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Abstract
Gram-positive bacteria endow their peptidoglycan with glycopolymers that are crucial
for viability and pathogenesis. However, the cellular machinery that executes this
function is not well understood. While decades of genetic and phenotypic work have
highlighted the LytR-CpsA-Psr (LCP) family of enzymes as cell-wall glycopolymer transferases,
their in vitro characterization has been elusive, largely due to a paucity of tools
for functional assays. In this report, we synthesized authentic undecaprenyl diphosphate-linked
wall teichoic acid (WTA) intermediates and built an assay system capable of monitoring
LCP-mediated glycopolymer transfer. We report that all Bacillus subtilis LCP enzymes
anchor WTAs to peptidoglycan in vitro. Furthermore, we probed the catalytic requirements
and substrate preferences for these LCP enzymes and elaborated in vitro conditions
for facile tests of enzyme function. This work sheds light on the molecular features
of glycopolymer transfer and aims to aid drug discovery and development programs exploiting
this promising antibacterial target.