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1.
Plants (Basel) ; 12(9)2023 Apr 29.
Article in English | MEDLINE | ID: mdl-37176899

ABSTRACT

Sophora tonkinensi is a shrub of the genus Sophora in the family Fabaceae with anti-inflammatory and pain-relieving effects. While the cultivation, chemical makeup, and medicinal properties of S. tonkinensis have been reported, the physiological mechanisms governing its dehydration and cryopreservation tolerance of seeds remain unclear. In this study, we investigated the morphological, physiological, biochemical, and protein expression characteristics of S. tonkinensis seeds subjected to dehydration and cryopreservation techniques via the observation of cell microstructure, determination of antioxidant enzyme activity, and iTRAQ-based proteomic analysis, respectively. The results of the study demonstrated that the seeds possessed a certain level of tolerance to dehydration. The highest germination percentage of 83.0% was observed after 2 h of dehydration (10.1% water content), which was identified as the optimal time point for cryopreservation. However, the germination percentage was reduced to only 30.5% when the water content reached 5.4%, indicating that S. tonkinensis seeds exhibit intermediate storage behavior. Further investigation revealed that during seed dehydration and cryopreservation treatment, liposomes were gradually and highly fused, whereas the activities of ROS scavenging and stress defense were significantly enhanced. During dehydration, the seed tissues formed a protective mechanism of stress resistance based on protein processing in the endoplasmic reticulum and antioxidant system, which was related to the dehydration tolerance. Moreover, only three differentially expressed LEA proteins were identified, and it is speculated that the strengthening of intracellular metabolism and the absence of specific LEA and dehydrins could be crucial factors for the reduced germination percentage after excessive dehydration and cryopreservation.

2.
Plant Cell Physiol ; 62(2): 366-377, 2021 May 11.
Article in English | MEDLINE | ID: mdl-33399871

ABSTRACT

Tea (Camellia sinensis [L.] O. Kuntze) tree is a perennial plant in which winter dormancy is an important biological adaptation to environmental changes. We discovered and reported a novel tea tree cultivar that can generate tender shoots in winter several years ago, but the molecular mechanism for this unique phenotype remains unknown . Here, we conducted comparative transcriptomics, proteomics and metabolomics along with phytohormone quantitation between the winter and spring tender shoots to investigate the physiological basis and putative regulatory mechanisms of its evergrowing character during winter. Our multi-omics study has led to the following findings. Gibberellin (GA) levels and key enzymes for GA biosynthesis and the signal transduction pathway were increased in the winter shoots, causing the ABA/GA content ratio to decrease, which might play a key regulatory role in maintaining normal growth during winter. The abundance of proteins, genes and metabolites involved in energy metabolism was all increased in winter shoots, indicating that energy is critical for continuous growth under the relatively weak-light and low-temperature environment. Abiotic resistance-related proteins and free amino acids were also increased in abundance in the winter shoots, which possibly represents an adaptation response to winter conditions. These results allowed us to hypothesize a novel molecular mechanism of adaptation for this unique tender shoot evergrowing in winter.


Subject(s)
Camellia sinensis/physiology , Plant Shoots/physiology , Adaptation, Physiological/genetics , Adaptation, Physiological/physiology , Camellia sinensis/genetics , Camellia sinensis/growth & development , Gene Expression Profiling , Metabolomics , Plant Dormancy/genetics , Plant Dormancy/physiology , Plant Growth Regulators/metabolism , Plant Growth Regulators/physiology , Plant Proteins/classification , Plant Proteins/metabolism , Plant Proteins/physiology , Plant Shoots/genetics , Plant Shoots/growth & development , Proteomics , Seasons , Signal Transduction/physiology
4.
Biomed Res Int ; 2020: 4741237, 2020.
Article in English | MEDLINE | ID: mdl-32337252

