Trifolium repens L.-Like Periodic Micronano Structured Superhydrophobic Surface with Ultralow Ice Adhesion for Efficient Anti-Icing/Deicing.

Wind turbine blades are often covered with ice and snow, which inevitably reduces their power generation efficiency and lifetime. Recently, a superhydrophobic surface has attracted widespread attention due to its potential values in anti-icing/deicing. However, the superhydrophobic surface can easily transition from Cassie-Baxter to Wenzel at low temperature, limiting its wide applications. Herein, inspired by the excellent water resistance and cold tolerance of Trifolium repens L. endowed by its micronano structure and low surface energy, a fresh structure was prepared by combining femtosecond laser processing technology and a boiling water treatment method. The prepared icephobic surface aluminum alloy (ISAl) mainly consists of a periodic microcrater array, nonuniform microclusters, and irregular nanosheets. This three-scale structure greatly promotes the stability of the Cassie-Baxter state. The critical Laplace pressure of ISAl is up to 1437 Pa, and the apparent water contact angle (CA) is higher than 150° at 0 °C. Those two factors contribute to its excellent anti-icing and deicing performances. The results show that the static icing delay time reaches 2577 s, and the ice adhesion strength is only 1.60 kPa. Furthermore, the anti-icing and deicing abilities of the proposed ISAl were examined under the environment of low temperature and high relative humidity to demonstrate its effectiveness. The dynamic anti-icing time of ISAl in extreme environments is up to 5 h, and ice can quickly fall with a speed of 34 r/min when it is in a horizontal rotational motion. Finally, ISAl has excellent reusability and mechanical durability, with the ice adhesion strength still being less than 6 kPa and the CA greater than 150° after 15 cycles of icing-deicing tests. The proposed structure would offer a promising strategy for the efficient anti-icing and deicing of wind turbine blades.

An efficient metal-free desulfurization strategy promoted by Togni-II reagent.

Desulfurization is a versatile synthetic tool in organic synthesis, particularly in peptide chemistry, where it offers an effective conversion strategy for compounds that contain mercaptan groups. In this study, we present a metal-free desulfurization method for amino acids and peptides using a Togni-II reagent as a radical initiator. Our method showed excellent efficiency and extensive substrate tolerance, circumventing the formation of radical adducts caused by VA-044. The obtained results further expand the applicability of Togni-II reagent as a key promotor in radical-based reactions.

Colletotrichum gloeosporioides Cg2LysM contributed to virulence toward rubber tree through affecting invasive structure and inhibiting chitin-triggered plant immunity.

Fungal chitin, as a typical microorganism-associated molecular pattern (PAMP), was recognized by plant LysM-containing protein to induce immunity called pattern-triggered immunity (PTI). To successfully infect host plant, fungal pathogens secreted LysM-containing effectors to inhibit chitin-induced plant immunity. Filamentous fungus Colletotrichum gloeosporioides caused rubber tree anthracnose which resulted in serious loss of natural rubber production worldwide. However, little is known about the pathogenesis mediated by LysM effector of C. gloeosporioide. In this study, we identified a two LysM-containing effector in C. gloeosporioide and named as Cg2LysM. Cg2LysM was involved not only in conidiation, appressorium formation, invasion growth and the virulence to rubber tree, but also in melanin synthesis of C. gloeosporioides. Moreover, Cg2LysM showed chitin-binding activity and suppression of chitin-triggered immunity of rubber tree such as ROS production and the expression of defense relative genes HbPR1, HbPR5, HbNPR1 and HbPAD4. This work suggested that Cg2LysM effector facilitate infection of C. gloeosporioides to rubber tree through affecting invasive structure and inhibiting chitin-triggered plant immunity.

Molecular characterization and expression analysis of pitaya (Hylocereus polyrhizus) HpLRR genes in response to Neoscytalidium dimidiatum infection.

