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Rare earth (RE 3+ )-doped phosphors generally suffer from thermal quenching, in which their photoluminescence (PL) intensities decrease at high temperatures. Herein, we report a class of unique two-dimensional negative-thermal-expansion phosphor of Sc 2 (MoO 4 ) 3 :Yb/Er. By virtue of the reduced distances between sensitizers and emitters as well as confined energy migration with increasing the temperature, a 45-fold enhancement of green upconversion (UC) luminescence and a 450-fold enhancement of near-infrared downshifting (DS) luminescence of Er 3+ are achieved upon raising the temperature from 298 to 773 K. The thermally boosted UC and DS luminescence mechanism is systematically investigated through in situ temperature-dependent Raman spectroscopy, synchrotron X-ray diffraction and PL dynamics. Moreover, the luminescence lifetime of 4 I 13/2 of Er 3+ in Sc 2 (MoO 4 ) 3 :Yb/Er displays a strong temperature dependence, enabling luminescence thermometry with the highest relative sensitivity of 12.3%/K at 298 K and low temperature uncertainty of 0.11 K at 623 K. These findings may gain a vital insight into the design of negative-thermal-expansion RE 3+ -doped phosphors for versatile applications. Rare-earth doped phosphors with negative thermal expansion (NTE) may display thermally-enhanced emission, but their performance is generally limited. Here the authors report thermally-boosted green upconversion luminescence and near-infrared downshifting luminescence in Sc 2 (MoO 4 ) 3 :Yb/Er phosphors with two-dimensional NTE, and their application in temperature sensing.

The mechanisms on metabolic regulation of immune responses are still elusive. We show here that viral infection induces immediate-early NF-κB activation independent of viral nucleic acid-triggered signaling, which triggers a rapid transcriptional induction of bile acid (BA) transporter and rate-limiting biosynthesis enzymes as well as accumulation of intracellular BAs in divergent cell types. The accumulated intracellular BAs activate SRC kinase via the TGR5-GRK-β-arrestin axis, which mediates tyrosine phosphorylation of multiple antiviral signaling components including RIG-I, VISA/MAVS, MITA/STING, TBK1 and IRF3. The tyrosine phosphorylation of these components by SRC conditions for efficient innate antiviral immune response. Consistently, TGR5 deficiency impairs innate antiviral immunity, whereas BAs exhibit potent antiviral activity in wild-type but not TGR5-deficient cells and mice. Our findings reveal an intrinsic and universal role of intracellular BA metabolism in innate antiviral immunity.

African swine fever (ASF) is a highly contagious and often fatal viral disease caused by African swine fever virus (ASFV), which poses a significant economic burden on the global pig industry. ASFV infection triggers a robust production of proinflammatory cytokines, leading to severe inflammation that contributes significantly to the high mortality rate associated with ASF. However, the underlying mechanisms remain incompletely understood. Here, we identified the ASFV B169L protein (pB169L) as a viroporin that exerts dual functions in viral replication and proinflammatory responses. We demonstrated that pB169L formed oligomeric calcium (Ca 2+ )-permeable channels in vitro by bilayer lipid membrane assay. The ectopically expressed pB169L significantly altered Ca 2+ homeostasis in cells and induced robust proinflammatory responses. Mutagenesis revealed critical residues—including P29, K55, and K57—that are indispensable for channel function and proinflammatory signaling. Importantly, the B169L gene knockdown during ASFV infection reduced inflammasome activation and viral replication, highlighting its dual role as both a structural component of virus and an inflammatory mediator. These findings provide the first direct evidence that ASFV encodes a functional viroporin and uncover a novel mechanism by which ASFV manipulates Ca 2+ homeostasis to drive inflammasome activation, offering new insights into ASFV pathogenesis and potential antiviral targets.

Multifunctional materials with a coexistence of proton conduction properties, single–molecule magnet (SMM) behaviors and magneto–optical Faraday effects have rarely been reported. Herein, a new pair of Cu(II)–Dy(III) enantiomers, [DyCu2(RR/SS–H2L)2(H2O)4(NO3)2]·(NO3)·(H2O) (R–1 and S–1) (H4L = [RR/SS] –N,N′–bis [3–hydroxysalicylidene] –1,2–cyclohexanediamine), has been designed and prepared using homochiral Schiff–base ligands. R–1 and S–1 contain linear Cu(II)–Dy(III)–Cu(II) trinuclear units and possess 1D stacking channels within their supramolecular networks. R–1 and S–1 display chiral optical activity and strong magneto–optical Faraday effects. Moreover, R–1 shows a zero–field SMM behavior. In addition, R–1 demonstrates humidity– and temperature–dependent proton conductivity with optimal values of 1.34 × 10−4 S·cm−1 under 50 °C and 98% relative humidity (RH), which is related to a 1D extended H–bonded chain constructed by water molecules, nitrate and phenol groups of the RR–H2L ligand.

African swine fever virus (ASFV) is the causative agent of African swine fever (ASF), a devastating disease epidemic in Asia and Europe. Large knowledge gaps regarding the biological characteristics of viral structural proteins have severely hindered the development of vaccines against ASF. The p22 protein, an internal envelope membrane protein of ASFV, is one such protein that is yet to be deciphered despite its significance. Here, our results indicated that p22 is not essential for the morphogenesis and replication of ASFV in porcine alveolar macrophages. The ASFV p22 negatively regulates the IFN- β -triggered activation of the Janus kinase-signal transducer and activator of transcription (JAK-STAT) signaling pathway. Mechanistically, the ASFV p22 promotes the association of the Tax1-binding protein 1 (TAX1BP1) with the type I IFN receptor 1 (IFNAR1) via its transmembrane region, thereby facilitating the autophagic degradation of IFNAR1 and impairing the host antiviral responses at the initial step of JAK-STAT signaling pathway. These findings clarify the biological functions of p22 in ASFV replication and uncover a novel autophagy degradation mechanism for IFNAR1, which provide a novel theoretical basis for understanding the biological characteristics of ASFV and may contribute to the development of vaccines and antiviral therapies against ASF.

