A hybrid anaerobic solid-liquid bioreactor for food waste digestion

A hybrid anaerobic solid-liquid (HASL) bioreactor is an enhanced two-phase anaerobic system, that consists of a solid waste reactor as the acidification reactor and a wastewater reactor, i.e. an upflow anaerobic sludge blanket (UASB) reactor as the methanogenic reactor. Food waste digestion in HASL bioreactors with pre-acidification and HASL operation stages was investigated in two separate runs. After 8 days of pre-acidification in Run A and 4 days in Run B, total volatile fatty acid (TVFA) and chemical oxygen demand (COD) concentrations in the leachates of both acidification reactors were similar. During HASL operation stage, TVFA and COD removal in the methanogenic phase were 77–100% and 75–95%, respectively. Some 99% of the total methane generated was from the methanogenic phase with a content of 68–70% methane. At the end of operation, about 59–60% of the added volatile solids (VS) were removed with a methane yield of 0.25 l g^–1 VS.     

Single-cell landscape of the ecosystem in early-relapse hepatocellular carcinoma

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Chimeric contribution of human extended pluripotent stem cells to monkey embryos ex vivo

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Bifidobacteria-mediated immune system imprinting early in life

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Tracing the invasion characteristics of the yellow-legged hornet,Vespa velutina nigrithorax (Hymenoptera: Vespidae), in Korea using newly detected variable mitochondrial DNA sequences

The yellow-legged hornet, Vespa velutina nigrithorax (Hymenoptera: Vespidae), invaded South Korea in 2003 through Busan metropolitan city, which is located in the southeast region of the country. Previous studies aiming to trace the origin of V. velutina in Korea used a portion of mitochondrial (mt) COI and detected a single haplotype common to the site of origin. However, no subsequent study on invasive dynamics such as additional entry and/or another site of entry has been performed. In this study, segments of mt COI, CytB, and lrRNA were sequenced from 238 individuals collected in 11 Korean and two Japanese localities, but no variation in each gene was observed. Thus, we developed two intergenic spacer (IGS) sequences from the publicly available mt genome of V. velutina, which provided substantially increased variability (i.e., 19 haplotypes with 1.74% maximum sequence divergence in 1,129–1,146-bp-long concatenated sequences). Population genetic analyses using the concatenated sequences unexpectedly provided higher genetic diversity estimates in the northwest and southwest regions, both of which also harbor international cargo ports, than in the southeast region, in which Busan is located. Furthermore, this genetic result was roughly concordant with our questionnaire survey demonstrating that V. velutina was observed in apiaries located in the northwest and southwest regions up to 2012, when there was no reported prevalent distribution of the hornet beyond the southeast region. These results collectively suggest that the northwest and southwest regions of Korea are additional sites of V. velutina entry to the country, independent from the southeast region origin.     

Negative regulation of AMPK signaling by high glucose via E3 ubiquitin ligase MG53

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The C-Terminal Amino Acid of the MHC-I Heavy Chain Is Critical for Binding to Derlin-1 in Human Cytomegalovirus US11-Induced MHC-I Degradation

Derlin-1 plays a critical role in endoplasmic reticulum-associated protein degradation (ERAD) of a particular subset of proteins. Although it is generally accepted that Derlin-1 mediates the export of ERAD substrates from the ER to the cytosol, little is known about how Derlin-1 interacts with these substrates. Human cytomegalovirus (HCMV) US11 exploits Derlin-1-dependent ERAD to degrade major histocompatibility complex class I (MHC-I) molecules and evade immune surveillance. US11 requires the cytosolic tail of the MHC-I heavy chain to divert MHC-I molecules into the ERAD pathway for degradation; however, the underlying mechanisms remain unknown. Here, we show that the cytosolic tail of the MHC-I heavy chain, although not required for interaction with US11, is required for tight binding to Derlin-1 and thus for US11-induced dislocation of the MHC-I heavy chain to the cytosol for proteasomal degradation. Surprisingly, deletion of a single C-terminal amino acid from the cytosolic tail disrupted the interaction between MHC-I molecules and Derlin-1, rendering mutant MHC-I molecules resistant to US11-induced degradation. Consistently, deleting the C-terminal cytosolic region of Derlin-1 prevented it from binding to MHC-I molecules. Taken together, these results suggest that the cytosolic region of Derlin-1 is involved in ERAD substrate binding and that this interaction is critical for the Derlin-1-mediated dislocation of the MHC-I heavy chain to the cytosol during US11-induced MHC-I degradation.