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TRIM14 is a key regulator of the type I interferon response during Mycobacterium tuberculosis infection

biorxiv. 2020; 
Caitlyn T. Hoffpauir, Samantha L. Bell, Kelsi O. West, Tao Jing, Sylvia Torres-Odio, Jeffery S. Cox, A. Phillip West, Pingwei Li, Kristin L. Patrick, Robert O. Watson
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Catalog Antibody Membranes were then incubated in secondary antibody for 1 hour and imaged using LI-COR Odyssey FC Imaging System. Primary antibodies used in this study: mouse monoclonal α-FLAG M2 antibody (Sigma-Aldrich, F3165), α-HA high affinity rat monoclonal antibody (Roche; 3F10), α-strep (Genscript A00626), α-phospho-Stat3 (Ser727) (Cell Signaling #9134), α-phospho-Stat3 (Ser754) (Cell Signaling #98543), α-Stat3 (124H6) Mouse mAb (Cell Signaling #9139), α-phospho-Stat1 (Tyr701) (58D6) Rabbit mAb #9167, α-TRIM14 G-15 (Santa Cruz sc79761), α-TRIM14 (Aviva ARP34737), and α-mouse monoclonal Beta-Actin (Abcam, #6276). Secondary antibodies used in this study: IR Dye CW 680 goat anti-rabbit, IR Dye CW 680 goat anti-rat 680, IR Dye CW800 goat anti-mouse (LI-COR), Alexfluor-488 anti-rabbit, Alexfluor-597 anti-rat, and Alexafluo-647 anti-mouse secondary antibodies for immunofluorescence (LI-COR). Get A Quote

摘要

Tripartite motif-containing proteins (TRIMs) play a variety of recently described roles in innate immunity. While many TRIMs regulate type I interferon (IFN) expression following cytosolic nucleic acid sensing of viruses, their contribution to innate immune signaling and gene expression during bacterial infection remains largely unknown. Because Mycobacterium tuberculosis is a potent activator of cGAS-dependent cytosolic DNA sensing, we set out to investigate a role for TRIM proteins in regulating macrophage responses to M. tuberculosis. Here we demonstrate that TRIM14, a non-canonical TRIM that lacks an E3 ligase RING domain, is a critical negative regulator of the type I IFN response in macrophages. We sho... More

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