Video1_A Superhydrophobic Moso Bamboo Cellulose Nano-Fibril Film Modified by Dopamine Hydrochloride.MP4

The moso bamboo fiber powder was used as raw material to prepare cellulose nano-fibril films, 5% of polyvinyl alcohol solution was used as a structural reinforcement agent, dopamine hydrochloride (DA) was used as a surface adhesive, and hexadecyl trimethoxy silane was used as a surface modifier. The superhydrophobic films were prepared by vacuum filtration and impregnation. The results showed that the water contact angle on the surface of the film could reach 156°. The microstructure and chemical composition of the film surface was further studied by scanning electron microscopy (SEM), Fourier transforms infrared spectroscopy (FTIR), and roughness measurement The scanning electron microscopy images showed that the nanofibers on the surface of Cellulose nanofibers film were arranged and randomly distributed, thus forming a dense network interwoven structure. In PDA hydrophobic modification solution, an Hexadecyltrimethoxysilane was hydrolyzed to a hexadecyl silanol to obtain the polar terminal hydroxyl of Hexadecyl silanol molecule. The -OCH3 terminal group of HDTMS reacted with hydroxyl/H2O to form a silanol (Si-OH) bond and further condensed to form a Si-O-Si network. In addition, due to the hydrophilicity of the surface of the nano cellulose film, a large amount of—OH was adsorbed on the surface of the nano cellulose film, resulted in the chemical connection between cetyl groups, thus realized the grafting of cetyl long-chain alkyl groups onto the fibers of the nano cellulose film.The film showed good self-cleaning and waterproof properties, which can be widely used in wet environment packaging and building.</p

Yang et al_2017_PLoS One_Alldata

Data associated with the glyphosate resistance and EPSPS gene expression of transgenic arabidopsis lines

Naked-Eye Detection of C1–C4 Alcohols Based on Ground-State Intramolecular Proton Transfer

Previous reports of fluorescent sensors for alcohols based on charge-transfer character of their excited state are based on mono-, di-, and tetra-phosphonate cavitands, which are capable of selecting analytes through shape/size selection and various specific H-bonding, CH−π, and cation–dipole interactions. To contrast, color changes based on absorption properties of the ground state are more suitable for direct observation with the naked eye. Three sensitive and selective colorimetric sensors for C1–C4 alcohols have been developed on the basis of alcohol-mediated ground-state intramolecular proton transfer. Reverse proton transfer induced by water achieves a fully reversible reaction. In addition, the solvent color indicates alcohol concentration

Table_1_Advances in the relationship between temporal muscle thickness and prognosis of patients with glioblastoma: a narrative review.docx

The most dangerous variety of glioma, glioblastoma, has a high incidence and fatality rate. The prognosis for patients is still bleak despite numerous improvements in treatment approaches. We urgently need to develop clinical parameters that can evaluate patients' conditions and predict their prognosis. Various parameters are available to assess the patient's preoperative performance status and degree of frailty, but most of these parameters are subjective and therefore subject to interobserver variability. Sarcopenia can be used as an objective metric to measure a patient's physical status because studies have shown that it is linked to a bad prognosis in those with cancers. For the purpose of identifying sarcopenia, temporal muscle thickness has demonstrated to be a reliable alternative for a marker of skeletal muscle content. As a result, patients with glioblastoma may use temporal muscle thickness as a potential marker to correlate with the course and fate of their disease. This narrative review highlights and defines the viability of using temporal muscle thickness as an independent predictor of survival in glioblastoma patients, and it evaluates recent research findings on the association between temporal muscle thickness and prognosis of glioblastoma patients.</p

1,8-Naphthyridine-Derived Ni²⁺/Cu²⁺-Selective Fluorescent Chemosensor with Different Charge Transfer Processses

A highly fluorescent chemosensor based on 1,8-naphthyridine with high sensitivity and selectivity toward Ni²⁺/Cu²⁺ over other cations both in aqueous solution over a wide pH range (4–10) and in cellular environments was developed. Counteranions such as acetate, sulfate, nitrate, and perchlorate have no influence on the detection of such metal ions. Ethylenediamine showed high selectivity toward the in situ-prepared Cu²⁺ complex over the Ni²⁺ complex, which can be applied to distinguish Ni²⁺ and Cu²⁺. The Ni²⁺-induced fluorescence on–off mechanism was revealed to be mediated by intramolecular charge transfer from the metal to the ligand, while that by Cu²⁺ involves intramolecular charge transfer from the ligand to the metal, as confirmed by picosecond time-resolved fluorescence spectroscopy and time-dependent density functional theory calculations

WtsE interacts with two maize PP2A B’ subunit proteins in yeast-two hybrid assays, and the deletion of the yeast PP2A B’ gene alleviates WtsE-induced cell death in yeast.

