Search

Salt intrusion presents a significant environmental challenge in numerous estuaries around the world, including the Modaomen Estuary in China. This phenomenon typically occurs during the winter season due to reduced freshwater flow. However, an unusual salt intrusion event was observed during the autumn of 2022, coinciding with a typhoon. In this study, we assess the response of the Modaomen to Typhoon Nesat in 2022 and examine the influence of the typhoon on salt intrusion using the Semi-implicit Cross-scale Hydroscience Integrated System Model (SCHISM). The model results reveal that salt intrusion during a typhoon event is primarily driven by the storm surge and landward Ekman transport. Northeasterly winds enhance stratification between saltwater and freshwater in the Modaomen. Moreover, with the typhoon's passage, the Denglongshan Station recorded a peak salinity of 17 psu, with salt intrusion stretching 29 km further. This escalation led to salinity levels surpassing the local drinking water standard of 0.5 psu across all freshwater intake points in Zhuhai City. Numerical experiments indicate that if Typhoon Nesat had occurred during spring tides, the salt intrusion would have been less severe. Furthermore, the study revealed that regulating the upstream runoff could potentially alleviate the effects of typhoon-induced salt intrusion on ensuring a safe water supply. With a runoff increase to 4000 m3/s, the impact of typhoons on Modaomen's drinking water supply can be managed, and at 6000 m3/s, the influence of typhoons on water supply becomes negligible. [ABSTRACT FROM AUTHOR]

The SARS-CoV-2 Omicron variant evades most currently approved neutralizing antibodies (nAbs) and caused drastic decrease of plasma neutralizing activity elicited by vaccination or prior infection, urging the need for the development of pan-variant antivirals. Breakthrough infection induces a hybrid immunological response with potentially broad, potent and durable protection against variants, therefore, convalescent plasma from breakthrough infection may provide a broadened repertoire for identifying elite nAbs. We performed single-cell RNA sequencing (scRNA-seq) and BCR sequencing (scBCR-seq) of B cells from BA.1 breakthrough-infected patients who received 2 or 3 previous doses of inactivated vaccine. Elite nAbs, mainly derived from the IGHV2–5 and IGHV3-66/53 germlines, showed potent neutralizing activity across Wuhan-Hu-1, Delta, Omicron sublineages BA.1 and BA.2 at picomolar NT50 values. Cryo-EM analysis revealed diverse modes of spike recognition and guides the design of cocktail therapy. A single injection of paired antibodies cocktail provided potent protection in the K18-hACE2 transgenic female mouse model of SARS-CoV-2 infection. In this study, the authors isolated and characterized neutralizing antibodies from vaccinated individuals with SARS-CoV-2 BA.1 breakthrough infection and show that elite antibodies derived from specific germlines provide potent pan-variant neutralization capacity and in vivo protection. [ABSTRACT FROM AUTHOR]

The adenosine 5ʹ-triphosphate (ATP)-binding cassette (ABC) transporter, IrtAB, plays a vital role in the replication and viability of Mycobacterium tuberculosis (Mtb), where its function is to import iron-loaded siderophores. Unusually, it adopts the canonical type IV exporter fold. Herein, we report the structure of unliganded Mtb IrtAB and its structure in complex with ATP, ADP, or ATP analogue (AMP-PNP) at resolutions ranging from 2.8 to 3.5 Å. The structure of IrtAB bound ATP-Mg2+ shows a "head-to-tail" dimer of nucleotide-binding domains (NBDs), a closed amphipathic cavity within the transmembrane domains (TMDs), and a metal ion liganded to three histidine residues of IrtA in the cavity. Cryo-electron microscopy (Cryo-EM) structures and ATP hydrolysis assays show that the NBD of IrtA has a higher affinity for nucleotides and increased ATPase activity compared with IrtB. Moreover, the metal ion located in the TM region of IrtA is critical for the stabilization of the conformation of IrtAB during the transport cycle. This study provides a structural basis to explain the ATP-driven conformational changes that occur in IrtAB. [ABSTRACT FROM AUTHOR]

Among various anode materials, SiO x is regarded as the next generation of promising anode due to its advantages of high theoretical capacity with 2680 mA h g -1 , low lithium voltage platform, and rich natural resources. However, the pure SiO x -based materials have slow lithium storage kinetics attributed to their low electron/ion conductive properties and the large volume change during lithiation/delithiation, restricting their practical application. Optimizing the SiO x material structures and the fabricating methods to mitigate these fatal defects and adapt to the market demand for energy density is critical. Hence, SiO x material with TiO 1- x N x phase modification has been prepared by simple, low-cost, and scalable ball milling and then combined with nitridation. Consequently, based on the TiO 1- x N x modified layer, which boosts high ionic/electronic conductivity, chemical stability, and excellent mechanical properties, the SiO x @TON-10 electrode shows highly stable lithium-ion storage performance for lithium-ion half/full batteries due to a stable solid-electrolyte interface layer, fast Li + transport channel, and alleviative volumetric expansion, further verifying its practical feasibility and universal applicability.

The type I adenosine 5'-triphosphate (ATP)-binding cassette (ABC) transporter DppABCD is believed to be responsible for the import of exogenous heme as an iron source into the cytoplasm of the human pathogen Mycobacterium tuberculosis ( Mtb ). Additionally, this system is also known to be involved in the acquisition of tri- or tetra-peptides. Here, we report the cryo-electron microscopy structures of the dual-function Mtb DppABCD transporter in three forms, namely, the apo , substrate-bound, and ATP-bound states. The apo structure reveals an unexpected and previously uncharacterized assembly mode for ABC importers, where the lipoprotein DppA, a cluster C substrate-binding protein (SBP), stands upright on the translocator DppBCD primarily through its hinge region and N-lobe. These structural data, along with biochemical studies, reveal the assembly of DppABCD complex and the detailed mechanism of DppABCD-mediated transport. Together, these findings provide a molecular roadmap for understanding the transport mechanism of a cluster C SBP and its translocator.