Heavy metal ions were common pollutants in water pollution. Amino acids, as important substances in organisms, participate in many life activities. The detection of heavy metal ions and amino acids...
Streptococcus suis serotype 2 (SS2) is a zoonotic pathogen that can cause meningitis both in pigs and in human beings. However, the pathogenesis of central nervous system (CNS) infection caused by SS2 have not yet been elucidated. To find the key molecules in cerebrospinal fluid (CSF) needed for the pathogenesis, a SS2 meningoencephalitic pig model and a SS2 non-meningoencephalitic pig model were established in this study. CSF was collected from infected piglets, and protein profiling was performed with label-free proteomics technology. A total of 813 differential proteins, including 52 up-regulated proteins and 761 down-regulated proteins, were found in the CSF of meningoencephalitic pigs compared with both non-meningoencephalitic pigs and healthy pigs. These 813 differential proteins were clustered into three main categories, namely, cellular component, biological process, and molecular function by gene ontology (GO) analysis. The most enriched subclasses of differential proteins in each category were exosome (44.3%), energy pathway (25.0%) and catalytic activity (11.3%), respectively. The most enriched subclasses of upregulated proteins were extracellular (62.1%), protein metabolism (34.5%) and cysteine-type peptidase activity (6.9%), and of downregulated proteins were exosomes (45.0%), energy pathway (24.0%) and catalytic activity (9.4%). Then, the differential proteins were further investigated by using the KEGG database and were found to participate in 16 KEGGs. The most enriched KEGG was citrate cycle (56.6%), and some of these differential proteins are associated with brain diseases such as Huntington's disease (18.6%), Parkinson's disease (23.8%) and Alzheimer's disease (17.6%). Sixteen of the 813 differential proteins, chosen randomly as examples, were further confirmed by enzyme-linked immunosorbent assay (ELISA) to support the proteomic data. To our knowledge, this is the first study to analyze the differential protein profiling of CSF between SS2 meningoencephalitic piglets and non-meningoencephalitic piglets by employing proteomic technology. The discovery and bioinformatics analysis of these differential proteins provides reference data not only for research on pathogenesis of SS2 CNS infection but also for diagnosis and drug therapy research.
PAPs (purple acid phosphatases) belong to the metallo-phosphoesterase superfamily and play important roles in developmental processes, phosphorus foraging, and recycling. However, the specific functions of BrPAPs in Brassica rapa are poorly understood. In this study, 39 BrPAPs were identified and divided into three major clades and nine subgroups. In 8 of the 39 BrPAPs, some invariant amino acid residues were lost or shifted. Based on an expression profiling analysis, BrPAP11, 14, 20, 24, 29, and 34 were specifically expressed in fertile floral buds, indicating their critical roles during pollen development. A total of 21 BrPAPs responded to Pi deprivation in either shoots or roots. Of these, BrPAP4, 5, 19, and 21 were upregulated in roots under Pi depravation conditions, while BrPAP12 was upregulated in the roots in normal conditions. BrPAP28 was upregulated in shoots under Pi depravation conditions, indicating its function shifted compared with its Arabidopsis homolog, AtPAP26. The present work contributes to further investigation of BrPAPs as candidate genes for genetic improvement studies of low phosphorus tolerance as well as for creating male sterile lines based on gene editing methods in Brassica rapa.
Bovine mastitis is an inflammatory response mainly caused by Staphylococcus aureus. Lysin is a cell wall hydrolase encoded and synthesized by a bacteriophage, which can kill specific Gram-positive bacteria. In this study, phage lysin “LysGH15” is used to treat the mice mastitis caused by S. aureus. The purified lysGH15 showed strong bactericidal activity in vitro. When treated with 25μg/mL of the LysGH15, the bacterial counts of S. aureus dropped approximately 5 log units within 10 min. In the in vivo experiments, the administration of LysGH15 significantly (P<0.05) reduced the colonies of S. aureus and alleviated damage to the breast tissue. Also, the levels of IL-6 and TNF-α in breast tissue were significantly decreased. It indicates that the LysGH15 can effectively treat the murine mastitis caused by S. aureus. This study demonstrated the potential of LysGH15 as an alternative to antibiotics for treating bovine mastitis caused by S. aureus
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