ABSTRACT
Porcine epidemic diarrhea virus (PEDV) results in PED, which is an infectious intestinal disease with the representative features of diarrhea, vomiting, and dehydration. PEDV infects neonatal piglets, causing high mortality rates. Therefore, elucidating the interaction between the virus and host in preventing and controlling PEDV infection is of immense significance. We found a new antiviral function of the host protein, RNA-binding motif protein 14 (RBM14), which can inhibit PEDV replication via the activation of autophagy and interferon (IFN) signal pathways. We found that RBM14 can recruit cargo receptor p62 to degrade PEDV nucleocapsid (N) protein through the RBM14-p62-autophagosome pathway. Furthermore, RBM14 can also improve the antiviral ability of the hosts through interacting with mitochondrial antiviral signaling protein to induce IFN expression. These results highlight the novel mechanism underlying RBM14-induced viral restriction. This mechanism leads to the degradation of viral N protein via the autophagy pathway and upregulates IFN for inhibiting PEDV replication; thus, offering new ways for preventing and controlling PED.IMPORTANCEPorcine epidemic diarrhea virus (PEDV) is a vital reason for diarrhea in neonatal piglets, which causes high morbidity and mortality rates. There is currently no effective vaccine or drug to treat and prevent infection with the PEDV. During virus infection, the host inhibits virus replication through various antiviral factors, and at the same time, the virus antagonizes the host's antiviral reaction through its own encoded protein, thus completing the process of virus replication. Our study has revealed that the expression of RNA-binding motif protein 14 (RBM14) was downregulated in PEDV infection. We found that RBM14 can recruit cargo receptor p62 to degrade PEDV N protein via the RBM14-p62-autophagosome pathway and interacted with mitochondrial antiviral signaling protein and TRAF3 to activate the interferon signal pathway, resulting in the inhibition of PEDV replication.
Subject(s)
Coronavirus Infections , Interferons , Porcine epidemic diarrhea virus , Swine Diseases , Animals , Autophagy , Cell Line , Coronavirus Infections/immunology , Coronavirus Infections/metabolism , Coronavirus Infections/veterinary , Diarrhea/veterinary , Interferons/metabolism , Nucleocapsid Proteins/metabolism , Porcine epidemic diarrhea virus/physiology , Swine , Swine Diseases/immunology , Swine Diseases/metabolism , Virus ReplicationABSTRACT
Excessive accumulation of reduced nicotinamide adenine dinucleotide (NADH) within biological organisms is closely associated with many diseases. It remains a challenge to efficiently convert superfluous and detrimental NADH to NAD+. NADH oxidase (NOX) is a crucial oxidoreductase that catalyzes the oxidation of NADH to NAD+. Herein, M1M2 (Mi=V/Mn/Fe/Co/Cu/Mo/Rh/Ru/Pd, i = 1 or 2) mated-atom nanozymes (MANs) are designed by mimicking natural enzymes with polymetallic active centers. Excitingly, RhCo MAN possesses excellent and sustainable NOX-like activity, with Km-NADH (16.11 µM) being lower than that of NOX-mimics reported so far. Thus, RhCo MAN can significantly promote the regeneration of NAD+ and regulate macrophage polarization toward the M2 phenotype through down-regulation of TLR4 expression, which may help to recover skin regeneration. However, RhRu MAN with peroxidase-like activity and RhMn MAN with superoxide dismutase-like activity exhibit little modulating effects on eczema. This work provides a new strategy to inhibit skin inflammation and promote skin regeneration.
