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Purpose: To systematically evaluate the effectiveness and safety of Compound Danshen injection in patients with pregnancy-induced hypertension (PIH). Methods: PubMed, Embase, Cochrane Library, Chinese biomedical literature database (CBM), VIP (xiAn), China National Knowledge Infrastructure (CNKI) and Wan Fang databases were searched up to March 20, 2018, for all randomized controlled trials (RCTs) on the use of Compound Danshen injection in patients with PIH. Data were extracted from included studies after assessing the quality of literature. Revman 5.3 software was used for statistical analysis． Results: A total of 18 RCTs involving 1735 patients were included. The results of meta-analysis indicated that the study group was superior to the control group in clinical effectiveness (RR = 1.15, 95 % CI: 1.02 - 1.30); intrauterine fetal distress (RR = 0.26, 95 % CI: 0.09 - 0.70); cesarean section (RR = 0.72, 95 % CI: 0.58 - 0.90), and neonatal asphyxia (RR = 0.23, 95 % CI: 0.11 - 0.48). There were no statistical differences in fetal heart rate abnormalities (RR = 0.58, 95 %, CI: 0.33 - 1.02, p > 0.05) and postpartum hemorrhage (RR = 0.86, 95 % CI: 0.53 - 1.42) between the two groups. Conclusion: Treatment of PIH with Compound Danshen injection (alone or in combination) is superior to the use of conventional western medical treatment in safety and effectiveness. However, higher quality clinical studies are needed to confirm these results because most trials included in this study were of low quality. [ABSTRACT FROM AUTHOR]

The nucleotide sequence of the predicted immunodominant region of bovine haptoglobin (pirBoHp), without the signal peptide sequence, was synthesized based on the codon usage bias of Escherichia coli. The synthesized pirBoHp gene was cloned into the prokaryotic expression vector pET-32a (+), which contains a His-tag. The recombinant pirBoHp protein was successfully expressed in E. coli BL21 (DE3) cells. Western blot analysis showed that the purified recombinant pirBoHp protein could be recognized by an anti-His-tag monoclonal antibody. Further investigations indicated that a polyclonal antibody against the recombinant pirBoHp protein could recognize the α and β chains of native bovine haptoglobin in a pooled plasma sample from dairy cattle suffering from foot rot. [ABSTRACT FROM AUTHOR]

Subversion of the host cell cycle to facilitate viral replication is a common feature of coronavirus infections. Coronavirus nucleocapsid (N) protein can modulate the host cell cycle, but the mechanistic details remain largely unknown. Here, we investigated the effects of manipulation of porcine epidemic diarrhea virus (PEDV) N protein on the cell cycle and the influence on viral replication. Results indicated that PEDV N induced Vero E6 cell cycle arrest at S-phase, which promoted viral replication (P,0.05). S-phase arrest was dependent on the N protein nuclear localization signal S71NWHFYYLGTGPHADLRYRT90 and the interaction between N protein and p53. In the nucleus, the binding of N protein to p53 maintained consistently high-level expression of p53, which activated the p53-DREAM pathway. The key domain of the N protein interacting with p53 was revealed to be S171RGNSQNRGNNQGRGASQNRGGNN194 (NS171-N194), in which G183RG185 are core residues. NS171-N194 and G183RG185 were essential for Ninduced S-phase arrest. Moreover, small molecular drugs targeting the NS171-N194 domain of the PEDV N protein were screened through molecular docking. Hyperoside could antagonize N protein-induced S-phase arrest by interfering with interaction between N protein and p53 and inhibit viral replication (P,0.05). The above-described experiments were also validated in porcine intestinal cells, and data were in line with results in Vero E6 cells. Therefore, these results reveal the PEDV N protein interacts with p53 to activate the p53-DREAM pathway, and subsequently induces S-phase arrest to create a favorable environment for virus replication. These findings provide new insight into the PEDV-host interaction and the design of novel antiviral strategies against PEDV. [ABSTRACT FROM AUTHOR]

A pair of primers was designed in an attempt to amplify outer membrane protein (OMP) gene of Fusobacterium necrophorum based on nucleotide sequence of the OMP of Fusobacterium nucleatum. Further analysis was performed to characterize its molecular properties and phylogeny in the genus Fusobacterium. We identified a predicated 43 kDa outer membrane protein (43 K OMP) in F. necrophorum, which showed the same properties as other pore-forming proteins of Gram-negative anaerobic bacteria according to analysis of signal peptide, AT-rich, membrane-spanning region and conserved motifs. The predicated 43 K OMP exhibited 70.22%, 62.04%, 56.75%, 58.72%, 51.59%, 31.49% and 50.26% amino acid identity with the OMPs of F. nucleatum, Fusobacterium varium, Fusobacterium ucerans, Fusobacterium periodonticum, Fusobacterium mortiferum, Fusobacterium gonidiaformans and F. necrophorum (hypothetical protein), respectively. 11 common conserved domains and 10 common variable domains were found among the 45 aligned OMPs of Fusobacterium species. Distributions of the conserved and variable domains were highly associated with predicted membrane-spanning regions, cell surface exposed regions and B-cell epitope regions. Phylogenetic analysis revealed the predicated 43 K OMP of F. necrophorum was closely related with the OMPs from F. nucleatum and F. periodonticum. These data will increase understanding of pathogenesis and genetic evolution of F. necrophorum. [ABSTRACT FROM AUTHOR]