Salmonella typhimurium enzymatically landscapes the host intestinal epithelial cell (IEC) surface glycome to increase invasion

Dayoung Park, Narine Arabyan, Cynthia C. Williams, Ting Song, Anupam Mitra, Bart C Weimer, Emanual Michael Maverakis, Carlito B Lebrilla

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Although gut host-pathogen interactions are glycan-mediated processes, few details are known about the participating structures. Here we employ high-resolution mass spectrometric profiling to comprehensively identify and quantitatively measure the exact modifications of native intestinal epithelial cell surface N-glycans induced by S. typhimurium infection. Sixty minutes postinfection, select sialylated structures showed decreases in terms of total number and abundances. To assess the effect of cell surface mannosylation, we selectively rerouted glycan expression on the host using the alpha-mannosidase inhibitor, kifunensine, toward overexpression of high mannose. Under these conditions, internalization of S. typhimurium significantly increased, demonstrating that bacteria show preference for particular structures. Finally, we developed a novel assay to measure membrane glycoprotein turnover rates, which revealed that glycan modifications occur by bacterial enzyme activity rather than by hostderived restructuring strategies. This study is the first to provide precise structural information on how host N-glycans are altered to support S. typhimurium invasion.

Original languageEnglish (US)
Pages (from-to)3653-3664
Number of pages12
JournalMolecular and Cellular Proteomics
Volume15
Issue number12
DOIs
StatePublished - Dec 1 2016

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Molecular Biology

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