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• Schools´ environments as enablers for sustainable urban transformation. • Climate action educational programs promote QHIM encouragement and behavioral change. • An analytical framework to identify critical points for social innovation projects. • Practical strategies for scaling climate action education programmes. • Extension of the collective efficacy to the whole social innovation process. Schools and their environment have the potential to be an enabler for urban transformation. These spaces constitute delimited social and physical contexts where different stakeholders and levers of change interact to face local and global challenges such as climate change. In this way, climate action educational programs (CAEPs) are presented as a tool for multi-stakeholder work, which enables the promotion of collective efficacy to catalyze transformations and behavioral changes. Through the case study of Ecology at your Doorstep project (EayD), this research seeks to analyze practical strategies to counteract the challenges of the sustainability of CAEPs. This analysis is based on the Quintuple Helix Innovation Model (QHIM), the principles of collective efficacy for behavioral change, and the social innovation process. The methodology includes interviews with key stakeholders representing the five helices, as well as surveys to students and teachers involved. The main contributions are: a new analytical framework to identify critical points with the potential to be replicated in other CAEPs and social innovation initiatives; the extension of the principles of collective efficacy to the whole social innovation process and the ecosystem of actors; and practical considerations when scaling CAEPs in urban contexts. [ABSTRACT FROM AUTHOR]

• Educational innovation emerges as a strategic pillar of governance for world-class universities. • Universities with more mature educational innovation governance rank higher in the Webometrics ranking. • There is an international tendency to base work on educational innovation projects. • The EI projects contribute to strategic changes that enhance the role of the university. There is a growing interest in educational innovation in universities at a global level, as a tool designed to create strategic changes in order to improve quality. This study evaluates the global improvement in universities as a result of educational innovation governance, as a pillar of the so-called world-class research universities and as a tool for continuous improvement in higher education. The methodology has been designed by different educational innovation groups from the Universidad Politécnica de Madrid, Universidad de Cádiz, and the International Project Management Association Spanish Board, and includes an analysis of 67 universities from 20 countries. The study is based on 32 universities in Spain, as well as 35 other international universities that carry out educational innovation activity. The results show that universities that have a more mature educational innovation governance in place, both in Spain as well as in other countries, are higher in the ranking of universities (Webometrics). These universities demonstrate a tendency to work on educational innovation projects, which are contributing to strategic changes that will permanently revitalise teaching, whilst also improving research and its links to society. [ABSTRACT FROM AUTHOR]

The core lipopolysaccharides (LPS) of Proteus mirabilis as well as those of Klebsiella pneumoniae and Serratia marcescens are characterized by the presence of a hexosamine-galacturonic acid disaccharide (αHexN-(1,4)-αGalA) attached by an α1,3 linkage to l-glycero-d-manno-heptopyranose II (l-glycero-α-d-manno-heptosepyranose II). In K. pneumoniae, S. marcescens, and some P. mirabilis strains, HexN is d-glucosamine, whereas in other P. mirabilis strains, it corresponds to d-galactosamine. Previously, we have shown that two enzymes are required for the incorporation of d-glucosamine into the core LPS of K. pneumoniae; the WabH enzyme catalyzes the incorporation of GlcNAc from UDP-GlcNAc to outer core LPS, and WabN catalyzes the deacetylation of the incorporated GlcNAc. Here we report the presence of two different HexNAc transferases depending on the nature of the HexN in P. mirabilis core LPS. In vivo and in vitro assays using LPS truncated at the level of galacturonic acid as acceptor show that these two enzymes differ in their specificity for the transfer of GlcNAc or GalNAc. By contrast, only one WabN homologue was found in the studied P. mirabilis strains. Similar assays suggest that the P. mirabilis WabN homologue is able to deacetylate both GlcNAc and GalNAc. We conclude that incorporation of d-galactosamine requires three enzymes: Gne epimerase for the generation of UDP-GalNAc from UDP-GlcNAc, N-acetylgalactosaminyltransferase (WabP), and LPS:HexNAc deacetylase. [ABSTRACT FROM AUTHOR]

