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
  • 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].
PMID: 30617292 DOI: 10.1038/s41589-018-0189-y
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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