ABSTRACT
Porcine epidemic diarrhea virus (PEDV) causes severe morbidity and mortality among newborn piglets. It significantly threatens the porcine industry in China and around the globe. To accelerate the developmental pace of drugs or vaccines against PEDV, a deeper understanding of the interaction between viral proteins and host factors is crucial. The RNA-binding protein, polypyrimidine tract-binding protein 1 (PTBP1), is crucial for controlling RNA metabolism and biological processes. The present work focused on exploring the effect of PTBP1 on PEDV replication. PTBP1 was upregulated during PEDV infection. The PEDV nucleocapsid (N) protein was degraded through the autophagic and proteasomal degradation pathways. Moreover, PTBP1 recruits MARCH8 (an E3 ubiquitin ligase) and NDP52 (a cargo receptor) for N protein catalysis and degradation through selective autophagy. Furthermore, PTBP1 induces the host innate antiviral response via upregulating the expression of MyD88, which then regulates TNF receptor-associated factor 3/ TNF receptor-associated factor 6 expression and induces the phosphorylation of TBK1 and IFN regulatory factor 3. These processes activate the type â IFN signaling pathway to antagonize PEDV replication. Collectively, this work illustrates a new mechanism related to PTBP1-induced viral restriction, where PTBP1 degrades the viral N protein and induces type â IFN production to suppress PEDV replication.
Subject(s)
Coronavirus Infections , Interferon Type I , Polypyrimidine Tract-Binding Protein , Porcine epidemic diarrhea virus , Proteolysis , Swine Diseases , Virus Replication , Animals , Cell Line , Chlorocebus aethiops , Coronavirus Infections/genetics , Coronavirus Infections/veterinary , Interferon Type I/metabolism , Porcine epidemic diarrhea virus/physiology , Signal Transduction , Swine , Swine Diseases/genetics , Swine Diseases/virology , Vero Cells , Polypyrimidine Tract-Binding Protein/metabolismABSTRACT
Due to the extensive genetic and antigenic variation in Porcine Reproductive and Respiratory Syndrome Virus (PRRSV), as well as its rapid mutability and evolution, PRRS prevention and control can be challenging. An expeditious and sensitive neutralization assay for PRRSV is presented to monitor neutralizing antibodies (NAbs) in serum during vaccine research. Here, a PRRSV expressing eGFP was successfully rescued with reverse genetics based on the infectious clone HuN4-F112-eGFP which we constructed. The fluorescent protein expressions of the reporter viruses remained stable for at least five passages. Based on this reporter virus, the neutralization assay can be easily used to evaluate the level of NAbs by counting cells with green fluorescence. Compared with the classical CPE assay, the newly developed assay increases sensitivity by one- to four-fold at the early antibody response stage, thus saving 2 days of assay waiting time. By using this assay to unveil the dynamics of neutralizing antibodies against PRRSV, priming immunity through either a single virulent challenge or only vaccination could produce limited NAbs, but re-infection with PRRSV would induce a faster and stronger NAb response. Overall, the novel HuN4-F112-eGFP-based neutralization assay holds the potential to provide a highly efficient platform for evaluating the next generation of PRRS vaccines.
ABSTRACT
Porcine epidemic diarrhea (PED) indicates the disease of the acute and highly contagious intestinal infection due to porcine epidemic diarrhea virus (PEDV), with the characteristics of watery diarrhea, vomiting, and dehydration. One of the reasons for diarrhea and death of piglets is PEDV, which leads to 100% mortality in neonatal piglets. Therefore, it is necessary to explore the interaction between virus and host to prevent and control PEDV. This study indicated that the host protein, pre-mRNA processing factor 19 (PRPF19), could be controlled by the signal transducer as well as activator of transcription 1 (STAT1). Thus, PEDV replication could be hindered through selective autophagy. Moreover, PRPF19 was found to recruit the E3 ubiquitin ligase MARCH8 to the N protein for ubiquitination. For the purpose of degradation, the ubiquitin N protein is acknowledged by the cargo receptor NDP52 and transported to autolysosomes, thus inhibiting virus proliferation. To conclude, a unique antiviral mechanism of PRPF19-mediated virus restriction was shown. Moreover, a view of the innate immune response and protein degradation against PEDV replication was provided in this study. IMPORTANCE The highly virulent porcine epidemic diarrhea virus (PEDV) emerged in 2010, and causes high mortality rates in newborn pigs. There are no effective and safe vaccines against the highly virulent PEDV. This virus has caused devastating economic losses in the pork industry worldwide. Studying the relationship between virus and host antiviral factors is important to develop the new antiviral strategies. This study identified the pre-mRNA processing factor 19 (PRPF19) as a novel antiviral protein in PEDV replication and revealed its viral restriction mechanisms for the first time. PRPF19 recruited the E3 ubiquitin ligase MARCH8 to the PEDV N protein for ubiquitination, and the ubiquitin N protein was acknowledged by the cargo receptor NDP52 and transported to autolysosomes for degradation. Our findings provide new insights in host antiviral factors PRPF19 that regulate the selective autophagy protein degradation pathway to inhibit PEDV replication.
Subject(s)
Capsid Proteins , Coronavirus Infections , Porcine epidemic diarrhea virus , Swine Diseases , Animals , Capsid Proteins/metabolism , Coronavirus Infections/immunology , Coronavirus Infections/veterinary , Coronavirus Infections/virology , Porcine epidemic diarrhea virus/physiology , Swine , Swine Diseases/immunology , Swine Diseases/virology , Ubiquitin-Protein Ligases/metabolism , Ubiquitins , Virus Replication/genetics , Nuclear Proteins/metabolism , AutophagyABSTRACT
IMPORTANCE: As a member of the δ-coronavirus family, porcine deltacoronavirus (PDCoV) is a vital reason for diarrhea in piglets, which can contribute to high morbidity and mortality rates. Initially identified in Hong Kong in 2012, the virus has rapidly spread worldwide. During PDCoV infection, the virus employs evasion mechanisms to evade host surveillance, while the host mounts corresponding responses to impede viral replication. Our research has revealed that PDCoV infection down-regulates the expression of PGAM5 to promote virus replication. In contrast, PGAM5 degrades PDCoV N through autophagy by interacting with the cargo receptor P62 and the E3 ubiquitination ligase STUB1. Additionally, PGAM5 interacts with MyD88 and TRAF3 to activate the IFN signal pathway, resulting in the inhibition of viral replication.
Subject(s)
Coronavirus Infections , Coronavirus Nucleocapsid Proteins , Deltacoronavirus , Interferon Type I , Mitochondrial Proteins , Phosphoprotein Phosphatases , Proteolysis , Swine Diseases , Swine , Virus Replication , Animals , Coronavirus Infections/immunology , Coronavirus Infections/veterinary , Coronavirus Infections/virology , Interferon Type I/immunology , Signal Transduction , Swine/virology , Swine Diseases/virology , Ubiquitin-Protein Ligases/metabolism , Virus Replication/immunology , Coronavirus Nucleocapsid Proteins/metabolism , Deltacoronavirus/immunology , Deltacoronavirus/metabolism , Phosphoprotein Phosphatases/metabolism , Mitochondrial Proteins/metabolism , Down-Regulation , Immune Evasion , RNA-Binding Proteins/metabolismABSTRACT
Porcine epidemic diarrhea virus (PEDV) causes diarrhea and dehydration in pigs and leads to great economic losses in the commercial swine industry. However, the underlying molecular mechanisms of host response to viral infection remain unclear. In the present study, we investigated a novel mechanism by which RALY, a member of the heterogeneous nuclear ribonucleoprotein family, significantly promotes the degradation of the PEDV nucleocapsid (N) protein to inhibit viral replication. Furthermore, we identified an interaction between RALY and the E3 ubiquitin ligase MARCH8 (membrane-associated RING-CH 8), as well as the cargo receptor NDP52 (nuclear dot protein 52 kDa), suggesting that RALY could suppress PEDV replication by degrading the viral N protein through a RALY-MARCH8-NDP52-autophagosome pathway. Collectively, these results suggest a preventive role of RALY against PEDV infection via the autophagy pathway and open up the possibility of inducing RALY in vivo as an effective prophylactic and preventive treatment for PEDV infection.