Polar and lateral flagellin proteins from Aeromonas hydrophila strain AH-3 (serotype O34) were found to be glycosylated with different carbohydrate moieties. The lateral flagellin was modified at three sites in O-linkage, with a single monosaccharide of 376 Da, which we show to be a pseudaminic acid derivative. The polar flagellin was modified with a heterogeneous glycan, comprised of a heptasaccharide, linked through the same 376-Da sugar to the protein backbone, also in O-linkage. Inframe deletion mutants of pseudaminic acid biosynthetic genes pseB and pseF homologues resulted in abolition of polar and lateral flagellar formation by posttranscriptional regulation of the flagellins, which was restored by complementation with wild type pseB or F homologues or Campylobacter pseB and F. [ABSTRACT FROM AUTHOR]

Abstract: Bacteria belonging to the genus Aeromonas are Gram-negative mesophilic and essentially ubiquitous in the microbial biosphere; moreover they are considered very important pathogens in fish and responsible for a great variety of human infections. The virulence of Gram-negative bacteria is often associated with the structure of lipopolysaccharides, which consist of three regions covalently linked: the glycolipid (lipid A), the oligosaccharide region (core region) and the O-specific polysaccharide (O-chain, O-antigen). The O-chain region seems to play an important role in host-pathogen interaction. In the case of Aeromonas hydrophila the majority of pathogenic strains belongs to serogroups O:11, O:16, O:18 and O:34. In this paper, we report the complete structure of the O-chain of A. hydrophila strain A19 (serogroup O:14), a pathogenic strain isolated from European eels, which showed high virulence when tested in trout or mice. Dried cells were extracted by the PCP (phenol/chloroform/petroleum ether) method obtaining the lipopolysaccharide. After mild acid hydrolysis the lipid A was removed by centrifugation and the obtained polysaccharide was fully characterized by means of chemical analysis and one- and two-dimensional NMR spectroscopy. All the data collected are directed towards the following structure:▪ [Copyright &y& Elsevier]

The core Iipopolysaccharide (LPS) of Aeromonas hydrophila AH-3 and Aeromonas salmonicida A450 is characterized by the presence of the pentasaccharide α-D-GlcN-(1→7)-L-α-D-Hep-(1→2)-L-α-D-Hep-(1→3)-L-α-D-Hep-(1→5)-α-Kdo. Previously it has been suggested that the WahA protein is involved in the incorporation of GIcN residue to outer core LPS. The WahA protein contains two domains: a glycosyltransferase and a carbohydrate esterase. In this work we demonstrate that the independent expression of the WahA glycosyltransferase domain catalyzes the incorporation of GIcNAc from UDP-GIcNAc to the outer core LPS. Independent expression of the carbohydrate esterase domain leads to the deacetylation of the GIcNAc residue to GlcN. Thus, the WahA is the first described bifunctional glycosyltransferase enzyme involved in the biosynthesis of core LPS. By contrast in Enterobacteriaceae containing GIcN in their outer core LPS the two reactions are performed by two different enzymes. [ABSTRACT FROM AUTHOR]

Abstract: High-molecular-mass polysaccharides were released by mild acid degradation of the lipopolysaccharides of two wild-type Vibrio vulnificus strain, a flagellated motile strain CECT 5198 and a non-flagellated non-motile strain S3-I2-36. Studies by sugar analysis and partial acid hydrolysis along with 1H and 13C NMR spectroscopies showed that the polysaccharides from both strains have the same trisaccharide repeating unit of the following structure: →4)-β-d-GlcpNAc3NAcylAN-(1→4)-α-l-GalpNAmA-(1→3)-α-d-QuipNAc-(1→ where QuiNAc stands for 2-acetamido-2,6-dideoxyglucose, GalNAmA for 2-acetimidoylamino-2-deoxygalacturonic acid, GlcNAc3NAcylAN for 2-acetamido-3-acylamino-2,3-dideoxyglucuronamide and acyl for 4-d-malyl (∼30%) or 2-O-acetyl-4-d-malyl (∼70%). The structure of the polysaccharide studied resembles much that of a marine bacterium Pseudoalteromonas rubra ATCC 29570 reinvestigated in this work. The latter differs in (i) the absolute configuration of malic acid (l vs d), (ii) 3-O-acetylation of GalNAmA and (iii) replacement of QuiNAc with its 4-keto biosynthetic precursor. [Copyright &y& Elsevier]

