What future/s for outdoor and environmental education in a world that has contended with COVID-19?

This is an unusual article in that it brings together the perspectives of many on this journal’s editorial board, around the issue of contending with COVID-19. Twenty statements showcase a range of thoughts and experiences, highlighting the differences and similarities in the way the pandemic is impacting on the educational practice of outdoor and environmental education. The future is not yet written, of course, so it is worth thinking about how the current moment may impact on the months and years to come. The aim of this article is to influence and support such thinking

Direct and indirect transmission of four Salmonella enterica serotypes in pigs

<p>Abstract</p> <p>Background</p> <p>Feed-borne spread of <it>Salmonella </it>spp. to pigs has been documented several times in recent years in Sweden. Experiences from the field suggest that feed-associated serotypes might be less transmittable and subsequently easier to eradicate from pig herds than other serotypes more commonly associated to pigs. Four <it>Salmonella </it>serotypes were selected for experimental studies in pigs in order to study transmissibility and compare possible differences between feed-assoociated (<it>S </it>Cubana and <it>S </it>Yoruba) and pig-associated serotypes (<it>S </it>Derby and <it>S </it>Typhimurium).</p> <p>Methods</p> <p>Direct contact transmission was studied in four groups of pigs formed by six 10-week-old salmonella negative pigs commingled with two fatteners excreting one of the four salmonella serotypes. Indirect transmission was studied by putting six 10-week-old salmonella negative pigs in each of four salmonella contaminated rooms. Each room had previously housed a group of pigs, excreting one of the four selected serotypes.</p> <p>All pigs were monitored for two weeks with respect to the faecal excretion of salmonella and the presence of serum antibodies. At the end of the trial, eight samples from inner tissues and organs were collected from each pig at necropsy.</p> <p>Results</p> <p>In the four direct transmission groups, one pig shed <it>Salmonella </it>(Cubana) at one occasion. At necropsy, <it>S </it>Typhimurium was isolated from one pig.</p> <p>In the indirect transmission groups, two pigs in the Yoruba room and one pig in each of the other rooms were excreting detectable levels of <it>Salmonella </it>once during the study period of two weeks. At necropsy, <it>S </it>Derby was isolated from one of six pigs in the Derby room and <it>S </it>Typhimurium was isolated from four of the six pigs in the Typhimurium room.</p> <p>No significant serological response could be detected in any of the 48 pigs.</p> <p>Conclusions</p> <p>These results show that all four selected serotypes were able to be transmitted in at least one of these field-like trials, but the transmission rate was low in all groups and no obvious differences between feed-associated and pig-associated serotypes in the transmission to naïve pigs and their subsequent faecal shedding were revealed. However, the post mortem results indicated a higher detection of <it>S </it>Typhimurium in the ileocecal lymph nodes of pigs introduced into a contaminated environment in comparison with the other three serotypes.</p

The Vinculin-ΔIn20/21 Mouse: Characteristics of a Constitutive, Actin-Binding Deficient Splice Variant of Vinculin

BACKGROUND: The cytoskeletal adaptor protein vinculin plays a fundamental role in cell contact regulation and affects central aspects of cell motility, which are essential to both embryonal development and tissue homeostasis. Functional regulation of this evolutionarily conserved and ubiquitously expressed protein is dominated by a high-affinity, autoinhibitory head-to-tail interaction that spatially restricts ligand interactions to cell adhesion sites and, furthermore, limits the residency time of vinculin at these sites. To date, no mutants of the vinculin protein have been characterized in animal models. METHODOLOGY/PRINCIPAL FINDINGS: Here, we investigate vinculin-DeltaEx20, a splice variant of the protein lacking the 68 amino acids encoded by exon 20 of the vinculin gene VCL. Vinculin-DeltaEx20 was found to be expressed alongside with wild type protein in a knock-in mouse model with a deletion of introns 20 and 21 (VCL-DeltaIn20/21 allele) and shows defective head-to-tail interaction. Homozygous VCL-DeltaIn20/21 embryos die around embryonal day E12.5 showing cranial neural tube defects and exencephaly. In mouse embryonic fibroblasts and upon ectopic expression, vinculin-DeltaEx20 reveals characteristics of constitutive head binding activity. Interestingly, the impact of vinculin-DeltaEx20 on cell contact induction and stabilization, a hallmark of the vinculin head domain, is only moderate, thus allowing invasion and motility of cells in three-dimensional collagen matrices. Lacking both F-actin interaction sites of the tail, the vinculin-DeltaEx20 variant unveils vinculin's dynamic binding to cell adhesions independent of a cytoskeletal association, and thus differs from head-to-tail binding deficient mutants such as vinculin-T12, in which activated F-actin binding locks the protein variant to cell contact sites. CONCLUSIONS/SIGNIFICANCE: Vinculin-DeltaEx20 is an active variant supporting adhesion site stabilization without an enhanced mechanical coupling. Its presence in a transgenic animal reveals the potential of splice variants in the vinculin gene to alter vinculin function in vivo. Correct control of vinculin is necessary for embryonic development

E-cadherin integrates mechanotransduction and EGFR signaling to control junctional tissue polarization and tight junction positioning

Generation of a barrier in multi-layered epithelia like the epidermis requires restricted positioning of functional tight junctions (TJ) to the most suprabasal viable layer. This positioning necessitates tissue-level polarization of junctions and the cytoskeleton through unknown mechanisms. Using quantitative whole-mount imaging, genetic ablation, and traction force microscopy and atomic force microscopy, we find that ubiquitously localized E-cadherin coordinates tissue polarization of tension-bearing adherens junction (AJ) and F-actin organization to allow formation of an apical TJ network only in the uppermost viable layer. Molecularly, E-cadherin localizes and tunes EGFR activity and junctional tension to inhibit premature TJ complex formation in lower layers while promoting increased tension and TJ stability in the granular layer 2. In conclusion, our data identify an E-cadherin-dependent mechanical circuit that integrates adhesion, contractile forces and biochemical signaling to drive the polarized organization of junctional tension necessary to build an in vivo epithelial barrier