Subject(s)
Coronavirus Infections , Porcine epidemic diarrhea virus , Swine Diseases , Animals , Autophagy , Chlorocebus aethiops , Coronavirus Infections/veterinary , Nucleocapsid Proteins , Porcine epidemic diarrhea virus/physiology , Ribonucleoproteins , Swine , Vero Cells , Virus ReplicationABSTRACT
Near-infrared-II (NIR-II) imaging has shown great potential for monitoring the pathological progression and deep tissue imaging but is limited to present unmet NIR-II agent. Present fluorophores show a promising prospect for NIR-II imaging, but brightness and photostability are still highly challenging during real-time monitoring. In this work, atom-engineered NIR-II Au24 Cd1 clusters with ultrahigh brightness, stability, and photostability are developed via single atomic Cd doping. Single atom Cd substitutions contribute to Cd 4d state in HOMO and redistribution of energy level near the gap, exhibiting 56-fold fluorescence enhancement of Au24 Cd1 clusters. Meanwhile, single atomic Cd reinforces CdAu bond energy, formation energy, and stabilized cluster structure, leading to persistent stability for up to 1 month without decay, as well as excellent photostability of 1 h without photobleaching, much longer than clinically approved indocyanine green (<5 min). In vivo imaging shows gold clusters can monitor acute kidney injury (AKI) even after 72 h of injury, enabling evaluating progression at a very long window. Meanwhile, the bioactive gold clusters can alleviate AKI-induced oxidative stress damage and acute neuroinflammation. Single atom-engineered gold clusters exhibit molecular tracking and diagnostic prospect in kidney-related diseases.
Subject(s)
Acute Kidney Injury , Gold , Humans , Gold/chemistry , Cadmium , Optical Imaging/methods , Indocyanine Green , Fluorescent Dyes/chemistryABSTRACT
Porcine epidemic diarrhea virus (PEDV) is a re-emerging enteric coronavirus currently spreading in several nations and inflicting substantial financial damages on the swine industry. The currently available coronavirus vaccines do not provide adequate protection against the newly emerging viral strains. It is essential to study the relationship between host antiviral factors and the virus and to investigate the mechanisms underlying host immune response against PEDV infection. This study shows that heterogeneous nuclear ribonucleoprotein K (hnRNP K), the host protein determined by the transcription factor KLF15, inhibits the replication of PEDV by degrading the nucleocapsid (N) protein of PEDV in accordance with selective autophagy. hnRNP K was found to be capable of recruiting the E3 ubiquitin ligase, MARCH8, aiming to ubiquitinate N protein. Then, it was found that the ubiquitinated N protein could be delivered into autolysosomes for degradation by the cargo receptor NDP52, thereby inhibiting PEDV proliferation. Moreover, based on the enhanced MyD88 expression, we found that hnRNP K activated the interferon 1 (IFN-1) signaling pathway. Overall, the data obtained revealed a new mechanism of hnRNP K-mediated virus restriction wherein hnRNP K suppressed PEDV replication by degradation of viral N protein using the autophagic degradation pathway and by induction of IFN-1 production based on upregulation of MyD88 expression. IMPORTANCE The spread of the highly virulent PEDV in many countries is still leading to several epidemic and endemic outbreaks. To elucidate effective antiviral mechanisms, it is important to study the relationship between host antiviral factors and the virus and to investigate the mechanisms underlying host immune response against PEDV infection. In the work, we detected hnRNP K as a new host restriction factor which can hinder PEDV replication through degrading the nucleocapsid protein based on E3 ubiquitin ligase MARCH8 and the cargo receptor NDP52. In addition, via the upregulation of MyD88 expression, hnRNP K could also activate the interferon (IFN) signaling pathway. This study describes a previously unknown antiviral function of hnRNP K and offers a new vision toward host antiviral factors that regulate innate immune response as well as a protein degradation pathway against PEDV infection.
