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Abstract

The intracellular pathogen . Typhimurium is a leading cause of foodborne illness across the world and is known to rely on a range of virulence factors to colonize the human host and cause disease. The gene coding for one such factor, , was determined to be upregulated upon macrophage entry and its disruption reduces survival in the macrophage. In this study we characterize the STM3169 protein, which forms the substrate binding protein (SBP) of an uncharacterized tripartite ATP-independent periplasmic (TRAP) transporter. Genome context analysis of the genes encoding this system in related bacteria suggests a function in sugar acid transport. We demonstrate that purified STM3169 binds -glucuronic acid with high affinity and specificity. . Typhimurium LT2 can use this sugar acid as a sole carbon source and the genes for a probable catabolic pathway are present in the genome. As this gene was previously implicated in macrophage survival, it suggests a role for -glucuronate as an important carbon source for . Typhimurium in this environment.

Funding
This study was supported by the:
  • Biotechnology and Biological Sciences Research Council (Award BB/N01040X/1)
    • Principle Award Recipient: Reyme Herman
  • This is an open-access article distributed under the terms of the Creative Commons Attribution License. This article was made open access via a Publish and Read agreement between the Microbiology Society and the corresponding author’s institution.
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/content/journal/micro/10.1099/mic.0.000967
2020-09-07
2024-04-24
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