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ADP-riboxanation: a new pyroptosis evasion strategy
Heyu Li1,2 , Fangfang Zhou3,* , Long Zhang1,*
1MOE Laboratory of Biosystems Homeostasis and Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute, Zhejiang University, Hangzhou 310058, China
2School of Medicine, Zhejiang University City College, Hangzhou 310015, China
3Institutes of Biology and Medical Science, Soochow University, Suzhou 215123, China
*Correspondence to:Fangfang Zhou , Email:zhoufangfang@suda.edu.cn Long Zhang , Email:l_zhang@zju.edu.cn
J Mol Cell Biol, Volume 14, Issue 1, January 2022, mjab077,  https://doi.org/10.1093/jmcb/mjab077

A recent study published in Nature by Li et al. (2021) revealed the underlying mechanism by which Shigella flexneri evades host pyroptosis using a type III secretion system (T3SS) effector, OspC3. OspC3 suppresses the proteolytic activity of caspase-11 or caspase-4 (hereafter referred to as ‘caspase-11/4’) in a nicotinamide adenine dinucleotide (NAD+)-dependent manner by catalyzing adenosine diphosphate riboxanation (ADP-riboxanation) on arginine 314 (Arg314) and Arg310 in caspase-4 and caspase-11, respectively (Figure 1). In addition, <em style="box-sizing: border-box; margin: 0px; padding: 0px; border: 0px; font-variant-numeric: inherit; font-stretch: inherit; font-size: 15px; line-height: inherit; font-family: Merriweather, serif; vertical-align: baseline; color: rgb(42, 42, 42); white-space: normal; ba


Volume 14, Issue 1
January 2022