Severe fever with thrombocytopenia syndrome (SFTS) virus is an emerging zoonotic virus in East Asia. However, SFTS virus (SFTSV) has not been reported to cause clinical infection in companion dogs to date. We report the case of a 4‐year‐old companion dog that presented with fever, vomiting, leukocytopenia and thrombocytopenia at a veterinary hospital in the Republic of Korea. It was diagnosed with SFTS, which was confirmed using real‐time reverse transcription PCR, sequencing and an indirect immunofluorescence assay, and recovered after supportive care. Further studies are required to investigate SFTSV infection in companion animals, living in close contact with humans, as well as animal‐to‐human transmission.

Arabidopsis thaliana gene At5g06450 encodes a putative DnaQ-like 3′-5′ exonuclease domain-containing protein (AtDECP). The DnaQ-like 3′-5′ exonuclease domain is often found as a proofreading domain of DNA polymerases. The overall structure of AtDECP adopts an RNase H fold that consists of a mixed β-sheet flanked by α-helices. Interestingly, AtDECP forms a homohexameric assembly with a central 6-fold symmetry, generating a central cavity. The ring-shaped structure and comparison with WRN-exo, the best structural homologue of AtDECP, suggest a possible mechanism for implementing its exonuclease activity using positively charged patch on the N-terminal side of the homohexameric assembly. The homohexameric structure of AtDECP provides unique information about the interaction between the DnaQ-like 3′-5′ exonuclease and its substrate nucleic acids.

Members of the universal stress protein (USP) family are conserved in a phylogenetically diverse range of prokaryotes, fungi, protists, and plants and confer abilities to respond to a wide range of environmental stresses. Arabidopsis thaliana contains 44 USP domain-containing proteins, and USP domain is found either in a small protein with unknown physiological function or in an N-terminal portion of a multi-domain protein, usually a protein kinase. Here, we report the first crystal structure of a eukaryotic USP-like protein encoded from the gene At3g01520. The crystal structure of the protein At3g01520 was determined by the single-wavelength anomalous dispersion method and refined to an R factor of 21.8% (Rfree = 26.1%) at 2.5 Å resolution. The crystal structure includes three At3g01520 protein dimers with one AMP molecule bound to each protomer, comprising a Rossmann-like α/β overall fold. The bound AMP and conservation of residues in the ATP-binding loop suggest that the protein At3g01520 also belongs to the ATP-binding USP subfamily members.

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BackgroundDysregulation of protein degradation is related with various diseases including Alzheimer’s disease. Bortezomib is the first drug to treat multiple myeloma, however, the major side effect is induction of peripheral neuropathy. This study was performed to explore the effects and mechanisms of proteasome inhibition in neural stem cells (NSCs).MethodCortical neural stem cells were obtained and cultured from embryonic day 14 rats. By immunocytochemistry (ICC), western blot analysis and real‐time PCR followed by reverse transcription PCR, the cell fate of neural stem cells were identified. Toxicity was determined by MTT assay and neurosphere size measurement. BCL2‐BAX protein ratio was detected by western blot to explore the cytotoxic mechanisms.ResultNeurogenesis was significantly increased by bortezomib in proliferating NSCs when determine by ICC, western blot and PCR. However, such effect was not observed during NSC differentiation. In addition, Bortezomib induced toxicity in both proliferating NSCs and differentiated cells.ConclusionBortezomib is toxic to NSCs and differentiated cells, however, it induced neurogenesis in NSCs.