An assay for the bacterial sweet spot

Glycosylation is critical for the proper folding and function of many eukaryotic proteins. A lack of native asparagine-linked glycosylation machinery has hampered production of eukaryotic proteins in Escherichia coli. This commentary by Danielle Tullman-Ercek discusses the work of Matt Delisa's group on an assay using beta-lactamase activity as a reporter for successful glycoprotein folding in the periplasm of E. coli. See accompanying article by Mansell et al. DOI: 10.1002/biot.201300026 Glycosylation is critical for the proper folding and function of many eukaryotic proteins. A lack of native asparagine-linked glycosylation machinery has hampered production of eukaryotic proteins in Escherichia coli. This commentary by Danielle Tullman-Ercek discusses the work of Matt Delisa's group on an assay using beta-lactamase activity as a reporter for successful glycoprotein folding in the periplasm of E. coli.