We report here a novel and simple method, without using any seeds or catalysts, to synthesize single-crystal germanium nanowires with tunable 10−115 nm diameters and of 10−20 μm length by the decomposition of a precursor [(CH3(CH2)7CHCH(CH2)7CH2NH2)4Ge]4+·(Cl-)4 (TOG) at 360 °C in trioctylamine. The diameter of Ge nanowires can be controlled by varying the concentration of TOG in solution.

Essential to bacterial pathogenesis, Salmonella enterica serovar Typhimurium (S. Typhimurium) has evolved the capacity to quickly sense and adapt to specific intracellular environment within distinct host cells. Here we examined S. Typhimurium proteomic remodeling within macrophages, allowing direct comparison with our previous studies in epithelial cells. In addition to many shared features, our data revealed proteomic signatures highly specific to one type of host cells. Notably, intracellular S. Typhimurium differentially regulates the two type III secretion systems (T3SSs) far more quickly in macrophages than in epithelial cells; bacterial flagellar and chemotaxis systems degenerate more quickly in macrophages than in HeLa cells as well. Importantly, our comparative analysis uncovered high levels of induction of bacterial histidine biosynthesis in macrophages but not in epithelial cells. Targeted metabolomic measurements revealed markedly lower histidine levels within macrophages. Intriguingly, further functional studies established that histidine biosynthesis that is defective (due to a hisG mutation) renders the bacterium (strain SL1344) hypersensitive to intracellular shortage of this amino acid. Indeed, another S. Typhimurium strain, namely, strain 14028s, with a fully functional biosynthetic pathway exhibited only minor induction of the his operon within infected macrophages. Our work thus provided novel insights into S. Typhimurium adaptation mechanisms within distinct host cells and also provided an elegant paradigm where proteomic profiling of intracellular pathogens is utilized to discriminate specific host environments (e.g., on the basis of nutrient availability). IMPORTANCE Salmonella Typhimurium is one of the leading causes of foodborne bacterial infection. Nevertheless, how Salmonella adapts to distinct types of host cells during infection remains poorly understood. By contrasting intracellular Salmonella proteomes from both infected macrophages and epithelial cells, we found striking proteomic signatures specific to particular types of host cells. Notably, Salmonella proteomic remodeling exhibited quicker kinetics in macrophages than in epithelial cells with respect to bacterial virulence and flagellar and chemotaxis systems. Furthermore, we unveiled high levels of induction of bacterial histidine biosynthesis in macrophages but not in epithelial cells, which is attributable to differing intracellular levels of this amino acid. Intriguingly, we found that a defective hisG gene renders a Salmonella strain hypersensitive to histidine shortage in macrophages. Overall, our work reveals specific Salmonella adaptation mechanisms in distinct host cells, which should aid in the development of novel anti-infection strategies.

Proton-coupled electron transfer (PCET) reactions at various interfaces (liquid/membrane, solid/electrolyte, liquid/liquid) lie at the heart of many processes in biology and chemistry. Mechanistic study can provide profound understanding of PCET and rational design of new systems. However, most mechanisms of PCET reactions at a liquid/liquid interface have been proposed based on electrochemical and spectroscopic data, which lack direct evidence for possible intermediates. Moreover, a liquid/liquid interface as one type of soft interface is dynamic, making the investigation of interfacial reactions very challenging. Herein a novel electrochemistry method coupled to mass spectrometry (EC-MS) was introduced for in situ study of the oxygen reduction reaction (ORR) by ferrocene (Fc) under catalysis from cobalt tetraphenylporphine (CoTPP) at liquid/liquid interfaces. The key units are two types of gel hybrid ultramicroelectrodes (agar-gel/organic hybrid ultramicroelectrodes and water/PVC-gel hybrid ultramicroelectrodes), which were made based on dual micro- or nanopipettes. A solidified liquid/liquid interface can be formed at the tip of these pipettes, and it serves as both an electrochemical cell and a nanospray emitter for mass spectrometry. We demonstrated that the solidified L/L interfaces were very similar to typical L/L interfaces. Key CoTPP intermediates of the ORR at the liquid/liquid interfaces were identified for the first time, and the four-electron oxygen reduction pathway predominated, which provides valuable insights into the mechanism of the ORR. Theoretical simulation has further supported the possibility of formation of intermediates. This type of platform is promising for in situ tracking and identifying intermediates to study complicated reactions at liquid/liquid interfaces or other soft interfaces.

Salmonella enterica serovar Typhimurium (S. Typhimurium), an important foodborne pathogen, often encounters phosphate (Pi) shortage both in the environment and inside host cells. To gain a global view on its physiological responses to Pi starvation, we performed proteomic profiling of S. Typhimurium upon the shift from Pi-rich to Pi-low conditions. In addition to the Pho regulon, many metabolic processes were up-regulated, such as glycolysis, pentose phosphate pathway, pyrimidine degradation, glycogen, and trehalose metabolism, allowing us to chart an overview of S. Typhimurium carbon metabolism under Pi starvation. Furthermore, proteomic analysis of a mutant lacking phoB (that encodes a key regulator of Pi shortage response) suggested that only a small subset of the altered proteins upon Pi limitation was PhoB-dependent. Importantly, we present evidence that S. Typhimurium N-acetylglucosamine catabolism was induced under Pi-limiting conditions in a PhoB-dependent manner. Immunoblotting and β-galactosidase assays demonstrated that PhoB was required for the full activation of NagB, a key enzyme of this pathway, in response to low Pi. Thus, our study reveals that N-acetylglucosamine catabolism may represent an additional PhoB-regulated pathway to tackle bacterial Pi shortage.