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What Is Glycobiology?

Glycobiology is the interdisciplinary study of the structure, biosynthesis, and biological functions of glycans (a generic term to describe the assembly of sugars in a biological context). Glycans belong to one of the four fundamental classes of macromolecules essential for life, alongside nucleic acids, proteins, and lipids. Every living cell is coated in a dense, complex layer of these glycans, known as the glycocalyx, which acts as the front line for structural protection, cell-cell communication, molecular recognition, and immunity. Unlike DNA and proteins, which follow linear genetic templates, glycan synthesis is a non-template-driven process involving a complex network of enzymes, such as glycosyltransferases, which link sugar units in both linear and branched patterns. This structural flexibility allows glycans to carry an information content that is vastly different from that of any other class of macromolecules, and thus, resulting in a complexity that imposes huge challenges for their research.

The physiological significance of glycobiology is exemplified in its known clinical applications. In diagnostics, specific glycan structures have been known as vital biomarkers, such as PSA, CA125, and CA19-9, for cancer detection. Many rare genetic diseases have root causes in the genetic defects related to glycan metabolic pathways, which are jointly known as congenital disorders of glycosylation (CDGs). In therapeutics, a monoclonal antibody (mAb) targeting GD2, a glycolipid, is an FDA-approved therapy for children with high-risk neuroblastoma. In infectious diseases, the influenza neuraminidase inhibitors prevent viral infection by blocking the de-sialylation of host cell glycocalyx, and highly effective glycoconjugate vaccines against pathogens like Streptococcus pneumoniae have shown great clinical benefit. One can envision further expansive clinical applications of glycobiology as we continue deepening our understanding into the different roles of glycans in biology.

Despite this potential, the application of glycobiology faces immense challenges, primarily the astonishing structural complexity of glycans, which stems from their non-linear and non-template-dependent biosynthetic pathways. This complexity is compounded by a lack of high-throughout tools for sequencing, amplification, or synthesis comparable to those used in genomics and proteomics, making detailed analysis time-consuming and technically demanding. Furthermore, glycans and their bioconjugates naturally exist as heterogeneous mixtures of glycoforms, where multiple different glycan structures are attached to the same protein/lipid/nucleic acid backbone, complicating the isolation of pure, functionally consistent materials. These overall challenges have greatly hindered the access of glycobiology by the scientific mainstream.

Lectins, Nature’s Glyco-Code Reader

The complexity of glycans imposes a vast analytical challenge for studying the structural function relationship and biological roles of glycans, and hence the under-development of clinical applications. At Glycogenetics, we address this challenge by focusing on developing reagents based on Nature’s glyco-code readers: lectins. Human lectins, our primary focus, recognize human glycan structures and are essential for translating glycan-encoded signals into biological responses, such as cell signaling, immune regulation, and extracellular structures, which are pivotal for maintaining human health. Our goal is to recombinantly express the >200 predicted human lectin genes in the human genome, and thus to give researchers high-quality, reliable reagents to probe the signaling pathways mediated by native lectin-ligand interactions. We also pursue the research on human lectins internally and through collaborations to expand their uses. We believe that our lectins and related glycan-detecting tools will accelerate the identification of novel biomarkers and mechanisms behind diseases for new drug development.

As users of lectins ourselves, we understand that the fundamental need of lectins resides in their practical uses. As many lectins have not been previously characterized, we not only strive to produce lectins with the highest quality standard, but we also provide the basic use case of our lectins to guide our users how to apply these lectins. Since lectins bind to glycan ligands, we routinely test their use as affinity reagents for common biochemical assays, such as blotting, flow cytometry, and immunostaining. Beyond these general biochemical binding assays, there are special uses of lectins that are more related to the biological functions of individual lectins that could lead to special applications. We have dedicated research and development efforts toward exploring these biological activities of our lectins products to help our customers choosing the right lectins for their research.

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