instance, targeted delivery using a langerin ligand analog substantially enhanced the specificity and efficiency of therapeutic delivery to Langerhans cells.

Vaccine development

design and synthesis of custom glycans that mimic bacteria-specific epitopes, enabling the creation of vaccines to elicit protective or therapeutic immune responses with increased immune response or stability to degradation. Additionally, specific glycan structures can be synthesized to selectively bind antibodies generated during bacterial infections, facilitating the identification of immunodominant epitopes for rational vaccine design.

Design and synthesis of glycan analytical standards for biomarker discovery in inflammatory and autoimmune diseases.

Asparia Glycomics developed patented CarboQuant ^13C-labeled glycan standards, which facilitated absolute quantification of N-glycans in serum proteins by mass spectrometry. Several autoimmune diseases like systemic lupus erythematosus (SLE) or rheumatoid arthritis present altered glycosylation markers that can be quantified employing the appropriate standards.

Glycan profiling

Asparia offers a broad glycan profiling service portfolio that may serve to indentify glycosylation pattern differences in immune or inflammatory diseases from healthy individuals. Some of these examples include:

Rheumatoid arthritis is associated with reduced galactosylation and sialylation of IgG antibodies, characterized by increased G0 glycoforms that lack galactose and terminate in N-acetylglucosamine.

• In inflammatory bowel disease, patients exhibit distinctive plasma N-glycome signatures characterized by increased abundance of large, complex glycans with reduced fucosylation and galactosylation, but enhanced sialylation.
• Multiple sclerosis patients show decreased IgG core fucosylation and increased high-mannose structures, while plasma proteins exhibit elevated antennary fucosylation, trisialylation, and tetrasialylation.

General Structural Analysis

General Structural Assignment Analysis, provides the precise identification of disease-associated glycans, enabling their use as diagnostic and prognostic biomarkers and as potential therapeutic targets in immune and inflammatory diseases. By characterizing aberrant glycosylation patterns, such as changes in antibody glycan profiles or cell-surface glycans, specificity and accuracy of disease detection and monitoring can be substantially improved—for example, identifying altered glycosylation on immunoglobulins or cell-surface proteins enhances disease screening and patient stratification.

• Elevated levels of certain monosaccharides, like fucose or sialic acid, are frequently associated with disease progression, immune cell activation, and mechanisms of immune evasion. This is the reason why the Monosaccharide Composition Analysis is key to studying the samples’ composition. 

Glycoproteomics

• mAbs’ efficacy and stability depend heavily on their precise molecular structure, and the Intact Mass Service helps to confirm the complete molecular weight, detect PTMs,  and identify protein variants or degradation products. Also, mass profiling of cytokines or immune receptors helps researchers study immune dysregulation in diseases such as autoimmune disorders or chronic inflammation. For example, Fc glycosylation of IgG antibodies directly impacts effector functions and anti-inflammatory activity. This information guides the design of therapeutic antibodies with optimized immune responses.
• N-glycosylation Site Occupation Analysis & Glycosylation Site-specific Glycan Profile  can identify partially glycosylated or abnormally glycosylated sites, uncovering changes in proteins related to disease progression. For example, variable domain glycosylation of immunoglobulins is related to autoimmunity and B-cell malignancies.

Microarray Technology

• Lectin Arrays are widely used in disease biomarker discovery to identify aberrant glycosylation patterns, biomarker discovery and patient stratification.

• Glycan Arrays enable the characterization of disease-specific glycan–immune interactions, facilitating the identification of biomarkers, identifying allergenic glycan structures, and guiding the development of targeted therapeutics or vaccines for immune and inflammatory diseases.