1. Academic Validation
  2. Legionella effector SetA as a general O-glucosyltransferase for eukaryotic proteins

Legionella effector SetA as a general O-glucosyltransferase for eukaryotic proteins

  • Nat Chem Biol. 2019 Mar;15(3):213-216. doi: 10.1038/s41589-018-0189-y.
Ling Gao 1 2 Qitao Song 1 2 Hao Liang 1 2 Yuntao Zhu 1 3 Tiantian Wei 2 4 Na Dong 5 6 Junyu Xiao 2 4 Feng Shao 6 Luhua Lai 1 2 3 7 Xing Chen 8 9 10 11 12
Affiliations

Affiliations

  • 1 College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
  • 2 Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.
  • 3 Beijing National Laboratory for Molecular Sciences, Peking University, Beijing, China.
  • 4 School of Life Sciences, Peking University, Beijing, China.
  • 5 State Key Lab of Animal Nutrition, Ministry of Agriculture Feed Industry Center, China Agricultural University, Beijing, China.
  • 6 National Institute of Biological Sciences, Beijing, China.
  • 7 Center for Quantitative Biology, Peking University, Beijing, China.
  • 8 College of Chemistry and Molecular Engineering, Peking University, Beijing, China. [email protected].
  • 9 Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China. [email protected].
  • 10 Beijing National Laboratory for Molecular Sciences, Peking University, Beijing, China. [email protected].
  • 11 Synthetic and Functional Biomolecules Center, Peking University, Beijing, China. [email protected].
  • 12 Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University, Beijing, China. [email protected].
Abstract

The identification of host protein substrates is key to understanding effector glycosyltransferases secreted by pathogenic bacteria and to using them for glycoprotein engineering. Here we report a chemical method for tagging, enrichment, and site-specific proteomic profiling of effector-modified proteins in host cells. Using this method, we discover that Legionella effector SetA α-O-glucosylates various eukaryotic proteins by recognizing a S/T-X-L-P/G sequence motif, which can be exploited to site-specifically introduce O-glucose on recombinant proteins.

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