Abstract: A polysaccharide isolated after mild acid degradation of the lipopolysaccharide of Vibrio vulnificus clinical isolate YJ016 was found to contain l-Fuc, d-GlcpNAc, 2,4-diacetamido-2,4,6-trideoxy-d-glucose (di-N-acetylbacillosamine, d-QuiNAc4NAc), and 2-acetimidoylamino-2-deoxy-l-galacturonic acid (l-GalNAmA). The last sugar derivative was confirmed by correlations for nitrogen-linked protons in 2D TOCSY and ROESY spectra measured in a H2O–D2O mixture. The following structure of the polysaccharide was established by 1H and 13C NMR spectroscopy, including 2D ROESY and 1H,13C HMBC experiments: Display Omitted where the degree of 6-O-acetylation of the lateral β-GlcNAc residue is ∼70%. [Copyright &y& Elsevier]

Abstract: A polysaccharide was isolated by GPC after mild acid treatment of the lipopolysaccharide of Vibrio vulnificus CECT4602 and found to contain l-Rha, d-GlcpNAc and 2-acetamido-2,3,6-trideoxy-3-(3-hydroxybutanoylamino)-l-mannose (l-RhaNAc3NHb). GLC analysis of the trifluoroacetylated (S)-2-octyl esters derived by full acid hydrolysis of the polysaccharide showed that ∼80% of the 3-hydroxybutanoic acid has the S configuration and ∼20% the R configuration. The following structure of the polysaccharide was established by 1H and 13C NMR spectroscopies, including 2D ROESY and 1H/13C HMBC experiments: ▪ [Copyright &y& Elsevier]

The core lipopolysaccharide (LPS) of Klebsiella pneumoniae is characterized by the presence of disaccharide αGlcN-(1,4)-αGalA attached by an α1,3 linkage to L-glycero-D-manno-heptopyranose II (LD-HeppII). Previously it has been shown that the WabH enzyme catalyzes the incorporation of GlcNAc from UDP-GlcNAc to outer core LPS. The presence of GlcNAc instead of GlcN and the lack of UDP-GlcN in bacteria indicate that an additional enzymatic step is required. In this work we identified a new gene (wabN) in the K. pneumoniae core LPS biosynthetic cluster. Chemical and structural analysis of K. pneumoniae non-polar wabN mutants showed truncated core LPS with GlcNAc instead of GlcN. In vitro assays using LPS truncated at the level of D-galacturonic acid (GalA) and cell-free extract containing WabH and WabN together led to the incorporation of GlcN, whereas none of them alone were able to do it. This result suggests that the later enzyme (WabN) catalyzes the deacetylation of the core LPS containing the GlcNAc residue. Thus, the incorporation of the GlcN residue to core LPS in K. pneumoniae requires two distinct enzymatic steps. WabN homologues are found in Serratia marcescens and some Proteus strains that show the same disaccharide αGlcN-(1,4)-αGalA attached by an α1,3 linkage to LD-HeppII. [ABSTRACT FROM AUTHOR]

A rough strain of Aeromonas hydrophila, AH-901, has an R-type lipopolysaccharide with the complete core. The following core structure was established by chemical degradations followed by sugar and methylation analyses along with ESIMS and NMR spectroscopy:where d-α-d-Hep and l-α-d-Hep stand for d-glycero- and l-glycero-α-d-manno-heptose, respectively; Kdo stands for 3-deoxy-d-manno-oct-2-ulosonic acid; all monosaccharides are in the pyranose form; the degree of substitution with β-d-Gal is ∼50%. Lipid A of the lipopolysaccharide has a 1,4′-bisphosphorylated β-d-GlcN-(1 → 6)-α-d-GlcN disaccharide backbone with both phosphate groups substituted with 4-amino-4-deoxyarabinose residues. [Copyright &y& Elsevier]

The O-polysaccharide of Aeromonas hydrophila O:34 was obtained by mild-acid degradation of the lipopolysaccharide and studied by chemical methods and NMR spectroscopy before and after O-deacetylation. The polysaccharide was found to contain d-Man, d-GalNAc and 6-deoxy-l-talose (l-6dTal), and the following structure of the tetrasaccharide repeating unit was established:where 6dTalI is O-acetylated stoichiometrically at position-2 and 6dTalII carries no, one or two O-acetyl groups at any positions. [Copyright &y& Elsevier]