The Biocontrol Effects of the Bacillus licheniformis W10 Strain and Its Antifungal Protein Against Brown Rot in Peach

The biocontrol effects of Bacillus licheniformis W10 bacterial suspension and its antifungal protein on peach brown rot caused by Monilinia fructicola in storage peach fruits and the effects on fruit quality were investigated. The results showed that the fruit disease suppression of B. licheniformis W10 bacterial suspension and antifungal protein were significantly higher than that of the control. Inoculation of bacterial suspension and antifungal protein prior to M. fructicola gave a better biocontrol effect, and the higher concentrations of bacterial (1 × 1010 cfu · mL−1) and antifungal protein (3.0 mg · mL−1) performed better control effects. The environmental conditions, such as temperature and humidity, affected biocontrol effects of W10 bacterial suspension and antifungal protein. The influence of environment conditions on the activity of antifungal protein was less than that on bacterial suspension. Moreover, lower temperature (4 °C) and relative humidity (RH 70%–75%) were favorable to prevent peach brown rot by W10 bacterial suspension and its antifungal protein. The W10 bacterial suspension and antifungal protein amended with calcium [0.1% Ca(NO3)2] could enhance the biocontrol effects, and obviously put off the occurrence of peach brown rot. In addition, the bacterial suspension and antifungal protein significantly reduced the natural decay rates of peach fruits during storage, and the effects were equal to carbendazim. Moreover, both W10 bacterial suspension and antifungal protein treatments did not have effects on external and internal fruit appearance, such as chromatic aberration parameter L* of flesh, flesh firmness, soluble solids content and weight loss. Therefore, the B. licheniformis W10 is a potential biocontrol factor for peach brown rot

Baroreceptor-Inspired Microneedle Skin Patch for Pressure-Controlled Drug Release

Objective: We have developed a baroreceptor-inspired microneedle skin patch for pressure-controlled drug release. Impact Statement: This design is inspired by the skin baroreceptors, which are mechanosensitive elements of the peripheral nervous system. We adopt the finger touching to trigger the electric stimulation, ensuring a fast-response and user-friendly administration with potentially minimal off-target effects. Introduction: Chronic skin diseases bring about large, recurrent skin damage and often require convenient and timely transdermal treatment. Traditional methods lack spatiotemporal controllable dosage, leaving a risk of skin irritation or drug resistance issues. Methods: The patch consists of drug-containing microneedles and stretchable electrode array. The electrode array, integrated with the piezoconductive switch and flexible battery, provides a mild electric current only at the spot that is pressed. Drugs in microneedles will then flow along the current into the skin tissues. The stretchable feature also provides the mechanical robustness and electric stability of the device on large skin area. Results: This device delivers Cy3 dye in pig skin with spatiotemporally controlled dosage, showing ~8 times higher fluorescence intensity than the passive delivery. We also deliver insulin and observe the reduction of the blood glucose level in the mouse model upon pressing. Compared with passive delivery without pressing, the dosage of drugs released by the simulation is 2.83 times higher. Conclusion: This baroreceptor-inspired microneedle skin patch acts as a good example of the biomimicking microneedle device in the precise control of the drug release profile at the spatiotemporal resolution

DNAJA3 Interacts with PEDV S1 Protein and Inhibits Virus Replication by Affecting Virus Adsorption to Host Cells

Porcine epidemic diarrhea virus (PEDV) infection causes huge economic losses to the pig industry worldwide. DNAJA3, a member of the Hsp40 family proteins, is known to play an important role in the replication of several viruses. However, it remains unknown if it interacts with PEDV. We found that DNAJA3 interacted with PEDV S1, initially with yeast two-hybrid screening and later with Co-IP, GST pull-down, and confocal imaging. Further experiments showed the functional relationship between DNAJA3 and PEDV in the infected IPEC-J2 cells. DNAJA3 overexpression significantly inhibited PEDV replication while its knockdown had the opposite effect, suggesting that it is a negative regulator of PEDV replication. In addition, DNAJA3 expression could be downregulated by PEDV infection possibly as the viral strategy to evade the suppressive role of DNAJA3. By gene silencing and overexpression, we were able to show that DNAJA3 inhibited PEDV adsorption to IPEC-J2 cells but did not affect virus invasion. In conclusion, our study provides clear evidence that DNAJA3 mediates PEDV adsorption to host cells and plays an antiviral role in IPEC-J2 cells

The Temperature-Dependent Thermal Expansion of 2,6-Diamino-3,5-dinitropyrazine-1-oxide Effected by Hydrogen Bond Network Relaxation

