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Shigella hijacks host ISGylation pathway by arginine ADP-riboxanation of HERC5
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  • Xiaoyun Liu,
  • Jie Jin,
  • Xianbin Meng,
  • Yi Yuan,
  • Yi Huo,
  • Jia Song,
  • Xuliang Deng,
  • Haiteng Deng
Xiaoyun Liu
Peking University School of Basic Medical Sciences

Corresponding Author:[email protected]

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Jie Jin
Peking University School of Basic Medical Sciences
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Xianbin Meng
Tsinghua University School of Life Sciences
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Yi Yuan
Peking University School of Basic Medical Sciences
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Yi Huo
BeiGene (Beijing) Co Ltd
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Jia Song
Peking University School of Stomatology Department of General Dentistry
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Xuliang Deng
Peking University School of Stomatology Department of General Dentistry
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Haiteng Deng
Tsinghua University School of Life Sciences
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Abstract

Shigella flexneri type III effector OspC3 was recently found to evade host pyroptosis by targeting caspase-11 for ADP-riboxanation. The ADP-riboxanase activity was shared by its paralogues, OspC1 and OspC2, whereas the host substrates of them are still unknown. To solve this problem, we employed eAf1521 enrichment coupled with mass spectrometry (MS)-based proteomics to profile the host substrates of OspC1. In this study, we identified HERC5 as a host target of OspC1. As described previously, HERC5 functions as an E3 ISG15 ligase and catalyzes the ISGylation of a huge subset of host and pathogen proteins upon bacterial infection. Here, we show that S. flexneri hijacks host ISGylation pathway by OspC1-catalyzed ADP-riboxanation of HERC5 to promote its own survival and proliferation in host cells.
20 Jun 2023Submitted to Molecular Microbiology
20 Jun 2023Submission Checks Completed
20 Jun 2023Assigned to Editor
21 Jun 2023Reviewer(s) Assigned
23 Jun 2023Review(s) Completed, Editorial Evaluation Pending