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1.
Front Microbiol ; 14: 1303979, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-38143871

RESUMO

Arbuscular mycorrhizal fungi (AMF) have demonstrated the potential to enhance the saline-alkali tolerance in plants. Nevertheless, the extent to which AMF can ameliorate the tolerance of salt-sensitive plants to alkaline conditions necessitates further investigation. The current study is primarily centered on elucidating the impact of AMF on the growth of the Huayu22 (H22) when cultivated in saline-alkaline soil. We leveraged DNA of rhizosphere microorganisms extracted from saline-alkali soil subjected to AMF treatment and conducted high-throughput sequencing encompassing 16S rRNA gene and ITS sequencing. Our findings from high-throughput sequencing unveiled Proteobacteria and Bacillus as the prevailing phylum and genus within the bacterial population, respectively. Likewise, the predominant fungal phylum and genus were identified as Ascomycota and Haematonectria. It is noteworthy that the relative abundance of Proteobacteria, Actinobacteria, Chloroflexi, Bacteroidetes, and Ascomycota exhibited significant increments subsequent to AMF inoculation. Our investigation into soil enzyme activity revealed a remarkable surge post-AMF inoculation. Notably, the amounts of pathogen growth inhibitory enzymes and organic carbon degrading enzymes rise, as predicted by the putative roles of microbial communities. In saline-alkali soil, inoculation of AMF did boost the yield of H22. Notable improvements were observed in the weight of both 100 fruits and 100 grains, which increased by 20.02% and 22.30%, respectively. Conclusively, this study not only provides a theoretical framework but also furnishes empirical evidence supporting the utilization of AMF as a viable strategy for augmenting the yield of salt-sensitive plants grown in alkaline conditions.

2.
Clin. transl. oncol. (Print) ; 25(6): 1522-1544, jun. 2023. ilus
Artigo em Inglês | IBECS | ID: ibc-221188

RESUMO

This study reviews newly discovered insect peptide point mutations as new possible cancer research targets. To interpret newly discovered peptide point mutations in insects as new possible cancer research targets, we focused on the numerous peptide changes found in the ‘CSP’ family on the sex pheromone gland of the female silkworm moth Bombyx mori. We predict that the Bombyx peptide modifications will have a significant effect on cancer CUP (cancers of unknown primary) therapy and that bacterial peptide editing techniques, specifically Lactobacillus combined to CRISPR, will be used to regulate ribosomes and treat cancer in humans (AU)


Assuntos
Humanos , Animais , Feminino , Bombyx , Neoplasias/genética , Neoplasias/terapia , Lactobacillus , Peptídeos , Ribossomos/genética
3.
Clin Transl Oncol ; 25(6): 1522-1544, 2023 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-36694080

RESUMO

This study reviews newly discovered insect peptide point mutations as new possible cancer research targets. To interpret newly discovered peptide point mutations in insects as new possible cancer research targets, we focused on the numerous peptide changes found in the 'CSP' family on the sex pheromone gland of the female silkworm moth Bombyx mori. We predict that the Bombyx peptide modifications will have a significant effect on cancer CUP (cancers of unknown primary) therapy and that bacterial peptide editing techniques, specifically Lactobacillus combined to CRISPR, will be used to regulate ribosomes and treat cancer in humans.


Assuntos
Bombyx , Neoplasias , Animais , Feminino , Humanos , Bombyx/genética , Peptídeos , Ribossomos/genética , Neoplasias/genética , Neoplasias/terapia
4.
Sci Rep ; 10(1): 19476, 2020 11 10.
Artigo em Inglês | MEDLINE | ID: mdl-33173074

RESUMO

High-throughput farming of animals for an essential purpose such as large scale health and production of hogs is a challenge for the food industry in the modern world. The problem is that the breeding of livestock for fast growth or high yields of meat is often associated with illness and microbial infection that develop under the breeding conditions. Piglet diarrhea is most common pig disease, leading to heavy mortality and thereby economic loss. We proved that chemical drugs can relieve the symptoms of diarrhea in ill piglets, but they do not treat the underlying cause, i.e. significantly altered bacterial gut flora. Using Illumina sequencing of fecal DNA, we showed that the bacterial gut flora of piglets treated with antibiotics remain close to the ill conditions. However, using Illumina sequencing of fecal DNA from piglets treated with a specific Bacillus (Bacillus subtilis Y-15, B. amyloliquefaciens DN6502 and B. licheniformis SDZD02) demonstrated the efficiency of natural bioproducts not only on curing diarrhea, but also on beneficial bacteria to re-establish in the piglet gut. We therefore propose a new natural "medicine" to be explored by the world farm animal agriculture industry, particularly for sustainable improvement of swine livestock production and health.


