High level in vivo mucin-type glycosylation in Escherichia coli.

ABSTRACT:

Background

Increasing efforts have been made to assess the potential of Escherichia coli strains for the production of complex recombinant proteins. Since a considerable part of therapeutic proteins are glycoproteins, the lack of the post-translational attachment of sugar moieties in standard E. coli expression strains represents a major caveat, thus limiting the use of E. coli based cell factories. The establishment of an E. coli expression system capable of protein glycosylation could potentially facilitate the production of therapeutics with a putative concomitant reduction of production costs.

Results

The previously established E. coli strain expressing the soluble form of the functional human-derived glycosyltransferase polypeptide N-acetylgalactosaminyltransferase 2 (G

SUBMITTER: Mueller P 

PROVIDER: S-EPMC6202839 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature