益生菌联合乌司他丁对脓毒症休克患者肠道菌群和胃肠功能及免疫功能的影响

探讨益生菌联合乌司他丁应用于脓毒症休克患者的效果,为该类患者的治疗提供参考。

回顾性选取2021年7月至2023年7月我院收治的80例脓毒症休克患者,按治疗方案不同划分组别。入选患者均给予常规基础治疗,其中单一组（38例）患者采用乌司他丁治疗,联合组（42例）患者采用益生菌联合乌司他丁进行治疗。对比两组患者疗效及各指标水平。

联合组患者治疗后SOFA、APACHE Ⅱ评分[（5.08±1.07）分、（12.75±2.48）分]均低于单一组[（7.16±1.54）分、（15.66±3.23）分]（t=7.707、4.544,均P＜0.05）。治疗后,联合组患者肠道乳杆菌与双歧杆菌数量[（5.91±1.02）lg CFU/g、（6.72±1.23）lg CFU/g]高于单一组[（5.24±0.85）lg CFU/g、（5.82±1.06）lg CFU/g],葡萄球菌数量[（3.77±0.32）lg CFU/g]低于单一组[（4.28±0.43）lg CFU/g]（t=3.173、6.055、3.488,均P＜0.05）。联合组患者治疗后GAS、MOT、IgA、IgG、IgM水平[（67.56±24.82）pg/mL、（408.52±118.47）pg/mL、（2.61±0.43）g/L、（12.24±1.36）g/L、（1.52±0.25）g/L]均优于单一组[（94.30±30.88）pg/mL、（326.39±107.76）pg/mL、（2.18±0.37）g/L、（10.45±1.13）g/L、（1.14±0.22）g/L]（t=4.287、3.232、4.770、6.365、7.184,均P＜0.05）。

益生菌联合乌司他丁对于脓毒症休克患者的治疗效果良好,可纠正肠道菌群失调,提升胃肠功能与免疫功能,促进预后改善。

     

Association between sheath blight resistance and chitinase activity in transgenic rice plants expressing McCHIT1 from bitter melon

No usable resources with high-level resistance to sheath blight (SB) have yet been found in rice germplasm resources worldwide. Therefore, creating and breeding new disease-resistant rice resources with sheath blight resistance (SBR) are imperative. In this study, we inoculated rice plants with hyphae of the highly pathogenic strain RH-9 of rice SB fungus Rhizoctonia solani to obtain eight stable transgenic rice lines harbouring the chitinase gene (McCHIT1) of bitter melon with good SBR in the T₅ generation. The mean disease index for SB of wild-type plants was 92% and 37–44% in transgenic lines. From 24 h before until 120 h after inoculation with R. solani, chitinase activity in stable transgenic plants with increased SBR was 2.0–5.5 and 1.8–2.7 times that of wild-type plants and plants of a disease-susceptible stable transgenic line, respectively. The correlation between SBR and chitinase activity in McCHIT1-transgenic rice line plants was significant. This work stresses how McCHIT1 from bitter melon can be used to protect rice plants from SB infection.

     

Integrin α1 Has a Long Helix,Extending from the Transmembrane Region to the Cytoplasmic Tail in Detergent Micelles

Integrin proteins are very important adhesion receptors that mediate cell-cell and cell-extracellular matrix interactions. They play essential roles in cell signaling and the regulation of cellular shape, motility, and the cell cycle. Here, the transmembrane and cytoplasmic (TMC) domains of integrin α1 and β1 were over-expressed and purified in detergent micelles. The structure and backbone relaxations of α1-TMC in LDAO micelles were determined and analyzed using solution NMR. A long helix, extending from the transmembrane region to the cytoplasmic tail, was observed in α1-TMC. Structural comparisons of α1-TMC with reported αIIb-TMC domains indicated different conformations in the transmembrane regions and cytoplasmic tails. An NMR titration experiment indicated weak interactions between α1-TMC and β1-TMC through several α1-TMC residues located at its N-terminal juxta-transmembrane region and C-terminal extended helix region.     

Structural studies of Mycobacterium tuberculosis Rv0899 reveal a monomeric membrane-anchoring protein with two separate domains

Rv0899 from Mycobacterium tuberculosis belongs to the OmpA (outer membrane protein A) family of outer membrane proteins. It functions as a pore-forming protein; the deletion of this gene impairs the uptake of some water-soluble substances, such as serine, glucose, and glycerol. Rv0899 has also been shown to play a part in low-pH environment adaption, which may play a part in pathogenic mycobacteria overcoming the host's defense mechanisms. Based on many bacterial physiological data and recent structural studies, it was proposed that Rv0899 forms an oligomeric channel to carry out such functions. In this work, biochemical and structural data obtained from solution NMR and EPR spectroscopy indicated that Rv0899 is a monomeric membrane-anchoring protein with two separate domains, rather than an oligomeric pore. Using NMR chemical shift perturbation and isothermal calorimetric titration assays, we show that Rv0899 was able to interact with Zn(2+) ions, which may indicate a role for Rv0899 in the process of Zn(2+) acquisition.     

Metal-ion interactions with sugars. Crystal structures and FT-IR studies of the LaCl3-ribopyranose and CeCl3-ribopyranose complexes

Single crystals of LaCl3.C5H10O5.5H2O (1) and CeCl3.C5H10O5.5H2O (2) were obtained from ethanol-water solutions and their structures determined by X-ray. The two complexes are isomorphous. Two configurations of complex 1 or complex 2, as a pair of isomers, were found in each single crystal in a disordered state. The ligand of one of the isomer is alpha-D-ribopyranose in the 4C1 conformation, the ligand of the other is beta-D-ribopyranose in the 1C4 conformation. For complex 1, the alpha:beta anomeric ratio is 51:49, and for complex 2, the ratio is 52:48. Both ligands of the two isomers provide three hydroxyl groups in ax-eq-ax orientation for coordination. The Ln3+ (Ln = La or Ce) ion is nine-coordinated with five Ln-O bonds from water molecules, three Ln-O bonds from hydroxyl groups of the D-ribopyranose, and one Ln-Cl bond from chloride ion. The hydroxyl groups, water molecules, and chloride ions form an extensive hydrogen-bond network. The IR spectral C-C, O-H, C-O, and C-O-H vibrations were observed to be shifted in both the two complexes and the IR results are in accord with those of X-ray diffraction.