BACKGROUND: Canker disease caused by Neoscytalidium dimidiatum is a devastating disease resulting in a major loss to the pitaya industry. However, resistance proteins in plants play crucial roles to against pathogen infection. Among resistance proteins, the leucine-rich repeat (LRR) protein is a major family that plays crucial roles in plant growth, development, and biotic and abiotic stress responses, especially in disease defense. RESULTS: In the present study, a transcriptomics analysis identified a total of 272 LRR genes, 233 of which had coding sequences (CDSs), in the plant pitaya (Hylocereus polyrhizus) in response to fungal Neoscytalidium dimidiatum infection. These genes were divided into various subgroups based on specific domains and phylogenetic analysis. Molecular characterization, functional annotation of proteins, and an expression analysis of the LRR genes were conducted. Additionally, four LRR genes (CL445.Contig4_All, Unigene28_All, CL28.Contig2_All, and Unigene2712_All, which were selected because they had the four longest CDSs were further assessed using quantitative reverse transcription PCR (qRT-PCR) at different fungal infection stages in different pitaya species (Hylocereus polyrhizus and Hylocereus undatus), in different pitaya tissues, and after treatment with salicylic acid (SA), methyl jasmonate (MeJA), and abscisic acid (ABA) hormones. The associated protein functions and roles in signaling pathways were identified. CONCLUSIONS: This study provides a comprehensive overview of the HpLRR family genes at transcriptional level in pitaya in response to N. dimidiatum infection, it will be helpful to understand the molecular mechanism of pitaya canker disease, and lay a strong foundation for further research.

MEC-2 and MEC-6 in the Caenorhabditis elegans sensory mechanotransduction complex: auxiliary subunits that enable channel activity.

The ion channel formed by the homologous proteins MEC-4 and MEC-10 forms the core of a sensory mechanotransduction channel in Caenorhabditis elegans. Although the products of other mec genes are key players in the biophysics of transduction, the mechanism by which they contribute to the properties of the channel is unknown. Here, we investigate the role of two auxiliary channel subunits, MEC-2 (stomatin-like) and MEC-6 (paraoxonase-like), by coexpressing them with constitutively active MEC-4/MEC-10 heteromeric channels in Xenopus oocytes. This work extends prior work demonstrating that MEC-2 and MEC-6 synergistically increase macroscopic current. We use single-channel recordings and biochemistry to show that these auxiliary subunits alter function by increasing the number of channels in an active state rather than by dramatically affecting either single-channel properties or surface expression. We also use two-electrode voltage clamp and outside-out macropatch recording to examine the effects of divalent cations and proteases, known regulators of channel family members. Finally, we examine the role of cholesterol binding in the mechanism of MEC-2 action by measuring whole-cell and single-channel currents in MEC-2 mutants deficient in cholesterol binding. We suggest that MEC-2 and MEC-6 play essential roles in modulating both the local membrane environment of MEC-4/MEC-10 channels and the availability of such channels to be gated by force in vivo.

Gain-of-function mutations in the MEC-4 DEG/ENaC sensory mechanotransduction channel alter gating and drug blockade.

MEC-4 and MEC-10 are the pore-forming subunits of the sensory mechanotransduction complex that mediates touch sensation in Caenorhabditis elegans (O'Hagan, R., M. Chalfie, and M.B. Goodman. 2005. Nat. Neurosci. 8:43-50). They are members of a large family of ion channel proteins, collectively termed DEG/ENaCs, which are expressed in epithelial cells and neurons. In Xenopus oocytes, MEC-4 can assemble into homomeric channels and coassemble with MEC-10 into heteromeric channels (Goodman, M.B., G.G. Ernstrom, D.S. Chelur, R. O'Hagan, C.A. Yao, and M. Chalfie. 2002. Nature. 415:1039-1042). To gain insight into the structure-function principles that govern gating and drug block, we analyzed the effect of gain-of-function mutations using a combination of two-electrode voltage clamp, single-channel recording, and outside-out macropatches. We found that mutation of A713, the d or degeneration position, to residues larger than cysteine increased macroscopic current, open probability, and open times in homomeric channels, suggesting that bulky residues at this position stabilize open states. Wild-type MEC-10 partially suppressed the effect of such mutations on macroscopic current, suggesting that subunit-subunit interactions regulate open probability. Additional support for this idea is derived from an analysis of macroscopic currents carried by single-mutant and double-mutant heteromeric channels. We also examined blockade by the diuretic amiloride and two related compounds. We found that mutation of A713 to threonine, glycine, or aspartate decreased the affinity of homomeric channels for amiloride. Unlike the increase in open probability, this effect was not related to size of the amino acid side chain, indicating that mutation at this site alters antagonist binding by an independent mechanism. Finally, we present evidence that amiloride block is diffusion limited in DEG/ENaC channels, suggesting that variations in amiloride affinity result from variations in binding energy as opposed to accessibility. We conclude that the d position is part of a key region in the channel functionally and structurally, possibly representing the beginning of a pore-forming domain.