Subject(s)
Coronavirus Infections , Heterogeneous-Nuclear Ribonucleoprotein K , Interferon Type I , Porcine epidemic diarrhea virus , Virus Replication , Animals , Antiviral Agents , Chlorocebus aethiops , Coronavirus Infections/veterinary , Heterogeneous-Nuclear Ribonucleoprotein K/genetics , Interferons , Myeloid Differentiation Factor 88 , Nucleocapsid Proteins/physiology , Porcine epidemic diarrhea virus/physiology , Swine , Swine Diseases/virology , Ubiquitin-Protein Ligases , Vero Cells , Interferon Type I/immunologyABSTRACT
Porcine epidemic diarrhea virus (PEDV) is the globally distributed alphacoronavirus that can cause lethal watery diarrhea in piglets, causing substantial economic damage. However, the current commercial vaccines cannot effectively the existing diseases. Thus, it is of great necessity to identify the host antiviral factors and the mechanism by which the host immune system responds against PEDV infection required to be explored. The current work demonstrated that the host protein, the far upstream element-binding protein 3 (FUBP3), could be controlled by the transcription factor TCFL5, which could suppress PEDV replication through targeting and degrading the nucleocapsid (N) protein of the virus based on selective autophagy. For the ubiquitination of the N protein, FUBP3 was found to recruit the E3 ubiquitin ligase MARCH8/MARCHF8, which was then identified, transported to, and degraded in autolysosomes via NDP52/CALCOCO2 (cargo receptors), resulting in impaired viral proliferation. Additionally, FUBP3 was found to positively regulate type-I interferon (IFN-I) signaling and activate the IFN-I signaling pathway by interacting and increasing the expression of tumor necrosis factor (TNF) receptor-associated factor 3 (TRAF3). Collectively, this study showed a novel mechanism of FUBP3-mediated virus restriction, where FUBP3 was found to degrade the viral N protein and induce IFN-I production, aiming to hinder the replication of PEDV. IMPORTANCE PEDV refers to the alphacoronavirus that is found globally and has re-emerged recently, causing severe financial losses. In PEDV infection, the host activates various host restriction factors to maintain innate antiviral responses to suppress virus replication. Here, FUBP3 was detected as a new host restriction factor. FUBP3 was found to suppress PEDV replication via the degradation of the PEDV-encoded nucleocapsid (N) protein via E3 ubiquitin ligase MARCH8 as well as the cargo receptor NDP52/CALCOCO2. Additionally, FUBP3 upregulated the IFN-I signaling pathway by interacting with and increasing tumor necrosis factor (TNF) receptor-associated factor 3 (TRAF3) expression. This study further demonstrated that another layer of complexity could be added to the selective autophagy and innate immune response against PEDV infection are complicated.
Subject(s)
Coronavirus Infections , Interferon Type I , Nucleocapsid Proteins , Porcine epidemic diarrhea virus , Transcription Factors , Animals , Antiviral Agents , Cell Line , Chlorocebus aethiops , Coronavirus Infections/metabolism , Interferon Type I/genetics , Interferon Type I/metabolism , Nucleocapsid Proteins/metabolism , Porcine epidemic diarrhea virus/physiology , Swine , TNF Receptor-Associated Factor 3 , Transcription Factors/metabolism , Ubiquitin-Protein Ligases , Vero CellsABSTRACT
In global infection and serious morbidity and mortality, porcine epidemic diarrhea virus (PEDV) has been regarded as a dreadful porcine pathogen, but the existing commercial vaccines are not enough to fully protect against the epidemic strains. Therefore, it is of great necessity to feature the PEDV-host interaction and develop efficient countermeasures against viral infection. As an RNA/DNA protein, the trans-active response DNA binding protein (TARDBP) plays a variety of functions in generating and processing RNA, including transcription, splicing, transport, and mRNA stability, which have been reported to regulate viral replication. The current work aimed to detect whether and how TARDBP influences PEDV replication. Our data demonstrated that PEDV replication was significantly suppressed by TARDBP, regulated by KLF16, which targeted its promoter. We observed that through the proteasomal and autophagic degradation pathway, TARDBP inhibited PEDV replication via the binding as well as degradation of PEDV-encoded nucleocapsid (N) protein. Moreover, we found that TARDBP promoted autophagic degradation of N protein via interacting with MARCHF8, an E3 ubiquitin ligase, as well as NDP52, a cargo receptor. We also showed that TARDBP promoted host antiviral innate immune response by inducing interferon (IFN) expression through the MyD88-TRAF3-IRF3 pathway during PEDV infection. In conclusion, these data revealed a new antiviral role of TARDBP, effectively suppressing PEDV replication through degrading virus N protein via the proteasomal and autophagic degradation pathway and activating type I IFN signaling via upregulating the expression of MyD88. IMPORTANCE PEDV refers to the highly contagious enteric coronavirus that has quickly spread globally and generated substantial financial damage to the global swine industry. During virus infection, the host regulates the innate immunity and autophagy process to inhibit virus infection. However, the virus has evolved plenty of strategies with the purpose of limiting IFN-I production and autophagy processes. Here, we identified that TARDBP expression was downregulated via the transcription factor KLF16 during PEDV infection. TARDBP could inhibit PEDV replication through the combination as well as degradation of PEDV-encoded nucleocapsid (N) protein via proteasomal and autophagic degradation pathways and promoted host antiviral innate immune response by inducing IFN expression through the MyD88-TRAF3-IRF3 pathway. In sum, our data identify a novel antiviral function of TARDBP and provide a better grasp of the innate immune response and protein degradation pathway against PEDV infection.
