scholarly journals Lipopolysaccharide-induced neutrophil extracellular trap formation in canine neutrophils is dependent on histone H3 citrullination by peptidylarginine deiminase

2017 ◽  
Vol 193-194 ◽  
pp. 29-37 ◽  
Author(s):  
Ronald H.L. Li ◽  
Geena Ng ◽  
Fern Tablin
2018 ◽  
Vol 201 (4) ◽  
pp. 1241-1252 ◽  
Author(s):  
Theodora A. M. Claushuis ◽  
Lieve E. H. van der Donk ◽  
Anna L. Luitse ◽  
Henk A. van Veen ◽  
Nicole N. van der Wel ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Qian Ou ◽  
Jia-qi Fang ◽  
Zhe-sheng Zhang ◽  
Zhe Chi ◽  
Jie Fang ◽  
...  

AbstractTcpC is a multifunctional virulence factor of uropathogenic E. coli (UPEC). Neutrophil extracellular trap formation (NETosis) is a crucial anti-infection mechanism of neutrophils. Here we show the influence of TcpC on NETosis and related mechanisms. We show NETosis in the context of a pyelonephritis mouse model induced by TcpC-secreting wild-type E. coli CFT073 (CFT073wt) and LPS-induced in vitro NETosis with CFT073wt or recombinant TcpC (rTcpC)-treated neutrophils are inhibited. rTcpC enters neutrophils through caveolin-mediated endocytosis and inhibits LPS-induced production of ROS, proinflammatory cytokines and protein but not mRNA levels of peptidylarginine deiminase 4 (PAD4). rTcpC treatment enhances PAD4 ubiquitination and accumulation in proteasomes. Moreover, in vitro ubiquitination kit analyses show that TcpC is a PAD4-targetd E3 ubiquitin-ligase. These data suggest that TcpC inhibits NETosis primarily by serving as an E3 ligase that promotes degradation of PAD4. Our findings provide a novel mechanism underlying TcpC-mediated innate immune evasion.


2019 ◽  
Vol 186 (2) ◽  
pp. 311-320 ◽  
Author(s):  
Ella Grilz ◽  
Lisa‐Marie Mauracher ◽  
Florian Posch ◽  
Oliver Königsbrügge ◽  
Sabine Zöchbauer‐Müller ◽  
...  

2016 ◽  
Vol 7 ◽  
Author(s):  
Yoshihiro Kusunoki ◽  
Daigo Nakazawa ◽  
Haruki Shida ◽  
Fumihiko Hattanda ◽  
Arina Miyoshi ◽  
...  

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