The utilization of intermittent renewable energy sources needs low-cost, reliable energy storage systems in the future. Among various electrochemical energy storage systems, redox flow batteries (RFBs) are promising with merits of independent energy storage and power generation capability, localization flexibility, high efficiency, low scaling-up cost, and excellent long charge/discharge cycle life. RFBs typically use metal ions as reacting species. The most exploited types are all-vanadium RFBs (VRFBs). Here, we discuss the core components for the VRFBs, including the development and application of different types of membranes, electrode materials, and stack system. In addition, we introduce the recent progress in the discovery of novel electrolytes, such as redox-active organic compounds, polymers, and organic/inorganic suspensions. Versatile structures, tunable properties, and abundant resources of organic-based electrolytes make them suitable for cost-effective stationary applications. With the active species in solid form, suspension electrolytes are expected to provide enhanced volumetric energy densities.

The DNA sensing pathway triggers innate immune responses against DNA virus infection, and NF-B signaling plays a critical role in establishing innate immunity. We report here that the herpes simplex virus 1 (HSV-1) ubiquitinspecific protease (UL36USP), which is a deubiquitinase (DUB), antagonizes NF-B activation, depending on its DUB activity. In this study, ectopically expressed UL36USP blocked promoter activation of beta interferon (IFN-␤) and NF-B induced by cyclic GMP-AMP synthase (cGAS) and stimulator of interferon genes (STING). UL36USP restricted NF-B activation mediated by overexpression of STING, TANKbinding kinase 1, IB kinase ␣ (IKK␣), and IKK␤, but not p65. UL36USP was also shown to inhibit IFN-stimulatory DNA-induced IFN-␤ and NF-B activation under conditions of HSV-1 infection. Furthermore, UL36USP was demonstrated to deubiquitinate IB␣ and restrict its degradation and, finally, abrogate NF-B activation. More importantly, the recombinant HSV-1 lacking UL36USP DUB activity, denoted as C40A mutant HSV-1, failed to cleave polyubiquitin chains on IB␣. For the first time, UL36USP was shown to dampen NF-B activation in the DNA sensing signal pathway to evade host antiviral innate immunity.IMPORTANCE It has been reported that double-stranded-DNA-mediated NF-B activation is critical for host antiviral responses. Viruses have established various strategies to evade the innate immune system. The N terminus of the HSV-1 UL36 geneencoded protein contains the DUB domain and is conserved across all herpesviruses. This study demonstrates that UL36USP abrogates NF-B activation by cleaving polyubiquitin chains from IB␣ and therefore restricts proteasome-dependent degradation of IB␣ and that DUB activity is indispensable for this process. This study expands our understanding of the mechanisms utilized by HSV-1 to evade the host antiviral innate immune defense induced by NF-B signaling.KEYWORDS HSV-1, DNA sensor, UL36, NF-B, IB␣ C ells have developed plenty of ways to govern their homeostasis, and the recognition of double-stranded DNA (dsDNA) by DNA sensors is a central host cellular defense against DNA virus infection. Among these DNA sensors, cyclic GMP-AMP synthase (cGAS), which is a nucleotidyltransferase, has been demonstrated to be the predominant cytosolic DNA sensor. Upon binding to DNA fragments, cGAS utilizes GTP and ATP to produce cyclic-GMP-AMP (cGAMP) through its enzymatic activity, and cGAMP activates an endoplasmic reticulum (ER)-resident receptor, stimulator of interferon genes (STING) (1). Activated STING then recruits TANK-binding kinase 1 (TBK1) and traffics from the ER to a perinuclear endosomal compartment, leading to the activation of transcription factors NF-B and interferon (IFN) regulatory factor 3 (IRF3), which induce IFN-␤ production (1-4).

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