Subject(s)
Coronavirus Infections , DNA-Binding Proteins , Interferon Type I , Porcine epidemic diarrhea virus , Virus Replication , Animals , Coronavirus Infections/veterinary , DNA-Binding Proteins/metabolism , Immunity, Innate , Interferon Regulatory Factor-3/metabolism , Interferon Type I/metabolism , Myeloid Differentiation Factor 88/metabolism , Nucleocapsid Proteins/metabolism , Porcine epidemic diarrhea virus/genetics , Porcine epidemic diarrhea virus/physiology , RNA/metabolism , Signal Transduction , Swine , TNF Receptor-Associated Factor 3/metabolismABSTRACT
African swine fever virus (ASFV) is a highly contagious and deadly virus that leads to high mortality rates in domestic swine populations. Although the envelope protein CD2v of ASFV has been implicated in immunomodulation, the molecular mechanisms underlying CD2v-mediated immunoregulation remain unclear. In this study, we generated a stable CD2v-expressing porcine macrophage (PAM-CD2v) line and investigated the CD2v-dependent transcriptomic landscape using RNA-seq. GO terms enrichment analysis and gene set enrichment analysis revealed that CD2v predominantly affected the organization and assembly process of the extracellular matrix. Wound healing and Transwell assays showed that CD2v inhibited swine macrophage migration. Further investigation revealed a significant decrease in the expression of transcription factor early growth response 1 (EGR1) through inhibiting the activity of extracellular signal-regulated kinase 1 and 2 (ERK1/2). Notably, EGR1 knockout in swine macrophages restricted cell migration, whereas EGR1 overexpression in PAM-CD2v restored the ability of macrophage migration, suggesting that CD2v inhibits swine macrophage motility by downregulating EGR1 expression. Furthermore, we performed chromatin immunoprecipitation and sequencing for EGR1 and the histone mark H3K27 acetylation (H3K27ac), and we found that EGR1 co-localized with the activated histone modification H3K27ac neighboring the transcriptional start sites. Further analysis indicated that EGR1 and H3K27ac co-occupy the promoter regions of cell locomotion-related genes. Finally, by treating various derivatives of swine macrophages with lipopolysaccharides, we showed that depletion of EGR1 decreased the expression of inflammatory cytokines including TNFα, IL1α, IL1ß, IL6, and IL8, which play essential roles in inflammation and host immune response. Collectively, our results provide new insights into the immunomodulatory mechanism of ASFV CD2v.
Subject(s)
African Swine Fever Virus , African Swine Fever , Swine Diseases , Swine , Animals , African Swine Fever Virus/genetics , Cytokines/genetics , Cytokines/metabolism , MAP Kinase Signaling System , Viral Proteins/metabolism , Macrophages , Cell MovementABSTRACT
During 2018-2020, we isolated 32 Eurasian avian-like swine influenza A(H1N1) viruses and their reassortant viruses from pigs in China. Genomic testing identified a novel reassortant H3N1 virus, which emerged in late 2020. Derived from G4 Eurasian H1N1 and H3N2 swine influenza viruses. This virus poses a risk for zoonotic infection.
Subject(s)
Influenza A Virus, H1N1 Subtype , Influenza, Human , Orthomyxoviridae Infections , Swine Diseases , Animals , Birds , Humans , Influenza A Virus, H1N1 Subtype/genetics , Influenza A Virus, H3N2 Subtype/genetics , Influenza A virus , Influenza, Human/epidemiology , Orthomyxoviridae Infections/epidemiology , Orthomyxoviridae Infections/veterinary , Phylogeny , Reassortant Viruses/genetics , Swine , Swine Diseases/epidemiologyABSTRACT
Using the inherent properties of a heterostructure, ultrafast photodetectors with high sensitivity can be progressively developed that have the potential to carve a niche among the optoelectronic devices. In this Letter, a heterojunction photodetector based on SnSe2/Bi2Se3 is constructed, and a visible-infrared photoresponse with good sensitivity at room temperature is obtained. The SnSe2/Bi2Se3 photodetector demonstrates a high Iph/Id ratio of 1.2 × 104 at 0â V. Moreover, the high responsivity of 2.3 A/W, detectivity of 1.6 × 1011 Jones, and fast response time of 40 µs are simultaneously achieved. The presented results offer an alternative route for ultrafast photodetectors with high sensitivity.
ABSTRACT
It is challenging to obtain wafer-scaled aligned films for completely exploiting the promising properties of semiconducting single-walled carbon nanotubes (s-SWCNTs). Aligned s-SWCNTs with a large area can be obtained by combining water evaporation and slow withdrawal-induced self-assembly in a dip-coating process. Moreover, the tunability of deposition morphology parameters such as stripe width and spacing is examined. The polarized Raman results show that s-SWCNTs can be aligned in ±8.6°. The derived two terminal photodetector shows both a high negative responsivity of 41 A/W at 520 nm and high polarization sensitivity. Our results indicate that aligned films with a large area may be useful to electronics- and optoelectronics-related applications.
ABSTRACT
Inspired by the growing family of Van der Waals materials, hBN supported phonon polaritons have attracted much attention due to their inherent hyperbolic dispersion properties in the mid-infrared. However, the lack of tunability imposes a severe restriction on the diversified, functional and integrated applications. Here, we propose a phase-gradient heterostructure metasurface to realize a dynamically tunable and polarization-sensitive perfect absorber in the mid-infrared through combining hBN and phase change VO2. Narrow-band perfect absorption at 7.2 µm can be switched to broadband around 11.2 µm through controlling the temperature of VO2. The governed physics of the bandwidth and absorption differences are demonstrated. Phonon polaritons in hBN phase-gradient configurations and plasmon polaritons in periodic VO2 blocks are respectively excited. We also investigate the absorption dependence on the polarization states of designed absorber. The method of engineering the absorption through controlling the temperature and polarization states opens up a new avenue for tunable applications such as data storage and integrated optical circuits.
ABSTRACT
The Au/SiO2nanocomposite grating coupler with a period of 600 nm was fabricated by implantation of 140 keV Au ions at a fluence of 6 × 1016ions·cm-2in combination with subsequent electron-beam lithography and ion beam etching. The thermal evolution of Au nanoparticles and its influence on the vertical coupling efficiency of the prepared grating coupler has been investigated in detail. The results clearly show that the coupling efficiency of the nanocomposite grating coupler could be affected by the thermal evolution of Au nanoparticles, which increases in the annealing temperature range up to 800 °C, and then decreases at 900 °C and above. Theoretical calculation demonstrates that the change of the coupling efficiency should be closely related to the synergistic effect of the scattering effect and the variation in the volume fraction of Au nanoparticles due to the thermal growth.