<p>(A) The N-terminal half of WtsE (WtsE-N’, aa 1–964) interacts with two maize PP2A B’ subunit proteins (WIP1 and WIP2). Interaction by yeast-two hybrid is selected on synthetic drop-out (SD) media lacking leucine, tryptophan, and adenine. EV: empty vector control. Pictures taken at 48 h are representative of three biological replicates. (B) Deletion of yeast <i>RTS1</i> (PP2A B’) allows better growth of yeast cells expressing full-length WtsE. WtsE expression is induced by galactose (2%), and is suppressed by glucose (2%). Pictures, taken at 96 hours after plating of a dilution series, show a representative of three biological replicates.</p

Direct and Indirect Targeting of PP2A by Conserved Bacterial Type-III Effector Proteins

<div><p>Bacterial AvrE-family Type-III effector proteins (T3Es) contribute significantly to the virulence of plant-pathogenic species of <i>Pseudomonas</i>, <i>Pantoea</i>, <i>Ralstonia</i>, <i>Erwinia</i>, <i>Dickeya</i> and <i>Pectobacterium</i>, with hosts ranging from monocots to dicots. However, the mode of action of AvrE-family T3Es remains enigmatic, due in large part to their toxicity when expressed in plant or yeast cells. To search for targets of WtsE, an AvrE-family T3E from the maize pathogen <i>Pantoea stewartii</i> subsp. <i>stewartii</i>, we employed a yeast-two-hybrid screen with non-lethal fragments of WtsE and a synthetic genetic array with full-length WtsE. Together these screens indicate that WtsE targets maize protein phosphatase 2A (PP2A) heterotrimeric enzyme complexes via direct interaction with B’ regulatory subunits. AvrE1, another AvrE-family T3E from <i>Pseudomonas syringae</i> pv. tomato strain DC3000 (<i>Pto</i> DC3000), associates with specific PP2A B’ subunit proteins from its susceptible host Arabidopsis that are homologous to the maize B’ subunits shown to interact with WtsE. Additionally, AvrE1 was observed to associate with the WtsE-interacting maize proteins, indicating that PP2A B’ subunits are likely conserved targets of AvrE-family T3Es. Notably, the ability of AvrE1 to promote bacterial growth and/or suppress callose deposition was compromised in Arabidopsis plants with mutations of PP2A genes. Also, chemical inhibition of PP2A activity blocked the virulence activity of both WtsE and AvrE1 <i>in planta</i>. The function of HopM1, a <i>Pto</i> DC3000 T3E that is functionally redundant to AvrE1, was also impaired in specific PP2A mutant lines, although no direct interaction with B’ subunits was observed. These results indicate that sub-component specific PP2A complexes are targeted by bacterial T3Es, including direct targeting by members of the widely conserved AvrE-family.</p></div

Virulence activities of WtsE in maize seedling leaves are suppressed in a dose dependent manner by cantharidin independent of an effect on WtsE secretion or short-term <i>Pnss</i> growth.

<p>Visual cell death symptoms (A) and electrolyte leakage (B) induced by wild-type, but not the <i>wtsE</i> mutant, <i>Pnss</i> are suppressed by cantharidin. Six-day-old maize seedlings were vacuum infiltrated with 10⁹ CFU/mL of wild-type <i>Pantoea stewartii</i> subsp. <i>stewartii</i> (<i>Pnss</i> WT) or a <i>wtsE</i> mutant strain (<i>Pnss</i> WtsE-) supplemented with 0, 5, 15, or 50 μM cantharidin. Similarly treated samples were subjected to electrolyte leakage analysis (B) or metabolite measurements (C). Values shown in (B) are mean ± SD from three biological replicates and were analyzed by one-way ANOVA followed by Tukey test. Different letters indicate significant differences at P<0.05. (C) The ability of wild-type, but not <i>wtsE</i> mutant, <i>Pnss</i> to induce accumulation of conjugated derivatives of phenolic amino acids is suppressed by cantharidin. Quantities of coumaroyl-tyramine and coumaroyl-tryptamine were measured by LC-MS/MS, normalized to the internal control formononetin and quantified relative to standard curve generated from pure coumaroyl-tyramine or coumaroyl-tryptamine. Values shown are mean ± SD of relative quantities of each compound with 100% representing the amount induced by <i>Pnss</i> WT in the absence of cantharidin. The data is compiled from three biological replicates and was analyzed by one-way ANOVA followed by Tukey test. Different letters indicate significant differences at P<0.05. (D) Cantharidin does not affect production or secretion of WtsE from <i>Pnss</i>. Wild-type <i>Pnss</i> and the type-III secretion system deficient mutant (<i>hrpJ</i>) bacteria were grown in <i>hrp</i>-inducing liquid medium supplemented with 0, 5, 15, or 50 μM cantharidin (CT). Cultures were separated into supernatant (Sup) and cell (Cell) fractions by centrifugation. The WtsE protein (~204 kDa) in each fraction was detected by immunoblotting using an anti-DspA/E antibody. Shown is a representative blot from three biological replicates. (E) Cantharidin treatment does not affect short-term <i>Pnss</i> growth in maize seedlings following high titer infiltration. Six-day-old maize seedlings were vacuum infiltrated with 10⁹ CFU/mL of wild-type <i>Pantoea stewartii</i> subsp. <i>stewartii</i> (<i>Pnss</i> WT) or a <i>wtsE</i> mutant strain (<i>Pnss</i> WtsE-) supplemented with 0 or 50 μM cantharidin (CT). Bacterial growth was assessed immediately following infiltration (0 h), or at 20 hai. Shown are mean ± SD from 3 biological replicates and data were analyzed by one-way ANOVA followed by Tukey test. Different letters indicate significant difference at P<0.01.</p

