Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology.

ABSTRACT:

Background

Bacterial surface glycans are assembled by glycosyltransferases (GTs) that transfer sugar monomers to long-chained lipid carriers. Most bacteria employ the 55-carbon chain undecaprenyl phosphate (Und-P) to scaffold glycan assembly. The amount of Und-P available for glycan synthesis is thought to be limited by the rate of Und-P synthesis and by competition for Und-P between phosphoglycosyl transferases (PGTs) and GTs that prime glycan assembly (which we collectively refer to as PGT/GTs). While decreasing Und-P availability disrupts glycan synthesis and promotes cell death, less is known about the effects of increased Und-P availability.

Results

To determine if cells can maintain higher Und-P levels, we first reduced intracellular competition for Und-P by deleting a

SUBMITTER: Kay EJ 

PROVIDER: S-EPMC10908060 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature