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. 2020 Jun 17;11:1191. doi: 10.3389/fmicb.2020.01191

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Copyright © 2020 Duma, Nothaft, Weaver, Fodor, Beadle, Linton, Benoit, Scott, Maier and Szymanski.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Functional analysis of Cff-Pgl pathway glycosyltransferases (GTases) in the heterologous E. coli glycosylation system. The GTase-activities of (A) PglA and PglJ were analyzed in western blots of Cj-CmeA-His₆ with His₆-tag antibodies (upper panel) and Cj-N-glycan specific (R1) antibodies (lower panel). (B) PglX and PglY activities were analyzed with His₆-tag specific antibodies in western blots of CmeA-His₆ used as the glycan acceptor to determine N-glycosylation activities. Whole cell extracts (5 μg) of E. coli CLM24 expressing the indicated gene/plasmid combinations are indicated above each lane. Non-, mono-, and di-glycosylated CmeA-His₆ proteins are labeled as 0N, 1N, and 2N, respectively. Molecular weight markers (MW) in kDa are indicated on the left.