Specific PP2A B’ subunits are required for virulence activities of AvrE1 and HopM1 in Arabidopsis leaves.

(A) Growth analysis in 5-week-old Arabidopsis plants, including PP2A mutants and complementation lines, at 4 days after infiltration of 105 CFU/ml of Pto DC3000, ΔCEL, ΔCEL+AvrE1, and ΔCEL+HopM1. Values shown are mean ± SEM from four biological replicates for A subunit and b’η, γ, θ, and ζ mutants, from three biological replicates for complementation lines, and from at least six biological replicates for α and β mutants. The inability of NP::α-GFP ln.19-3 and 35S::GFP-α ln. 1–6 to complement T3E-promoted bacterial growth may result from an adverse effect of too high and too low α transcript level, respectively (S8 Fig). Data was analyzed by one-way ANOVA followed by the Tukey test comparing different bacterial strains on individual plant genotypes. Different letters of the same style (eg. A vs B, or A’ vs B’) indicate significant differences at PPto ΔCEL-induced callose deposition by AvrE1 depends on the PP2A B’α subunit. rcn1-6 showed reduced callose deposition in response to ΔCEL infection. Leaves of five-week-old Arabidopsis plants were infiltrated with the indicated bacterial strains (108 CFU/ml) or buffer (10 mM MgCl2), and collected at 16 hai for callose staining. Values shown are mean ± SEM from 3–5 biological replicates with Col-0 included in each individual experiment. ** indicates a significant difference by Student’s t-test at P<0.01.</p

Non-lethal fragments of AvrE1 associate with Arabidopsis PP2A B’ regulatory subunits homologous to the WtsE-interacting proteins, as well as maize WIPs.

<p>(A) Diagram of non-lethal fragments of AvrE1 effector protein. WxxxE motifs and the putative ERMRS motif are indicated by blue lines. (B-C) AvrE1 fragments associate with specific Arabidopsis PP2A B’ subunits following <i>Agro</i>-transient expression in <i>N</i>. <i>benthamiana</i>. GFP-B’α, β, ξ, ι, η, or free GFP were co-expressed with AvrE1-HA fragments in <i>N</i>. <i>benthamiana</i>. Co-immunoprecipitation of GFP-B’α, β, ξ, ι, η, or free GFP was detected using anti-GFP antibody following HA-pull down of AvrE1 fragments (B). Reciprocally, PP2A B’ subunits were pulled-down using anti-GFP antibody and co-immunoprecipitation of AvrE1-HA fragments or HA-RIN4 was detected by immunoblotting with anti-HA antibody (C). Shown are representative blots from three biological replicates. GFP-B’ ξ in (C) was tested separately from the rest of the panel. (D) AvrE1 fragments associate with maize WIPs. Arabidopsis GFP-B’β, maize GFP-WIP1, GFP-WIP2, or free GFP were co-expressed with AvrE1-HA fragments in <i>N</i>. <i>benthamiana</i>. PP2A B’ subunits from Arabidopsis and maize were pulled down using anti-GFP antibody and co-immunoprecipitation of AvrE1-HA fragments was detected by immunoblotting with anti-HA antibody. Shown is a blot representative of three biological replicates, Arabidopsis GFP-B’β was included in two replicates. Arrows indicate predicted sizes of the GFP-PP2A B’ full-length constructs.</p