Trehalose is a natural glucose disaccharide identified in the 19th century in fungi and insect cocoons, and later across the three domains of life. In members of the genusMycobacterium, which includes the tuberculosis (TB) pathogen and over 160 species of nontuberculous mycobacteria (NTM), many of which are opportunistic pathogens, trehalose has been an important focus of research over the last 60 years. It is a crucial player in the assembly and architecture of the remarkable mycobacterial cell envelope as an element of unique highly antigenic glycolipids, namely trehalose dimycolate (‘cord factor’). Free trehalose has been detected in the mycobacterial cytoplasm and occasionally in oligosaccharides with unknown function. TB and NTM infection statistics and death toll, the decline in immune responses in the aging population, human immunodeficiency virus/AIDS or other debilitating conditions, and the proliferation of strains with different levels of resistance to the dated drugs in use, all merge into a serious public-health threat urging more effective vaccines, efficient diagnostic tools and new drugs. This review deals with the latest findings on mycobacterial trehalose biosynthesis, catabolism, processing and recycling, as well with the ongoing quest for novel trehalose-related mechanisms to be targeted by novel TB therapeutics. In this context, the drug-discovery pipeline has recently included new lead compounds directed toward trehalose-related targets highlighting the potential of these pathways to stem the tide of rising drug resistance.

Urinary tract infections (UTIs) are among the most common infectious diseases worldwide. This type of infections can be healthcare-associated or community-acquired and affects millions of people every year. Different diagnostic procedures are available to detect pathogens in urine and they can be divided into two main categories: laboratory-based and point-of-care (POC) detection techniques. Traditional methodologies are often time-consuming, thus, achieving a rapid and accurate identification of pathogens is a challenging feature that has been pursued by many research groups and companies operating in this area. The purpose of this review is to compare and highlight advantages and disadvantages of the traditional and currently most used detection methods, as well as the emerging POC approaches and the relevant advances in on-site detection of pathogens´ mechanisms, suitable to be adapted to UTI diagnosis. Lately, the commercially available UTI self-testing kits and devices are helping in the diagnosis of urinary infections as patients or care givers are able to perform the test, easily and comfortably at home and, upon the result, decide when to attend an appointment/Urgent Health Care Unit.

Strains of Thermus thermophilus accumulate primarily trehalose and smaller amounts of mannosylglycerate in response to salt stress in yeast extract-containing media (O. C. Nunes, C. M. Manaia, M. S. da Costa, and H. Santos, Appl. Environ. Microbiol. 61:2351-2357, 1995). A 2.4-kbp DNA fragment from T. thermophilus strain RQ-1 carrying otsA (encoding trehalose-phosphate synthase [TPS]), otsB (encoding trehalose-phosphate phosphatase [TPP]), and a short sequence of the 5′ end of treS (trehalose synthase [TreS]) was cloned from a gene library. The sequences of the three genes (including treS ) were amplified by PCR and sequenced, revealing that the genes were structurally linked. To understand the role of trehalose during salt stress in T. thermophilus RQ-1, we constructed a mutant, designated RQ-1M6, in which TPS ( otsA ) and TPP ( otsB ) genes were disrupted by gene replacement. Mutant RQ-1M6 accumulated trehalose and mannosylglycerate in a medium containing yeast extract and NaCl. However, growth in a defined medium (without yeast extract, known to contain trehalose) containing NaCl led to the accumulation of mannosylglycerate but not trehalose. The deletion of otsA and otsB reduced the ability to grow in defined salt-containing medium, with the maximum salinity being 5% NaCl for RQ-1 and 3% NaCl for RQ-1M6. The lower salt tolerance observed in the mutant was relieved by the addition of trehalose to the growth media. In contrast to trehalose, the addition of glycine betaine, mannosylglycerate, maltose, and glucose to the growth medium did not allow the mutant to grow at higher salinities. The results presented here provide crucial evidence for the importance of the TPS/TPP pathway for the synthesis and accumulation of trehalose and the decisive contribution of this disaccharide to osmotic adaptation in T. thermophilus RQ-1.

Polyurethanes (PUs) are extremely versatile materials used across different industries. Traditionally, they are synthesized by reacting polyols and isocyanates, both of which are petroleum-derived reagents. In response to the demand for more eco-friendly materials, research has increasingly focused on developing new routes for PU synthesis using renewable feedstocks. While substituting isocyanates remains a greater challenge, replacing fossil-based polyols with bio-based alternatives is now a promising strategy. This review explores the main natural sources and their transformations into bio-polyols, the incorporation of bio-fillers into PU formulations, and the production of non-isocyanate polyurethanes (NIPUs). Additionally, the study summarizes the growing body of research that has reported successful outcomes using bio-polyols in PU foams for distinct applications.

Trehalose is the primary organic solute in Rubrobacter xylanophilus under all conditions tested, including those for optimal growth. We detected genes of four different pathways for trehalose synthesis in the genome of this organism, namely, the trehalose-6-phosphate synthase (Tps)/trehalose-6-phosphate phosphatase (Tpp), TreS, TreY/TreZ, and TreT pathways. Moreover, R. xylanophilus is the only known member of the phylum Actinobacteria to harbor TreT. The Tps sequence is typically bacterial, but the Tpp sequence is closely related to eukaryotic counterparts. Both the Tps/Tpp and the TreT pathways were active in vivo, while the TreS and the TreY/TreZ pathways were not active under the growth conditions tested and appear not to contribute to the levels of trehalose observed. The genes from the active pathways were functionally expressed in Escherichia coli , and Tps was found to be highly specific for GDP-glucose, a rare feature among these enzymes. The trehalose-6-phosphate formed was specifically dephosphorylated to trehalose by Tpp. The recombinant TreT synthesized trehalose from different nucleoside diphosphate-glucose donors and glucose, but the activity in R. xylanophilus cell extracts was specific for ADP-glucose. The TreT could also catalyze trehalose hydrolysis in the presence of ADP, but with a very high K _m . Here, we functionally characterize two systems for the synthesis of trehalose in R. xylanophilus , a representative of an ancient lineage of the actinobacteria, and discuss a possible scenario for the exceptional occurrence of treT in this extremophilic bacterium.