ABSTRACT

Tuberculosis (TB) is an infectious disease, caused by Mycobacterium tuberculosis, primarily affecting the lungs. The M. tuberculosis strain of the Haarlem family named M was responsible for a large multidrug-resistant TB (MDR-TB) outbreak in Buenos Aires. This outbreak started in the early 1990s and in the mid 2000s still accounted for 29% of all MDR-TB cases in Argentina. By contrast, a clonal variant of strain M, named 410, has caused a single tuberculosis case since the onset of the outbreak. The molecular bases of the high epidemiological fitness of the M strain remain unclear. To assess its unique molecular properties, herein, we performed a comparative protein and lipid analysis of a representative clone of the M strain (Mp) and the nonprosperous M variant 410. We also evaluated their growth in low pH. The variant 410 had higher levels of latency proteins under standard conditions and delayed growth at low pH, suggesting that it is more sensitive to stress stimuli than Mp. Moreover, Mp showed higher levels of mycolic acids covalently attached to the cell wall and lower accumulation of free mycolic acids in the outer layer than the 410 strain. The low expression of latency proteins together with the reduced content of surface mycolic acids may facilitate Mp to evade the host immune responses.


Subject(s)
Drug Resistance, Multiple, Bacterial , Mycobacterium tuberculosis/drug effects , Mycobacterium tuberculosis/isolation & purification , Tuberculosis, Multidrug-Resistant/epidemiology , Argentina/epidemiology , Bacterial Proteins , Cell Wall/metabolism , Disease Outbreaks , Hydrogen-Ion Concentration , Mycolic Acids/metabolism , Proteomics , Tandem Mass Spectrometry , Tuberculosis, Multidrug-Resistant/drug therapy , Tuberculosis, Multidrug-Resistant/microbiology
5.
Antonie Van Leeuwenhoek ; 113(7): 907-917, 2020 Jul.
Article in English | MEDLINE | ID: mdl-32193664

ABSTRACT

An aerobic, Gram-stain-negative, motile and rod-shaped bacterial strain, designated as Z1-4T, was isolated from the phycosphere microbiota of marine dinoflagellate Alexandrium minutum that produces paralytic shellfish poisoning toxins. Phylogenetic analysis based on 16S rRNA gene sequences showed that the new isolate belongs to the genus Mesorhizobium, and it was closely related to Mesorhizobium waimense LMG 28228T and Mesorhizobium amorphae LMG 18977T with both 16S rRNA gene sequence similarities of 97.3%. The values of average nucleotide identity (ANI) and digital DNA-DNA hybridization (dDDH) relatedness between strain Z1-4T and its relatives are both well below the thresholds used for the delineation of a new species. A genome-based phylogenetic tree constructed by up-to-date bacterial core gene set (UBCG) indicates that strain Z1-4T forms an independent branch within the genus Mesorhizobium. The respiratory quinone of strain Z1-4T was Q-10. The major fatty acids were similar to other members of the genus Mesorhizobium containing the summed feature 8, C16:0, C19:0cycloω8c, C17:0 and summed feature 3. The polar lipids are phosphatidylmonomethylethanolamine, diphosphatidylglycerol, phosphatidylcholine, phosphatidylethanolamine, phosphatidylglycerol, an unidentified aminophospholipid, five glycolipids and seven unknown polar lipids. The DNA G + C content was determined to be 62.1 mol % based on its genomic sequence. Combined evidences based on the genotypic, chemotaxonomic and phenotypic characteristics clearly indicates that strain Z1-4T represents a novel species of the genus Mesorhizobium, for which the name Mesorhizobium alexandrii sp. nov. is proposed. The type strain is Z1-4T (= KCTC 72512T = CCTCC AB 2019101T).


