Engineered Escherichia coli produce self-assembling glycoprotein nanoparticles
Researchers led by Tim Keys in the Aebi group (IMB) teamed up with the Hilvert lab (D-CHAB) to produce a variety of glycosylated proteinaceous nanoparticles. The paper in Nature Communications shows how installing protein glycosylation machinery in the bacterial cytoplasm provides biosynthetic access to diverse glycoprotein structures
Combining protein glycosylation with advanced protein engineering platforms hold transformative potential for the development of next generation vaccines and therapeutics. Towards this goal, we have developed a simple glycoengineering platform that operates in the cytoplasm of E. coli. The platform leverages a glycosyltransferase that modifies specific asparagine residues of a protein with a glucose monosaccharide. This glucose provides a site-specific handle on the recombinant protein for biosynthesis of oligo- or polysaccharide structures. We demonstrate the versatility of the platform by modifying proteins with sugars of bacterial and mammalian origin and by producing a variety of self-assembling glycoprotein nanoparticles, including programmable protein cages, evolvable nucleocapsids, and virus-like particles.
Link to the publication in external pageNature Communications