Ultrawide and unidirectional enhancements of a photonic spin Hall effect in a tilted uniaxial crystal.

Since the enhancement of the photonic spin Hall effect (PSHE) is limited around the Brewster's angle, the scientific problem of how to extend the range of incident angles and to keep them unidirectional for the enhanced PSHE remains open. Here, we propose an effective method to achieve the ultrawide angle and unidirectional enhancement of PSHE via the omnidirectional Brewster's effect in a tilted uniaxial crystal. By properly setting the permittivity and the optical axial angle of the uniaxial crystal, the omnidirectional Brewster's effect can be obtained to realize an ultrawide angle enhancement of the PSHE. Then, by appropriately deviating the optical axial angle, the ultrawide enhancement of the PSHE can be achieved within the maximum incident angle range of 60° with unchanged direction. These findings inspire an unprecedented route to facilitate the applications in precision measurement and spin-dependent devices.

Thickness-dependent in-plane shift of photonic spin Hall effect in an anisotropic medium.

As the in-plane spin splitting (IPSS) has a broad application for the precision measurement and sensing, it is extremely important to explore its enhancement mechanism via the photonic spin Hall effect (PSHE). However, for a multilayer structure, the thickness in most of previous works is generally set as a fixed value, lacking the deeply exploration of the influence of thickness on the IPSS. By contrast, here we demonstrate the comprehensive understanding of thickness-dependent IPSS in a three layered anisotropic structure. As thickness increases, near the Brewster angle, the enhanced in-plane shift exhibits a thickness-dependently periodical modulation, besides with much wider incident angle than that in an isotropic medium. While near the critical angle, it becomes thickness-dependently periodical or linear modulation under different dielectric tensors of the anisotropic medium, no longer keeps almost constant in an isotropic medium. In addition, as exploring the asymmetric in-plane shift with arbitrary linear polarization incidence, the anisotropic medium could bring more obvious and wider range of thickness-dependently periodical asymmetric splitting. Our results deepen the understanding of enhanced IPSS, which is expected to promise a pathway in an anisotropic medium for the spin control and integrated device based on PSHE.

Elimination of plasma soluble antigen in cynomolgus monkeys by combining pH-dependent antigen binding and novel Fc engineering.

A conventional antibody targeting a soluble antigen in circulation typically requires a huge dosage and frequent intravenous administration to neutralize the antigen. This is because antigen degradation is reduced by the formation of antigen-antibody immune complexes, which escape from lysosomal degradation using neonatal Fc receptor (FcRn)-mediated recycling. To address this, we developed an antigen-sweeping antibody that combines pH-dependent antigen binding and Fc engineering to enhance Fc receptor binding. The sweeping antibody actively eliminates the plasma antigens by increasing the cellular uptake of the immune complex and dissociating the antigens in the acidic endosome for degradation. Strong antigen sweeping can reduce the dosage, potentially achieve higher efficacy, and expand the scope of antigen space available for targeting by antibodies. In this study, to further improve the sweeping efficacy, we developed a novel antibody Fc variant by enhancing Fcγ receptor IIb (FcγRIIb) binding and modulating charge characteristics for increased cellular uptake of the immune complex, together with enhancing FcRn binding for efficient salvage of the antigen-free antibodies. Our Fc variant achieved strong antigen sweeping in cynomolgus monkeys with antibody pharmacokinetics comparable to a wild-type human IgG1 antibody. The positive-charge substitutions enhanced uptake of the immune complex by FcγRIIb-expressing cells in vitro, which was completely inhibited by an anti-FcγRIIb antibody. This suggests that the strong in vivo sweeping efficacy improved by the charge engineering is more likely achieved by FcγRIIb-dependent uptake of the immune complex rather than nonspecific uptake. We expect this novel Fc engineering can maximize the antigen sweeping efficacy even in humans and create novel therapeutic antibodies that meet unmet medical needs for patients.

Products distribution and hazardous elements migration during pyrolysis of oily sludge from the oil refining process.

Oily sludge is a hazardous waste due to the enrichment of nitrogen, sulfur, PAHs, and heavy metals. In this work, an oily sludge from oil refining factory was pyrolyzed at various temperatures of 250-850 °C in a fixed bed reactor focusing on product distribution and migration of hazardous compounds of PAHs, sulfur, nitrogen-containing compounds, and heavy metals. The mechanism of PAHs formation and migration of nitrogen, sulfur, heavy metals were elucidated by comprehensive analysis of the solid, liquid, and gas products. The distribution and risk analysis of heavy metals were also conducted. The pyrolytic products distribution was markedly affected by pyrolysis temperatures. A maximum oil yield was observed at 500 °C, which can further crack into gas due to secondary reaction. The pyrolytic gas was enriched in the order of CO2 > CO > CH4 > H2. At lower temperatures, CO2 was largely generated due to the elimination of oxygen-containing functional groups, while H2 was mainly formed above 450 °C due to the recombination reaction. Higher temperatures promoted more N-/S-containing compounds into tar and gas phases. The N-/S-containing compounds mainly included NH3, HCN, H2S, SO2, COS in the gas phase and amines, indoles, pyridines, nitriles, thiophenes in liquid phase. PAHs with 2-ring to 5-ring were mainly generated due to the secondary reaction at higher temperatures. Moreover, Pyrolysis caused the accumulation of heavy metals in chars. Cd presented a high potential risk while the other heavy metals in chars presented a low risk.

Butyrophilin 3A1 binds phosphorylated antigens and stimulates human γδ T cells.

Human T cells that express a T cell antigen receptor (TCR) containing γ-chain variable region 9 and δ-chain variable region 2 (Vγ9Vδ2) recognize phosphorylated prenyl metabolites as antigens in the presence of antigen-presenting cells but independently of major histocompatibility complex (MHC), the MHC class I-related molecule MR1 and antigen-presenting CD1 molecules. Here we used genetic approaches to identify the molecule that binds and presents phosphorylated antigens. We found that the butyrophilin BTN3A1 bound phosphorylated antigens with low affinity, at a stoichiometry of 1:1, and stimulated mouse T cells with transgenic expression of a human Vγ9Vδ2 TCR. The structures of the BTN3A1 distal domain in complex with host- or microbe-derived phosphorylated antigens had an immunoglobulin-like fold in which the antigens bound in a shallow pocket. Soluble Vγ9Vδ2 TCR interacted specifically with BTN3A1-antigen complexes. Accordingly, BTN3A1 represents an antigen-presenting molecule required for the activation of Vγ9Vδ2 T cells.