Environmental DNA can act as a biodiversity barometer of anthropogenic pressures in coastal ecosystems

Loss of biodiversity from lower to upper trophic levels reduces overall productivity and stability of coastal ecosystems in our oceans, but rarely are these changes documented across both time and space. The characterisation of environmental DNA (eDNA) from sediment and seawater using metabarcoding offers a powerful molecular lens to observe marine biota and provides a series of ‘snapshots’ across a broad spectrum of eukaryotic organisms. Using these next-generation tools and downstream analytical innovations including machine learning sequence assignment algorithms and co-occurrence network analyses, we examined how anthropogenic pressures may have impacted marine biodiversity on subtropical coral reefs in Okinawa, Japan. Based on 18 S ribosomal RNA, but not ITS2 sequence data due to inconsistent amplification for this marker, as well as proxies for anthropogenic disturbance, we show that eukaryotic richness at the family level significantly increases with medium and high levels of disturbance. This change in richness coincides with compositional changes, a decrease in connectedness among taxa, an increase in fragmentation of taxon co-occurrence networks, and a shift in indicator taxa. Taken together, these findings demonstrate the ability of eDNA to act as a barometer of disturbance and provide an exemplar of how biotic networks and coral reefs may be impacted by anthropogenic activities

Scoping Study On Local Faith Communities In Urban Displacement: Evidence on Localisation and Urbanisation

<p>The aim of this report is to highlight evidence regarding the roles and impact that Local Faith Communities (LFCs) play in relation to urban refugees, with the aim of informing interconnected conversations around localisation and urbanisation.</p><p>The international community is increasingly committed to supporting local responses to displacement, at a time when the humanitarian system is overburdened, underfunded and in flux as the world reportedly faces the highest levels of displacement ever recorded – over 65 million people in 2017, who have been forced to flee their homes due to conflict, violence, and persecution. In 2016 the World Humanitarian Summit (WHS) resulted in the Charter for Change and a renewed call for meaningful support for the ‘localisation of humanitarian aid’ agenda. In part building on the UNHCR’s work following the High Commissioner’s Dialogue on Faith and Protection in December 2012, this includes recognition of the actual and potential roles of LFCs in offering protection, solidarity and assistance to displaced people throughout different stages and spaces of their journeys.</p><div><div><div><p>This evidence is therefore centrally relevant to two key debates in contemporary humanitarian policy and practice – localisation and urbanisation – whose outcomes will have a significant impact on the future of refugee protection.</p></div></div></div

Myofibrillar and Mitochondrial Protein Synthesis Rates Do Not Differ in Young Men Following the Ingestion of Carbohydrate with Whey, Soy, or Leucine-Enriched Soy Protein after Concurrent Resistance- and Endurance-Type Exercise

Whey and micellar casein are high-quality dairy proteins that can stimulate postprandial muscle protein synthesis rates. How whey and casein compare with milk protein in their capacity to stimulate postprandial myofibrillar (MyoPS) and mitochondrial (MitoPS) protein synthesis rates during postexercise recovery is currently unknown. Objective: The objective of this study was to compare postprandial MyoPS and MitoPS rates after protein-carbohydrate co-ingestion with milk protein, whey, or micellar casein during recovery from a single bout of concurrent resistance- and endurance-type exercise in young healthy men. Methods: In a randomized, double-blind, parallel-group design, 48 healthy, young, recreationally active men (mean SEM age: 23 0.3 y) received a primed continuous infusion of L-[ring-13C6]-phenylalanine and L-[ring-3,5-2H2]-tyrosine and ingested 45 g carbohydrate with 0 g protein (CHO), 20 g milk protein (MILK), 20 g whey protein (WHEY), or 20 g micellar casein protein (CASEIN) after a sequential bout of resistance- and endurance-type exercise (i.e., concurrent exercise). Blood and muscle biopsies were collected over 360 min during recovery from exercise to assess MyoPS and MitoPS rates and signaling through mammalian target of rapamycin complex 1 (mTORC1). Results: Despite temporal differences in postprandial plasma leucine concentrations between treatments (P < 0.001), MyoPS rates over 360 min of recovery did not differ between treatments (CHO: 0.049% 0.003%/h; MILK: 0.059% 0.003%/h; WHEY: 0.054% 0.002%/h; CASEIN: 0.059% 0.005%/h; P = 0.11). When MILK, WHEY, and CASEIN were pooled into a single group (PROTEIN), protein co-ingestion resulted in greater MyoPS rates compared with CHO (PROTEIN: 0.057% 0.002%/h; CHO: 0.049% 0.003%/h; P = 0.04). MitoPS rates and signaling through the mTORC1 pathway were similar between treatments. Conclusion: MyoPS and MitoPS rates do not differ after co-ingestion of either milk protein, whey protein, or micellar casein protein with carbohydrate during recovery from a single bout of concurrent resistance- and endurance-type exercise in recreationally active young men. Co-ingestion of protein with carbohydrate results in greater MyoPS, but not MitoPS rates, when compared with the ingestion of carbohydrate only during recovery from concurrent exercise. This trial was registered at Nederlands Trial Register: NTR5098. J Nutr 2019;149:198-209

