University of Basel

About: University of Basel is a education organization based out in Basel, Basel-Stadt, Switzerland. It is known for research contribution in the topics: Population & Transplantation. The organization has 25084 authors who have published 52975 publications receiving 2388002 citations. The organization is also known as: Universität Basel & Basel University.

A new antibiotic selectively kills Gram-negative pathogens

Abstract: The current need for novel antibiotics is especially acute for drug-resistant Gram-negative pathogens1,2. These microorganisms have a highly restrictive permeability barrier, which limits the penetration of most compounds3,4. As a result, the last class of antibiotics that acted against Gram-negative bacteria was developed in the 1960s2. We reason that useful compounds can be found in bacteria that share similar requirements for antibiotics with humans, and focus on Photorhabdus symbionts of entomopathogenic nematode microbiomes. Here we report a new antibiotic that we name darobactin, which was obtained using a screen of Photorhabdus isolates. Darobactin is coded by a silent operon with little production under laboratory conditions, and is ribosomally synthesized. Darobactin has an unusual structure with two fused rings that form post-translationally. The compound is active against important Gram-negative pathogens both in vitro and in animal models of infection. Mutants that are resistant to darobactin map to BamA, an essential chaperone and translocator that folds outer membrane proteins. Our study suggests that bacterial symbionts of animals contain antibiotics that are particularly suitable for development into therapeutics.

Infra‐red thermometry of alpine landscapes challenges climatic warming projections

Abstract: Rough mountain terrain offers climatic conditions (niches) to plants and animals poorly represented by conventional climate station data. However, the extent to which actual temperatures deviate from those of the freely circulating atmosphere had never been assessed at a landscape level. Here, we quantify thermal life conditions across topographically rich mountain terrain by using a combination of thermal (IR) imagery of surface temperature with data from a large number of miniature data loggers buried at 3 cm soil depth. The data obtained from six alpine (Alps) and arctic-alpine slopes (Norway, Sweden, Svalbard) evidence persistent root zone temperatures of 2-4 K above air temperature during summer. Surface temperatures show strong positive (2-9 K) and negative (3-8 K) deviations from air temperature on bright days and clear nights, respectively. As to be expected, south oriented slopes are warmer than west and north slopes but microclimatic variation on clear sky days was strong within all slopes, with 8.4 ± 2.5 K (mean ± SD) surface temperature differences persisting over several hours per day along horizontal (i.e., equal elevation) transects. Life conditions of alpine organisms are thus strongly decoupled from conditions in the free atmosphere and cannot reliably be inferred from climate station data in both, temperate and arctic latitudes. Microtopography can mimic temperature differences of large elevational (or latitudinal) gradients over very short horizontal distances. This is important in the context of climate change because it shows that species do not necessarily need to climb several hundred meters in elevation to escape the warmth. Quite often, few meters of horizontal shift will do. For plants unable to, or too slow to adapt to a warmer climate, thermal microhabitat mosaics offer both refuge habitats as well as stepping stones as atmospheric temperatures rise.

X-ray structure of the mouse serotonin 5-HT3 receptor

Abstract: Neurotransmitter-gated ion channels of the Cys-loop receptor family mediate fast neurotransmission throughout the nervous system. The molecular processes of neurotransmitter binding, subsequent opening of the ion channel and ion permeation remain poorly understood. Here we present the X-ray structure of a mammalian Cys-loop receptor, the mouse serotonin 5-HT3 receptor, at 3.5 A resolution. The structure of the proteolysed receptor, made up of two fragments and comprising part of the intracellular domain, was determined in complex with stabilizing nanobodies. The extracellular domain reveals the detailed anatomy of the neurotransmitter binding site capped by a nanobody. The membrane domain delimits an aqueous pore with a 4.6 A constriction. In the intracellular domain, a bundle of five intracellular helices creates a closed vestibule where lateral portals are obstructed by loops. This 5-HT3 receptor structure, revealing part of the intracellular domain, expands the structural basis for understanding the operating mechanism of mammalian Cys-loop receptors.