42 research outputs found
Π Π°Π·ΡΠ°Π±ΠΎΡΠΊΠ° ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΡ ΡΠ²Π΅ΡΠ΄ΠΎΠΉ Π΄ΠΎΠ·ΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΉ Π»Π΅ΠΊΠ°ΡΡΡΠ²Π΅Π½Π½ΠΎΠΉ ΡΠΎΡΠΌΡ ΠΡΠ°ΠΌΠΈΡΠΈΠ΄ΠΈΠ½Π° Π‘ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ Π²Π»Π°ΠΆΠ½ΠΎΠΉ Π³ΡΠ°Π½ΡΠ»ΡΡΠΈΠΈ Π²ΠΎ Π²Π·Π²Π΅ΡΠ΅Π½Π½ΠΎΠΌ ΡΠ»ΠΎΠ΅
Π Π°Π±ΠΎΡΠ° ΠΏΠΎΡΠ²ΡΡΠ΅Π½Π° ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ ΠΏΡΠΎΡΠ΅ΡΡΠ° Π³ΡΠ°Π½ΡΠ»ΡΡΠΈΠΈ ΠΏΠ΅ΠΏΡΠΈΠ΄Π½ΠΎΠ³ΠΎ Π°Π½ΡΠΈΠ±ΠΈΠΎΡΠΈΠΊΠ° Ρ Π±Π΅ΡΠ°-ΡΠΈΠΊΠ»ΠΎΠ΄Π΅ΠΊΡΡΡΠΈΠ½ΠΎΠΌ Π²ΠΎ Π²Π·Π²Π΅ΡΠ΅Π½Π½ΠΎΠΌ ΡΠ»ΠΎΠ΅. ΠΠΎΠ»ΡΡΠ΅Π½ ΠΈ ΠΎΡ
Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΠ·ΠΎΠ²Π°Π½ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡ Π²ΠΊΠ»ΡΡΠ΅Π½ΠΈΡ Π°Π½ΡΠΈΠ±ΠΈΠΎΡΠΈΠΊΠ° Ρ Π±Π΅ΡΠ°-ΡΠΈΠΊΠ»ΠΎΠ΄Π΅ΠΊΡΡΡΠΈΠ½ΠΎΠΌ. ΠΠ·ΡΡΠ΅Π½Ρ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΡ, Π²Π»ΠΈΡΡΡΠΈΠ΅ Π½Π° ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΏΡΠΎΡΠ΅ΡΡΠ° ΠΈΠ½ΠΊΠ°ΠΏΡΡΠ»ΡΡΠΈΠΈ. ΠΠ½Π°Π»ΠΈΠ· Π²ΡΡΠ²ΠΎΠ±ΠΎΠΆΠ΄Π΅Π½ΠΈΡ ΠΏΠΎΠΊΠ°Π·Π°Π» ΡΠ°ΡΡΠ²ΠΎΡΠΈΠΌΠΎΡΡΡ Π³ΡΠ°ΠΌΠΈΡΠΈΠ΄ΠΈΠ½Π° Π‘ Π² Π²ΠΎΠ΄Π½ΠΎΠΌ ΡΠ°ΡΡΠ²ΠΎΡΠ΅. Π ΡΠ°Π±ΠΎΡΠ΅ Π±ΡΠ»ΠΈ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½Ρ ΡΠ΅Ρ
Π½ΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠ²ΠΎΠΉΡΡΠ²Π° ΡΠΌΠ΅ΡΠΈ ΠΈ ΡΠ²ΠΎΠΉΡΡΠ²Π° ΡΠ°Π±Π»Π΅ΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΉ ΡΠΎΡΠΌΡ. Π Π°Π·ΡΠ°Π±ΠΎΡΠ°Π½Π° ΡΠ΅Ρ
Π½ΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠ°Ρ ΡΡ
Π΅ΠΌΠ° ΠΏΡΠΎΠΈΠ·Π²ΠΎΠ΄ΡΡΠ²Π°.In this study granulation of a peptide antibiotic with beta-cyclodextrin in bed fluidization was investigated. The inclusion complex of antibiotic with beta-cyclodextrin was obtained and characterized. The parameters of granulation affecting on encapsulation process were studied. A release analysis showed the solubility of gramicidin S in aqueous solution. The processability of the mixture was investigated and the property of the bulk product was analyzed. The technological scheme of production is developed
Human metapneumovirus driven IFN-Ξ² production antagonizes macrophage transcriptional induction of IL1-Ξ² in response to bacterial pathogens
Human metapneumovirus (HMPV) is a pneumovirus that may cause severe respiratory disease in humans. HMPV infection has been found to increase susceptibility to bacterial superinfections leading to increased morbidity and mortality. The molecular mechanisms underlying HMPV-mediated increase in bacterial susceptibility are poorly understood and largely understudied. Type I interferons (IFNs), while critical for antiviral defenses, may often have detrimental effects by skewing the host immune response and cytokine output of immune cells. It is currently unknown if HMPV skews the inflammatory response in human macrophages triggered by bacterial stimuli. Here we report that HMPV pre-infection impacts production of specific cytokines. HMPV strongly suppresses IL-1Ξ² transcription in response to LPS or heat-killed Pseudomonas aeruginosa and Streptococcus pneumonia, while enhancing mRNA levels of IL-6, TNF-Ξ± and IFN-Ξ². We demonstrate that in human macrophages the HMPV-mediated suppression of IL-1Ξ² transcription requires TANK-binding kinase 1 (TBK1) and signaling via the IFN-Ξ²-IFNAR axis. Interestingly, our results show that HMPV pre-infection did not impair the LPS-stimulated activation of NF-ΞΊB and HIF-1Ξ±, transcription factors that stimulate IL-1Ξ² mRNA synthesis in human cells. Furthermore, we determined that sequential HMPV-LPS treatment resulted in accumulation of the repressive epigenetic mark H3K27me3 at the IL1B promoter. Thus, for the first time we present data revealing the molecular mechanisms by which HMPV shapes the cytokine output of human macrophages exposed to bacterial pathogens/LPS, which appears to be dependent on epigenetic reprogramming at the IL1B promoter leading to reduced synthesis of IL-1Ξ². These results may improve current understanding of the role of type I IFNs in respiratory disease mediated not only by HMPV, but also by other respiratory viruses that are associated with superinfections.</p
