Capacity fading induced by unstable surface chemical properties and intrinsic structural degradation is a critical challenge for the commercial utilization of Ni-rich cathodes. Here, a highly stabilized Ni-rich cathode with enhanced rate capability and cycling life is constructed by coating the molybdenum compound on the surface of LiNi 0.815 Co 0.15 Al 0.035 O 2 secondary particles. The infused Mo ions in the boundaries not only induce the Li 2 MoO 4 layer in the outermost but also form an epitaxially grown outer surface region with a NiO-like phase and an enriched content of Mo 6+ on the bulk phase. The Li 2 MoO 4 layer is expected to reduce residential lithium species and promote the Li + transfer kinetics. The transition NiO-like phase, as a pillaring layer, could maintain the integrity of the crystal structure. With the suppressed electrolyte−cathode interfacial side reactions, structure degradation, and intergranular cracking, the modified cathode with 1% Mo exhibits a superior discharge capacity of 140 mAh g −1 at 10 C, a superior cycling performance with a capacity retention of 95.7% at 5 C after 250 cycles, and a high thermal stability.

Powdery mildew is a fungal disease found in a wide range of plants and can significantly reduce crop yields. Bacterial strain LJ02 is a biocontrol agent (BCA) isolated from a greenhouse in Tianjin, China. In combination of morphological, physiological, biochemical and phylogenetic analyses, strain LJ02 was classified as a new member of Bacillus amyloliquefaciens. Greenhouse trials showed that LJ02 fermentation broth (LJ02FB) can effectively diminish the occurrence of cucurbits powdery mildew. When treated with LJ02FB, cucumber seedlings produced significantly elevated production of superoxide dismutase, peroxidase, polyphenol oxidase and phenylalanine ammonia lyase as compared to that of the control. We further confirmed that the production of free salicylic acid (SA) and expression of one pathogenesis-related (PR) gene PR-1 in cucumber leaves were markedly elevated after treating with LJ02FB, suggesting that SA-mediated defense response was stimulated. Moreover, LJ02FB-treated cucumber leaves could secrete resistance-related substances into rhizosphere that inhibit the germination of fungi spores and the growth of pathogens. Finally, we separated bacterium and its fermented substances to test their respective effects and found that both components have SA-inducing activity and bacterium plays major roles. Altogether, we identified a BCA against powdery mildew and its mode of action by inducing systemic resistance such as SA signaling pathway.

A highly active and stable photocatalyst MoS2-graphene/CdS nanoparticles/nanorods was prepared using a facile two-step hydrothermal method. The noble-metal-free photocatalyst achieved a remarkable quantum yield of 65.8% at 420 nm for photocatalytic H2 evolution from water.

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Group C rotavirus (GCRV) is distributed worldwide as an enteric pathogen in humans and animals. However, to date, whole-genome sequences are available only for a human strain (Bristol) and a porcine strain (Cowden). To investigate the genetic diversity of human GCRVs, nearly full-length sequences of all 11 RNA segments were determined for human GCRVs detected recently in India (v508), Bangladesh (BS347), China (Wu82 and YNR001) and Japan (OH567 and BK0830) and analysed phylogenetically with sequence data for GCRVs published previously. All the RNA segments of human GCRV strains except for the VP3 gene showed high levels of conservation (.93 % nucleotide sequence identity, .92 % amino acid sequence identity), belonging to a single genetic cluster distinct from those of animal GCRVs. In contrast, the VP3 genes of human GCRVs could be discriminated into two clusters, designated M2 and M3, that were distinguished phylogenetically from those of porcine and bovine GCRVs (clusters M1 and M4, respectively). Between M2 and M3, amino acid sequence identity of the VP3 gene was 84.1-84.7 %, whereas high identities were observed within each cluster (92.3-97.6 % for M2, 98.2-99.3 % for M3). Sequence divergence among the four VP3 clusters was observed throughout the amino acid sequence except for conserved motifs, including those possibly related to enzyme functions of VP3. The presence of obvious genetic diversity only in the VP3 gene among human GCRVs suggested that either the M2 or M3 VP3 gene of human GCRVs might have been derived through reassortment from an animal GCRV or from an unidentified human GCRV strain belonging to a novel genogroup. INTRODUCTIONRotavirus, a member of the family Reoviridae, is the most important viral pathogen that causes gastroenteritis in humans. The rotavirus genome consists of 11 segments of dsRNA, and the viral particle is composed of three concentric layers, the outer capsid, inner capsid and core (Estes & Kapikian, 2007). The outer capsid consists of two structural proteins, VP4 and VP7, which contain neutralization antigens. The inner capsid consists of structural protein VP6. Rotavirus is classified into seven groups, A-G, based on the antigenicity of the inner capsid protein VP6 and genomic characteristics (Kapikian et al., 2001). In humans, groups A, B and C have been detected to date. Group A rotavirus (GARV) is the most prevalent throughout the world and is recognized as the leading viral pathogen of acute gastroenteritis in children. For epidemiological investigations of GARV, a genetic classification system based on the outer capsid proteins VP7 (G type) and VP4 (P type) has been adopted (Santos & Hoshino, 2005). In addition, a full-genome-based genotyping system composed of genotypes of the 11 individual RNA segments has been proposed on the basis of full-The GenBank/EMBL/DDBJ accession numbers for the GCRV sequences determined in this study are HQ185629-HQ185631 (v508), HQ185632-HQ185642 (BS347), HQ185643-HQ185651 (Wu82), HQ185652-HQ185662 (YNR001), HQ185663-HQ185672 (OH567) and ...

Mitochondrial RNA (mtRNA) polymerases are related to bacteriophage RNA polymerases, but contain a unique amino-terminal extension of unknown origin and function. In addition to harboring mitochondrial targeting information, we show here that the amino-terminal extension of yeast mtRNA polymerase is required for a mtDNA maintenance function that is separable from the known RNA polymerization activity of the enzyme. Deletion of 185 Nterminal amino acids from the enzyme results in a temperature-sensitive mitochondrial petite phenotype, characterized by increased instability and eventual loss of the mitochondrial genome. Mitochondrial transcription initiation in vivo is largely unaffected by this mutation and expression of just the amino-terminal portion of the protein in trans partially suppresses the mitochondrial defect, indicating that the amino-terminal extension of the enzyme harbors an independent functional domain that is required for mtDNA replication and͞or stability. These results suggest that amino-terminal extensions present in mtRNA polymerases comprise functional domains that couple additional activities to the transcription process in mitochondria.

Novel rotavirus strains B219 and ADRV-N derived from adult diarrheal cases in Bangladesh and China, respectively, are considered to belong to a novel rotavirus group (species) distinct from groups A, B, and C, by genetic analysis of five viral genes encoding VP6, VP7, NSP1, NSP2, and NSP3. In this study, the nucleotide sequences of the remaining six B219 gene segments encoding VP1, VP2, VP3, VP4, NSP4, and NSP5 were determined. The nucleotide sequences of the group B human rotavirus VP1 and VP3 genes were also determined in order to compare the whole genome of B219 with those of group A, B, and C rotavirus genomes. The nucleotide and deduced amino acid sequences of all B219 gene segments showed considerable identity to the ADRV-N (strain J19) sequences (87.7-94.3% and 88.7-98.7%, respectively). In contrast, sequence identity to groups A-C rotavirus genes was less than 61%. However, functionally important domains and structural characteristics in VP1-VP4, NSP4, and NSP5, which are conserved in group A, B, or C rotaviruses, were also found in the deduced amino acid sequences of the B219 proteins. Hence, the basic structures of all B219 viral proteins are considered to be similar to those of the known rotavirus groups.