Subject(s)
Dinoflagellida/microbiology , Mesorhizobium/classification , Mesorhizobium/isolation & purification , Microbiota , Phylogeny , Seawater/microbiology , Bacterial Typing Techniques , Base Composition , DNA, Bacterial/genetics , Fatty Acids/analysis , Genes, Bacterial , Mesorhizobium/genetics , Mesorhizobium/physiology , Nucleic Acid Hybridization , Quinones , RNA, Ribosomal, 16S/genetics
6.
BMC Plant Biol ; 17(1): 206, 2017 Nov 20.
Article in English | MEDLINE | ID: mdl-29157222

ABSTRACT

BACKGROUND: A recently discovered tea [Camellia sinensis (L.) O. Kuntze] cultivar can generate tender shoots in winter. We performed comparative proteomics to analyze the differentially accumulated proteins between winter and spring tender shoots of this clonal cultivar to reveal the physiological basis of its evergrowing character during winter. RESULTS: We extracted proteins from the winter and spring tender shoots (newly formed two leaves and a bud) of the evergrowing tea cultivar "Dongcha11" respectively. Thirty-three differentially accumulated high-confidence proteins were identified by matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF / TOF MS). Among these, 24 proteins had increased abundance while nine showed were decreased abundance in winter tender shoots as compared with the spring tender shoots. We categorized the differentially accumulated proteins into eight critical biological processes based on protein function annotation including photosynthesis, cell structure, protein synthesis & destination, transporters, metabolism of sugars and polysaccharides, secondary metabolism, disease/defense and proteins with unknown functions. Proteins with increased abundance in winter tender shoots were mainly related to the processes of photosynthesis, cytoskeleton and protein synthesis, whereas those with decreased abundance were correlated to metabolism and the secondary metabolism of polyphenolic flavonoids. Biochemical analysis showed that the total contents of soluble sugar and amino acid were higher in winter tender shoots while tea polyphenols were lower as compared with spring tender shoots. CONCLUSIONS: Our study suggested that the simultaneous increase in the abundance of photosynthesis-related proteins rubisco, plastocyanin, and ATP synthase delta chain, metabolism-related proteins eIF4 and protease subunits, and the cytoskeleton-structure associated proteins phosphatidylinositol transfer protein and profilin may be because of the adaptation of the evergrowing tea cultivar "Dongcha11" to low temperature and light conditions. Histone H4, Histone H2A.1, putative In2.1 protein and protein lin-28 homologs may also regulate the development of winter shoots and their response to adverse conditions.


Subject(s)
Camellia sinensis/growth & development , Plant Shoots/physiology , Proteomics/methods , Camellia sinensis/physiology , Electrophoresis, Gel, Two-Dimensional , Light , Mass Spectrometry , Photosynthesis/physiology , Plant Proteins/analysis , Plant Proteins/physiology , Plant Shoots/chemistry , Real-Time Polymerase Chain Reaction , Seasons , Temperature
7.
J Hazard Mater ; 293: 112-21, 2015 Aug 15.
Article in English | MEDLINE | ID: mdl-25855568

ABSTRACT

Highly ordered iron, nitrogen, and fluorine tri-doped TiO2 (Fe, (N, F)-TiO2) nanotube arrays were successfully synthesized by a facile one-step electrochemical method in an NH4F electrolyte containing Fe ions. The morphology, structure, composition, and photoelectrochemical property of the as-prepared nanotube arrays were characterized by various methods. The photoactivities of the samples were evaluated by the degradation of phenol in an aqueous solution under visible light. Tri-doped TiO2 showed higher photoactivities than undoped TiO2 under visible light. The optimum Fe(3+) doping amount at 0.005M exhibited the highest photoactivity and exceeded that of undoped TiO2 by a factor of 20 times under visible light. The formation of N 2p level near the valence band (VB) contributed to visible light absorption. Doping fluorine and appropriate Fe(3+) ions reduced the photogenerated electrons-holes recombination rate and enhanced visible light photoactivity. The X-ray photoelectron spectroscopy (XPS) and Fourier transform infrared spectroscopy (FTIR) results indicated the presence of synergistic effects in Fe, N, and F tri-doped TiO2, which enhanced visible light photoactivity. The Fe, (N, F)-TiO2 photocatalyst exhibited high stability.


