An assay for the bacterial sweet spot

Danielle Tullman-Ercek*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1377-1378
Number of pages2
JournalBiotechnology Journal
Volume8
Issue number12
DOIs
StatePublished - Dec 1 2013

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Molecular Medicine

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