All cells and numerous macromolecules in nature, both microbial and human, are covered with a dense and complex array of complex carbohydrates, known individually as glycans and collectively as the glycocalyx. These glycans are based on either single sugars, monosaccharides (e.g. pentoses, hexoses, hexosamines, deoxyhexoses, uronic acids and sialic acids), two or more conjugated sugars, oligosaccharides, or in a polymeric structure called a polysaccharide. Normally glycans are conjugated to other biomolecules. Conjugated glycans are categorized as glycoproteins, proteoglycans and glycolipids. The high variety of linkages between these glycans monomers leads to almost infinite glycan structures and illustrates how a relatively small number of genes in the typical genome can generate enormous biological complexities. Thus, it is not surprising temporal and spatial patterns of glycan expression exist across a wide array of biological processes, including cell communication, host protection, transcription, differentiation, activation, apoptosis and structure. Glycans perform these functions by interacting with many types of proteins, as exemplified by their binding to enzymes, antibodies, and glycan-binding proteins (GBPs). Binding of glycans to proteins and antibodies represents the predominant way information contained in glycan structures is recognized, deciphered, and put into biological action. In addition, since glycans are a major component of all cell surfaces they are most likely the first component recognized by the host immune system.
It is believed glycans, compared to other macromolecules, such as nucleic acids (DNA/RNA), Proteins, Lipids have the most overlap between microbial species and humans. Bacteria produce a variety of glycoconjugates and polysaccharides of enormous structural diversity and complexity including peptidoglycans, periplasmic glucans, lipopolysaccharides (LPS), and extracellular polysaccharides that make up capsules and biofilms. These glycans play important roles in the biology, and sometimes result in the pathogenicity, of bacterial cells. As an example, capsular polysaccharides and LPS containing the major antigenic determinants distinguish various serotypes of bacteria, eliciting strong immune responses in animals. Also, the cell wall of most fungi is composed of glycoproteins embedded within a polysaccharide matrix or scaffolding. The glycoproteins typically have elongated filaments or hyphae, which are comprised of complex polysaccharides including mannans, galactans, glucans, and chitin. Glycans, as polysaccharides or components of glycoproteins, play a major role in the pathogenesis and diagnosis of many disease causing fungal species.
Human cells are covered with a dense and complex array of glycans called the glycocalyx, which comprises of various forms of glycoconjugates (glycoproteins, glycolipids, and proteoglycans). It is believed different cell types express distinct sets of glycans, and glycosylation of a single cell type significantly changes during cell development and differentiation. Research has shown abnormal glycosylations may be the cause of many diseases. This overlap creates one of most important day to day differences among people, the ABO blood type. Blood types are based on the different glycosylation patterns off red blood cells and the anti-glycan antibodies that recognized the glycosylation differences. These differences likely result from microbial exposure.
Glycominds’ technology platform assesses the immune response by measuring the level of antibody biomarkers against glycans. Many chronic diseases show changes in anti-glycan antibodies. Glycominds focuses on autoimmune diseases and inflammation, where levels of antibody follows the changes in the innate immunity. Glycominds is the first group to focus on understanding how changes in glycan patterns affect the immune system, disease outcome and response to treatment. This novel approach enables Glycominds to identify relevant disease pathophysiology and mechanisms of action as they relate to glycans and levels of anti-glycan antibodies.