Subject(s)
Fluorine/chemistry , Iron/chemistry , Light , Nanotubes , Nitrogen/chemistry , Titanium , Electrochemical Techniques , Microscopy, Electron, Scanning , Nanotubes/chemistry , Nanotubes/radiation effects , Nanotubes/ultrastructure , Phenol/chemistry , Photolysis , Titanium/chemistry , Titanium/radiation effects , Water Pollutants, Chemical/chemistry
8.
Environ Sci Pollut Res Int ; 21(12): 7737-45, 2014 Jun.
Article in English | MEDLINE | ID: mdl-24627203

ABSTRACT

A new method for the degradation of bisphenol A (BPA) in aqueous solution was developed. The oxidative degradation characteristics of BPA in a heterogeneous Fenton reaction catalyzed by Fe3O4/graphite oxide (GO) were studied. Transmission electron microscopic images showed that the Fe3O4 nanoparticles were evenly distributed and were ∼6 nm in diameter. Experimental results suggested that BPA conversion was affected by several factors, such as the loading amount of Fe3O4/GO, pH, and initial H2O2 concentration. In the system with 1.0 g L(-1) of Fe3O4/GO and 20 mmol L(-1) of H2O2, almost 90% of BPA (20 mg L(-1)) was degraded within 6 h at pH 6.0. Based on the degradation products identified by GC-MS, the degradation pathways of BPA were proposed. In addition, the reused catalyst Fe3O4/GO still retained its catalytic activity after three cycles, indicating that Fe3O4/GO had good stability and reusability. These results demonstrated that the heterogeneous Fenton reaction catalyzed by Fe3O4/GO is a promising advanced oxidation technology for the treatment of wastewater containing BPA.


Subject(s)
Benzhydryl Compounds/chemistry , Ferrosoferric Oxide/chemistry , Graphite/chemistry , Hydrogen Peroxide/chemistry , Iron/chemistry , Nanocomposites/chemistry , Oxides/chemistry , Phenols/chemistry , Wastewater/chemistry , Adsorption , Catalysis , Hydrogen-Ion Concentration , Oxidation-Reduction
9.
Sci Rep ; 3: 2318, 2013.
Article in English | MEDLINE | ID: mdl-23897131

ABSTRACT

Recently, a highly dangerous bird flu has infected over 130 patients in China, and the outbreak was attributed to a novel avian-origin H7N9 virus. Here, we performed a systematic analysis of the virus. We clarified the controversial viewpoint on neuraminidase (NA) origin and confirmed it was reassorted from Korean wild birds with higher confidence, whereas common ancestors of pathogenic H7N9 genes existed only one or two years ago. Further analysis of NA sequences suggested that most variations are not drug resistant and current drugs are still effective for the therapy. We also identified a potentially optimal 9-mer epitope, which can be helpful for vaccine development. The interaction of hemagglutinin (HA) and human receptor analog was confirmed by structural modeling, while NA might influence cellular processes through a PDZ-binding motif. A simplified virus infection model was proposed. Taken together, our studies provide a better understanding of the newly reassorted H7N9 viruses.


Subject(s)
Influenza A Virus, H7N9 Subtype/physiology , Influenza, Human/epidemiology , Amino Acid Motifs , Amino Acid Sequence , Amino Acid Substitution , Animals , Antiviral Agents/chemistry , Antiviral Agents/metabolism , Antiviral Agents/pharmacology , Binding Sites , China , Codon , Drug Resistance, Viral , Epitopes/chemistry , Epitopes/immunology , Genetic Variation , HLA-B Antigens/chemistry , HLA-B Antigens/metabolism , Hemagglutinin Glycoproteins, Influenza Virus/chemistry , Hemagglutinin Glycoproteins, Influenza Virus/genetics , Humans , Influenza A Virus, H7N9 Subtype/drug effects , Influenza Vaccines/immunology , Influenza, Human/transmission , Models, Biological , Models, Molecular , Molecular Docking Simulation , Molecular Sequence Data , Neuraminidase/chemistry , Neuraminidase/genetics , Peptides/chemistry , Peptides/immunology , Phylogeny , Protein Binding , Protein Conformation , Receptors, Antigen, T-Cell/chemistry , Receptors, Antigen, T-Cell/metabolism , Virulence
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