Protein Ingestion before Sleep Increases Muscle Mass and Strength Gains during Prolonged Resistance-Type Exercise Training in Healthy Young Men

BACKGROUND: It has been demonstrated that protein ingestion before sleep increases muscle protein synthesis rates during overnight recovery from an exercise bout. However, it remains to be established whether dietary protein ingestion before sleep can effectively augment the muscle adaptive response to resistance-type exercise training. OBJECTIVE: Here we assessed the impact of dietary protein supplementation before sleep on muscle mass and strength gains during resistance-type exercise training. METHODS: Forty-four young men (22 +/- 1 y) were randomly assigned to a progressive, 12-wk resistance exercise training program. One group consumed a protein supplement containing 27.5 g of protein, 15 g of carbohydrate, and 0.1 g of fat every night before sleep. The other group received a noncaloric placebo. Muscle hypertrophy was assessed on a whole-body (dual-energy X-ray absorptiometry), limb (computed tomography scan), and muscle fiber (muscle biopsy specimen) level before and after exercise training. Strength was assessed regularly by 1-repetition maximum strength testing. RESULTS: Muscle strength increased after resistance exercise training to a significantly greater extent in the protein-supplemented (PRO) group than in the placebo-supplemented (PLA) group (+164 +/- 11 kg and +130 +/- 9 kg, respectively; P < 0.001). In addition, quadriceps muscle cross-sectional area increased in both groups over time (P < 0.001), with a greater increase in the PRO group than in the PLA group (+8.4 +/- 1.1 cm2 vs. +4.8 +/- 0.8 cm2, respectively; P < 0.05). Both type I and type II muscle fiber size increased after exercise training (P < 0.001), with a greater increase in type II muscle fiber size in the PRO group (+2319 +/- 368 mum2) than in the PLA group (+1017 +/- 353 mum2; P < 0.05). CONCLUSION: Protein ingestion before sleep represents an effective dietary strategy to augment muscle mass and strength gains during resistance exercise training in young men. This trial was registered at clinicaltrials.gov as NCT02222415

Oligomerization of the Macrophage Mannose Receptor Enhances gp120-mediated Binding of HIV-1

C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N-acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dendritic cells, and mannose receptor (MR) on dendritic cells and macrophages bind the human immunodeficiency virus (HIV) envelope protein gp120 principally via high mannose oligosaccharides. These C-type lectin receptors can also oligomerize to facilitate enhanced ligand binding. This study examined the effect of oligomerization of MR on its ability to bind to mannan, monomeric gp120, native trimeric gp140, and HIV type 1 BaL. Mass spectrometry analysis of cross-linked MR showed homodimerization on the surface of primary monocyte-derived dendritic cells and macrophages. Both monomeric and dimeric MR were precipitated by mannan, but only the dimeric form was co-immunoprecipitated by gp120. These results were confirmed independently by flow cytometry analysis of soluble monomeric and trimeric HIV envelope and a cellular HIV virion capture assay. As expected, mannan bound to the carbohydrate recognition domains of MR dimers mostly in a calcium-dependent fashion. Unexpectedly, gp120-mediated binding of HIV to dimers on MR-transfected Rat-6 cells and macrophages was not calcium-dependent, was only partially blocked by mannan, and was also partially inhibited by N-acetylgalactosamine 4-sulfate. Thus gp120-mediated HIV binding occurs via the calcium-dependent, non-calcium-dependent carbohydrate recognition domains and the cysteine-rich domain at the C terminus of MR dimers, presenting a much broader target for potential inhibitors of gp120-MR binding