Diketopyrrolopyrrole (DPP) is an important type of π-conjugated building block for high-performance organic electronic materials. DPP-based conjugated materials are usually synthesized via Suzuki, Stille, or Negishi cross-coupling reactions, which require organometallic precursors. In this paper, a series of novel phenyl-cored DPP molecules, including five meta-phenyl-cored molecules and four para-phenyl-cored molecules, have been synthesized in moderate to good yields, in a facile manner, through the Pd-catalyzed direct arylation of C–H bonds, and their optoelectrical properties have been investigated in detail. All new molecules have been fully characterized by NMR, MALDI-TOF MS, elemental analysis, UV–visible spectroscopy, and cyclic voltammetry. This synthetic strategy has evident advantages of atom- and step-economy and low cost, compared with traditional cross-coupling reactions.

African swine fever (ASF) is a highly contagious and severe hemorrhagic disease caused by African swine fever virus (ASFV). Currently, few safe and effective vaccines or antiviral drugs are available for its prevention. Interferon (IFN), a key component of innate antiviral immunity, induces interferon-stimulated genes (ISGs) by activating the JAK-STAT signalling pathway, resulting in antiviral effects. ASFV strains, including ASFV SY18, ASFV HLJ18, and ASFV BA71V, are highly sensitive to IFN-I treatment; however, the mechanisms by which ASFV antagonizes the host type I IFN response have not been fully elucidated. In this study, we identified the ASFV B125R protein (pB125R) as a negative regulator of the JAK-STAT pathway. We observed that ectopically expressed pB125R significantly suppressed the IFN-β-triggered activation of JAK-STAT signalling in HEK293T and PK-15 cells. Mechanistic studies revealed that pB125R binds to IFNAR2 and promotes its autophagic degradation, impairing the signal transduction of the IFN response at an early stage. This ultimately reduces the nuclear translocation of the ISGF3 complex and decreases ISG production. Our findings highlight the immunosuppressive activity of pB125R and reveal a novel mechanism by which ASFV evades the host IFN response, contributing to potential strategies for developing vaccines and therapeutics against ASF.

The African swine fever virus (ASFV) is an ancient, structurally complex, double-stranded DNA virus that causes African swine fever. Since its discovery in Kenya and Africa in 1921, no effective vaccine or antiviral strategy has been developed. Therefore, the selection of more suitable vaccines or antiviral targets is the top priority to solve the African swine fever virus problem. B125R, one of the virulence genes of ASFV, encodes a non-structural protein (pB125R), which is important in ASFV infection. However, the epitope of pB125R is not well characterized at present. We observed that pB125R is specifically recognized by inactivated ASFV-positive sera, suggesting that it has the potential to act as a protective antigen against ASFV infection. Elucidation of the antigenic epitope within pB125R could facilitate the development of an epitope-based vaccine targeting ASFV. In this study, two strains of monoclonal antibodies (mAbs) against pB125R were produced by using the B cell hybridoma technique, named 9G11 and 15A9. The antigenic epitope recognized by mAb 9G11 was precisely located by using a series of truncated ASFV pB125R. The 52DPLASQRDIYY62 (epitope on ASFV pB125R) was the smallest epitope recognized by mAb 9G11 and this epitope was highly conserved among different strains. The key amino acid sites were identified as D52, Q57, R58, and Y62 by the single-point mutation of 11 amino acids of the epitope by alanine scanning. In addition, the immunological effects of the epitope (pB125R-DY) against 9G11 were evaluated in mice, and the results showed that both full-length pB125R and the epitope pB125R-DY could induce effective humoral and cellular immune responses in mice. The mAbs obtained in this study reacted with the eukaryotic-expressed antigen proteins and the PAM cell samples infected with ASFV, indicating that the mAb can be used as a good tool for the detection of ASFV antigen infection. The B cell epitopes identified in this study provide a fundamental basis for the research and development of epitope-based vaccines against ASFV.

African swine fever (ASF), caused by African swine fever virus (ASFV), is a highly contagious and fatal disease found in swine. However, the viral proteins and mechanisms responsible for immune evasion are poorly understood, which has severely hindered the development of vaccines. This review mainly focuses on studies involving the innate antiviral immune response of the host and summarizes the latest studies on ASFV genes involved in interferon (IFN) signaling and inflammatory responses. We analyzed the effects of candidate viral proteins on ASFV infection, replication and pathogenicity and identified potential molecular targets for novel ASFV vaccines. These efforts will contribute to the construction of novel vaccines and wonder therapeutics for ASF.

Monodispersed spheres (1–4 μm in diameter) of BaWO 4 :Eu 3+ (hereafter BWO:Eu) red-phosphor exhibiting intense emission at 615 nm were synthesized via a mild hydrothermal method. X-ray diffraction, scanning electron microscope, photoluminescence excitation and emission spectra, and decay curve were used to characterize the properties of BWO:Eu phosphors. An intense red emission was obtained by exciting either into the 5 L 6 state with 394 nm or the 5 D 2 state with 465 nm, that correspond to two popular emission lines from near-UV and blue LED chips, respectively. The values of Ω 2,4 experimental intensity parameters (13.8 × 10 −20 and 8.2 × 10 −20  cm 2 ) are determined. The high-emission quantum efficiency of the BWO:Eu phosphor suggests this material could be promising red phosphors for generating white light in phosphor-converted white light-emitting diodes.