Assuntos
Antibacterianos/administração & dosagem , Bacillus subtilis/fisiologia , Bacillus/fisiologia , Diarreia/terapia , Probióticos/administração & dosagem , Doenças dos Suínos/terapia , Ração Animal/análise , Animais , Bacillus/metabolismo , Bacillus subtilis/metabolismo , Bactérias/classificação , Bactérias/efeitos dos fármacos , Bactérias/genética , Cruzamento/métodos , Diarreia/microbiologia , Fezes/microbiologia , Sequenciamento de Nucleotídeos em Larga Escala/métodos , Microbiota/genética , Probióticos/metabolismo , RNA Ribossômico 16S/genética , Suínos , Doenças dos Suínos/microbiologia
5.
PLoS One ; 10(3): e0121108, 2015.
Artigo em Inglês | MEDLINE | ID: mdl-25815820

RESUMO

The relationship between salt bridges and stability/enzymatic activity is unclear. We studied this relationship by systematic alanine-scanning mutation analysis using the typical M4 family metalloprotease Pseudomonas aeruginosa elastase (PAE, also known as pseudolysin) as a model. Structural analysis revealed seven salt bridges in the PAE structure. We constructed ten mutants for six salt bridges. Among these mutants, six (Asp189Ala, Arg179Ala, Asp201Ala, Arg205Ala, Arg245Ala and Glu249Ala) were active and four (Asp168Ala, Arg198Ala, Arg253Ala, and Arg279Ala) were inactive. Five mutants were purified, and their catalytic efficiencies (kcat/Km), half-lives (t1/2) and thermal unfolding curves were compared with those of PAE. Mutants Asp189Ala and Arg179Ala both showed decreased thermal stabilities and increased activities, suggesting that the salt bridge Asp189-Arg179 stabilizes the protein at the expense of catalytic efficiency. In contrast, mutants Asp201Ala and Arg205Ala both showed slightly increased thermal stability and slightly decreased activity, suggesting that the salt bridge Asp201-Arg205 destabilizes the protein. Mutant Glu249Ala is related to a C-terminal salt bridge network and showed both decreased thermal stability and decreased activity. Furthermore, Glu249Ala showed a thermal unfolding curve with three discernable states [the native state (N), the partially unfolded state (I) and the unfolded state (U)]. In comparison, there were only two discernable states (N and U) in the thermal unfolding curve of PAE. These results suggest that Glu249 is important for catalytic efficiency, stability and unfolding cooperativity. This study represents a systematic mutational analyses of salt bridges in the model metalloprotease PAE and provides important insights into the structure-function relationship of enzymes.


Assuntos
Elastase Pancreática/química , Conformação Proteica , Pseudomonas aeruginosa/enzimologia , Relação Estrutura-Atividade , Alanina/química , Alanina/genética , Catálise , Estabilidade Enzimática , Mutagênese Sítio-Dirigida , Elastase Pancreática/genética , Pseudomonas aeruginosa/patogenicidade , Sais/química
6.
Wei Sheng Wu Xue Bao ; 50(9): 1258-63, 2010 Sep.
Artigo em Chinês | MEDLINE | ID: mdl-21090268

RESUMO

OBJECTIVE: We expressed mature chicken interleukin-18 (mChIL-18) in Pichia pastoris. METHODS: The mChIL-18 gen was reconstructed by using site-specific mutagenesis based on the Pichia pastoris-preferred codons. The recombinant plasmid pPIC9K/mChIL-18 was constructed and transformed to Pichia pastoris GS115 by electroperation. Multi-copy recombinant strains were screened by Geneticin (G418). The expression of mChIL-18 protein was induced by methanol. SDS-PAGE and Western-blot were used to analyze the expressed products. The bioactivity of mChIL-18 was measured by methyl thiazolyl tetrazolium assays and chicken embryo fibroblasts-vesicular stomatitis virus (CEF-VSV) system. RESULTS: The protein of mChIL-18 could be secreted by GS115. The optimum expression conditions, a rate of 480 mg/L,were obtained as follows:temperature 28 degrees C, pH 6.5, methanol concentration 2% and expression time 120 h. The obtained mChIL-18 protein could stimulate T lymphocytes proliferation. IFN-gamma induced by mChIL-18 could directly inhibit the growth of VSV in CEF,and its antiviral activity was about 1.7 x 10(4) U/mL which was produced by 400 microg/L of mChIL-18. CONCLUSION: The high expression of bioactive recombinant mature chicken interleukin-18 (mChiL-18) in Pichia pastoris had been achieved.


Assuntos
Interleucina-18/metabolismo , Proteínas Mutantes/metabolismo , Pichia/metabolismo , Animais , Western Blotting , Galinhas , Eletroforese em Gel de Poliacrilamida , Interleucina-18/genética , Proteínas Mutantes/genética , Pichia/genética
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