PROTEIN GLYCOSYLATION IN BACTERIAL CELLS AND ITS POTENTIAL APPLICATIONS

Bacterial glycoconjugates are widespread and have diverse biological functions. Multiple bacterial glycoproteins are involved in adhesion, invasion or evasion of host defense mechanisms. A range of glycosylation pathways has recently been an object of intense research. Their activity is based on the glycosyltransferases - enzymes that transfer sugar moieties directly to the acceptor protein (sequential glycosylation) or to a lipid carrier from which the glycan is transferred by an oligosaccharyltransferase onto the target protein (en-bloc glycosylation). Successful implementation of complete glycosylation systems in Escherichia coli cells resulted in rapid development of bacterial lycoengineering. Oligosaccharyltransferases are characterized by a broad substrate specificity which may be exploited to produce glycoconjugate vaccines.

Automated summary

Bacterial glycoconjugates play diverse biological roles, with glycosyltransferases being key enzymes for glycosylation. Oligosaccharyltransferases, with broad substrate specificity, can be utilized to produce glycoconjugate vaccines.