ABSTRACT
Ag/SiO2and Au/SiO2samples were prepared by separately implanting 30 keV Ag and Au ions into 0.5-mm-thick SiO2slabs at a fluence of 6 × 1016ion·cm-2, and their optical and structural properties were studied in detail by using a fiber spectrometer and a transmission electron microscope, respectively. Our results showed that the two samples featured by their respective nanocomposite surface layers were asymmetrical in structure, and hence, their characteristic signals in the reflectance spectra excited by the lights incident from the rear surfaces were able to exhibit corresponding blueshifts when the overlays on the implanted surfaces were increased in refractive index with respect to air. Our results also showed that each of characteristic signals was strongly dependent on the localized surface plasmon resonance (LSPR) behavior of the involved Ag or Au nanoparticles (NPs), and it could not appear at a wavelength position smaller than or equal to that of the LSPR absorption peak since the involved Ag or Au NPs were quite small in size. These results meant that the two samples could be regarded as the LSPR sensors with a negative refractive index sensitivity (RIS), although their sensing abilities would lose when the overlays were very large in refractive index. Especially, the two samples were demonstrated to be relatively high in stability because the involved Ag and Au NPs were closely hugged and chemically protected by the matrices of SiO2, and consequently, they could have a chance to become prospective sensing devices in some special fields as long as their RISs and linearities could be improved in the future. The above findings substantially confirmed that the metal ion implantation into transparent dielectric slab was an effective route to the high-stability LSPR sensors.
ABSTRACT
PRDM1 is a tumor suppressor that plays an important role in B and T cell lymphomas. Our previous studies demonstrated that PRDM1ß is a p53-response gene in human colorectal cancer cells. However, the function of PRDM1ß in colorectal cancer cells and colon tumor organoids is not clear. Here we show that PRDM1ß is a p53-response gene in human colon organoids and that low PRDM1 expression predicts poor survival in colon cancer patients. We engineered PRDM1 knockouts and overexpression clones in RKO cells and characterized the PRDM1-dependent transcript landscapes, revealing that both the α and ß transcript isoforms repress MYC-response genes and stem cell-related genes. Finally, we show that forced expression of PRDM1 in human colon cancer organoids prevents the formation and growth of colon tumor organoids in vitro. These results suggest that p53 may exert tumor-suppressive effects in part through a PRDM1-dependent silencing of stem cell genes, depleting the size of the normal intestinal stem cell compartment in response to DNA damage.
Subject(s)
Cell Proliferation/physiology , Colonic Neoplasms/metabolism , Organoids , Positive Regulatory Domain I-Binding Factor 1/physiology , Cell Line, Tumor , Clustered Regularly Interspaced Short Palindromic Repeats , Colon/chemistry , Colon/metabolism , Colonic Neoplasms/genetics , Colonic Neoplasms/mortality , Disease-Free Survival , Humans , Organoids/cytology , Organoids/metabolism , Positive Regulatory Domain I-Binding Factor 1/genetics , Positive Regulatory Domain I-Binding Factor 1/metabolism , Tumor Suppressor Protein p53/genetics , Tumor Suppressor Protein p53/metabolismABSTRACT
Reactive oxygen and nitrogen species (RONS), especially reactive nitrogen species (RNS) are intermediate products during incidence of nervous system diseases, showing continuous damage for traumatic brain injury (TBI). Here, we developed a carbogenic nanozyme, which shows an antioxidant activity 12 times higher than ascorbic acid (AA) and behaves as multienzyme mimetics. Importantly, the nanozyme exhibits an ultrahigh scavenging efficiency (â¼16 times higher than AA) toward highly active RNS, such as â¢NO and ONOO- as well as traditional reactive oxygen species (ROS) including O2â¢-, H2O2, and â¢OH. In vitro experiments show that neuron cells injured by H2O2 or lipopolysaccharide can be significantly recovered after carbogenic nanozyme treatment via scavenging all kinds of RONS. Moreover, the carbogenic nanozyme can serve as various enzyme mimetics and eliminate the harmful peroxide and glutathione disulfide from injured mice, demonstrating its potential as a therapeutic for acute TBI.