Closing Water Cycles in the Built Environment through Nature-Based Solutions: The Contribution of Vertical Greening Systems and Green Roofs

Water in the city is typically exploited in a linear process, in which most of it is polluted, treated, and discharged; during this process, valuable nutrients are lost in the treatment process instead of being cycled back and used in urban agriculture or green space. The purpose of this paper is to advance a new paradigm to close water cycles in cities via the implementation of naturebased solutions units (NBS_u), with a particular focus on building greening elements, such as green roofs (GRs) and vertical greening systems (VGS). The hypothesis is that such “circular systems” can provide substantial ecosystem services and minimize environmental degradation. Our method is twofold: we first examine these systems from a life-cycle point of view, assessing not only the inputs of conventional and alternative materials, but the ongoing input of water that is required for irrigation. Secondly, the evapotranspiration performance of VGS in Copenhagen, Berlin, Lisbon, Rome, Istanbul, and Tel Aviv, cities with different climatic, architectural, and sociocultural contexts have been simulated using a verticalized ET0 approach, assessing rainwater runoff and greywater as irrigation resources. The water cycling performance of VGS in the mentioned cities would be sufficient at recycling 44% (Lisbon) to 100% (Berlin, Istanbul) of all accruing rainwater roof–runoff, if water shortages in dry months are bridged by greywater. Then, 27–53% of the greywater accruing in a building could be managed on its greened surface. In conclusion, we address the gaps in the current knowledge and policies identified in the different stages of analyses, such as the lack of comprehensive life cycle assessment studies that quantify the complete “water footprint” of building greening systems.info:eu-repo/semantics/publishedVersio

TDP-43 overexpression moderately suppresses HIV-1 gene expression in 293T cells.

<p>293T cells were transfected with (A) TDP-43-CFP expression plasmid or (B) TDP-43-IRES-BFP expression plasmid. One day later cells were exposed to equal amounts of <i>env</i>-defective VSV-G pseudotyped HIV-IRES-GFP or HIV-iGag-GFP. 48 hours later levels of GFP were quantified by FACS specifically in the transfected, i.e. CFP/BFP positive population, as marker for viral gene expression. The graph shows mean values and standard deviation from (A) four and (B) five independent experiments. GFP levels in the population transfected with CFP/BFP only were set to 100%. Statistical significant results are indicated by the respective p-value; ns =  not significant.</p

Characterization of TDP-43 expression constructs.

<p>Lysates of 293T cells transfected with the indicated TDP-43 expression vectors were analysed for TDP-43 expression by WB. Sample list: 1, mock; 2, TDP-43-V5; 3, TDP-43-CFP; 4, TDP-43-IRES-BFP.</p

TDP-43 does not suppress HIV-1 Tat mediated LTR transactivation.

<p>HeLa-HIV-indi cells expressing dsRed under control of the HIV-1 LTR were transfected with or without HIV-1 Tat and the indicated amounts of TDP-43-V5 expression plasmid. 36–48 hours later cells were trypsinized and dsRed expression was quantified by FACS. The graph depicts mean values and standard deviation of three independent duplicate transfections. The level of dsRed expression induced by Tat without TDP-43 cotransfection was set to 100%.</p

Release of Immunomodulatory Ebola Virus Glycoprotein-Containing Microvesicles Is Suppressed by Tetherin in a Species-Specific Manner

Summary: The Ebola virus glycoprotein (EBOV-GP) forms GP-containing microvesicles, so-called virosomes, which are secreted from GP-expressing cells. However, determinants of GP-virosome release and their functionality are poorly understood. We characterized GP-mediated virosome formation and delineated the role of the antiviral factor tetherin (BST2, CD317) in this process. Residues in the EBOV-GP receptor-binding domain (RBD) promote GP-virosome secretion, while tetherin suppresses GP-virosomes by interactions involving the GP-transmembrane domain. Tetherin from multiple species interfered with GP-virosome release, and tetherin from the natural fruit bat reservoir showed the highest inhibitory activity. Moreover, analyses of GP from various ebolavirus strains, including the EBOV responsible for the West African epidemic, revealed the most efficient GP-virosome formation by highly pathogenic ebolaviruses. Finally, EBOV-GP-virosomes were immunomodulatory and acted as decoys for EBOV-neutralizing antibodies. Our results indicate that GP-virosome formation might be a determinant of EBOV immune evasion and pathogenicity, which is suppressed by tetherin. : Nehls et al. demonstrate that the glycoprotein of the highly pathogenic Ebola virus is incorporated into secretory vesicles, called GP-virosomes, to dampen the immune response and capture neutralizing antibodies. The lack of replication competence and the incorporation of antigenically intact GP might qualify GP-virosomes as safe vaccine candidates. Keywords: Ebola virus, glycoprotein, microvesicles, virosome, exosome, tetherin, immune modulation, immune evasion, antiviral immune response, neutralizing antibod

Cathelicidin and PMB neutralize endotoxins by multifactorial mechanisms including LPS interaction and targeting of host cell membranes

Antimicrobial peptides (AMPs) contribute to an effective protection against infections. The antibacterial function of AMPs depends on their interactions with microbial membranes and lipids, such as lipopolysaccharide (LPS; endotoxin). Hyperinflammation induced by endotoxin is a key factor in bacterial sepsis and many other human diseases. Here, we provide a comprehensive profile of peptide-mediated LPS neutralization by systematic analysis of the effects of a set of AMPs and the peptide antibiotic polymyxin B (PMB) on the physicochemistry of endotoxin, macrophage activation, and lethality in mice. Mechanistic studies revealed that the host defense peptide LL-32 and PMB each reduce LPS-mediated activation also via a direct interaction of the peptides with the host cell. As a biophysical basis, we demonstrate modifications of the structure of cholesterol-rich membrane domains and the association of glycosylphosphatidylinositol (GPI)-anchored proteins. Our discovery of a host cell–directed mechanism of immune control contributes an important aspect in the development and therapeutic use of AMPs