Abstract

Bacterial glycans are essential components of bacterial walls and crucially important cell surface antigens such as lipopolysaccharide and polysaccharide capsules, which act as virulence-causing factors. Polysaccharide capsules in bacteria are naturally composed of recurring oligosaccharides and lipopolysaccharides. LPS is composed of domains that are hydrophobic in nature known as lipid A or endotoxin, which is a nonrepeating oligosaccharide "core", and an O-antigen. Interaction of glycan-receptor is critical in pattern recognition of microorganisms and regulatory signals that perform regular immune cell activities. The true glycan structure is important for collaboration with the immune system of host, as demonstrated by microorganisms that produce polycarbohydrates that mimic host particles in order to evade the immunity of host. Certain bacteria circumvent antibody defences by molecularly mimicking the glycan structures of host and masquerade as "self" to avoid identification by immune system. Phages are the most prevalent biological entities on our planet, and they evolved glycan-binding proteins (GBPs) to bind to bacterial glycans. These proteins are in charge of the breakdown of antibodies and are impervious to harsh conditions where bacteria live for example, the gut of mammals, water, and soil. In order to increase contact with bacterial glycans, the phages manufacture multimeric proteins.

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