<div><p>The temperature-dependent thermal expansion of 2,6-diamino-3,5-dinitropyrazine-1-oxide (LLM-105) was investigated by using powder X-ray diffraction (PXRD) together with Rietveld refinement to estimate the dimension at a crystal lattice level. In the temperature range of 30–200°C, the coefficient of thermal expansion (CTE) of LLM-105 is temperature dependent, which is different from other explosives, such as hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX), 2,2′,4,4′,6,6′-hexanitrostilbene (HNS) and octahydro-1,3,5,7-tetranitro-1,3,5,7-tetrazocine (HMX), with constant CTEs. The results of temperature-dependent infrared (IR) spectra indicated that the intermolecular hydrogen bond network relaxes with increasing temperature, which results in temperature-dependent thermal expansion. In this work, more accurate CTEs for LLM-105 crystals are obtained and the effects of the hydrogen bond network on the thermal expansion are further clarified. These results are beneficial to the design of materials with structural peculiarities and as-expected thermal expansion to satisfy different application requirements.</p></div

Porcine Epidemic Diarrhea Virus Antagonizes Host IFN-λ-Mediated Responses by Tilting Transcription Factor STAT1 toward Acetylation over Phosphorylation To Block Its Activation

ABSTRACT Porcine epidemic diarrhea virus (PEDV) is the main etiologic agent causing acute swine epidemic diarrhea, leading to severe economic losses to the pig industry. PEDV has evolved to deploy complicated antagonistic strategies to escape from host antiviral innate immunity. Our previous study demonstrated that PEDV downregulates histone deacetylase 1 (HDAC1) expression by binding viral nucleocapsid (N) protein to the transcription factor Sp1, inducing enhanced protein acetylation. We hypothesized that PEDV inhibition of HDAC1 expression would enhance acetylation of the molecules critical in innate immune signaling. Signal transducer and activator of transcription 1 (STAT1) is a crucial transcription factor regulating expression of interferon (IFN)-stimulated genes (ISGs) and anti-PEDV immune responses, as shown by overexpression, chemical inhibition, and gene knockdown in IPEC-J2 cells. We further show that PEDV infection and its N protein overexpression, although they upregulated STAT1 transcription level, could significantly block poly(I·C) and IFN-λ3-induced STAT1 phosphorylation and nuclear localization. Western blotting revealed that PEDV and its N protein promote STAT1 acetylation via downregulation of HDAC1. Enhanced STAT1 acetylation due to HDAC1 inhibition by PEDV or MS-275 (an HDAC1 inhibitor) impaired STAT1 phosphorylation, indicating that STAT1 acetylation negatively regulated its activation. These results, together with our recent report on PEDV N-mediated inhibition of Sp1, clearly indicate that PEDV manipulates the Sp1-HDAC1-STAT1 signaling axis to inhibit transcription of OAS1 and ISG15 in favor of its replication. This novel immune evasion mechanism is realized by suppression of STAT1 activation through preferential modulation of STAT1 acetylation over phosphorylation as a result of HDAC1 expression inhibition. IMPORTANCE PEDV has developed sophisticated evasion mechanisms to escape host IFN signaling via its structural and nonstructural proteins. STAT1 is one of the key transcription factors in regulating expression of ISGs. We found that PEDV and its N protein inhibit STAT1 phosphorylation and nuclear localization via inducing STAT1 acetylation as a result of HDAC1 downregulation, which, in turn, dampens the host IFN signaling activation. Our study demonstrates a novel mechanism that PEDV evades host antiviral innate immunity through manipulating the reciprocal relationship of STAT1 acetylation and phosphorylation. This provides new insights into the pathogenetic mechanisms of PEDV and even other coronaviruses

Waste to Treasure: Regeneration of Porous Co-Based Catalysts from Spent LiCoO₂ Cathode Materials for an Efficient Oxygen Evolution Reaction

The increasing demand for portable electronic devices and electric vehicles (EVs) has triggered the rapid growth of the rechargeable Li-ion battery (LIB) market. However, in the near future, it is predicted that a large amount of spent LIBs will be scrapped, imposing huge pressure on environmental protection and resource reclaiming. The effective recycling or regeneration of the spent LIBs not only relieves the environmental burdens but also avoids the waste of valuable metal resources. Herein, a porous Co9S8/Co3O4 heterostructure is successfully synthesized from the spent LiCoO2 (LCO) cathode materials via a conventional hydrometallurgy and sulfidation process. The fabricated Co9S8/Co3O4 catalyst exhibits high catalytic activity toward oxygen evolution reaction (OER) in an alkaline solution, with an overpotential of 274 mV to achieve the current density of 10 mA cm–2 and a Tafel slope of 48.7 mV dec–1. This work demonstrates a facile regeneration process of Co-based electrocatalysts from the spent LiCoO2 cathode materials for efficient oxygen evolution reaction