Human metapneumovirus driven IFN-Ξ² production antagonizes macrophage transcriptional induction of IL1-Ξ² in response to bacterial pathogens
Human metapneumovirus (HMPV) is a pneumovirus that may cause severe respiratory disease in humans. HMPV infection has been found to increase susceptibility to bacterial superinfections leading to increased morbidity and mortality. The molecular mechanisms underlying HMPV-mediated increase in bacterial susceptibility are poorly understood and largely understudied. Type I interferons (IFNs), while critical for antiviral defenses, may often have detrimental effects by skewing the host immune response and cytokine output of immune cells. It is currently unknown if HMPV skews the inflammatory response in human macrophages triggered by bacterial stimuli. Here we report that HMPV pre-infection impacts production of specific cytokines. HMPV strongly suppresses IL-1Ξ² transcription in response to LPS or heat-killed Pseudomonas aeruginosa and Streptococcus pneumonia, while enhancing mRNA levels of IL-6, TNF-Ξ± and IFN-Ξ². We demonstrate that in human macrophages the HMPV-mediated suppression of IL-1Ξ² transcription requires TANK-binding kinase 1 (TBK1) and signaling via the IFN-Ξ²-IFNAR axis. Interestingly, our results show that HMPV pre-infection did not impair the LPS-stimulated activation of NF-ΞΊB and HIF-1Ξ±, transcription factors that stimulate IL-1Ξ² mRNA synthesis in human cells. Furthermore, we determined that sequential HMPV-LPS treatment resulted in accumulation of the repressive epigenetic mark H3K27me3 at the IL1B promoter. Thus, for the first time we present data revealing the molecular mechanisms by which HMPV shapes the cytokine output of human macrophages exposed to bacterial pathogens/LPS, which appears to be dependent on epigenetic reprogramming at the IL1B promoter leading to reduced synthesis of IL-1Ξ². These results may improve current understanding of the role of type I IFNs in respiratory disease mediated not only by HMPV, but also by other respiratory viruses that are associated with superinfections
The PeptideAtlas project
The completion of the sequencing of the human genome and the concurrent, rapid development of high-throughput proteomic methods have resulted in an increasing need for automated approaches to archive proteomic data in a repository that enables the exchange of data among researchers and also accurate integration with genomic data. PeptideAtlas (http://www.peptideatlas.org/) addresses these needs by identifying peptides by tandem mass spectrometry (MS/MS), statistically validating those identifications and then mapping identified sequences to the genomes of eukaryotic organisms. A meaningful comparison of data across different experiments generated by different groups using different types of instruments is enabled by the implementation of a uniform analytic process. This uniform statistical validation ensures a consistent and high-quality set of peptide and protein identifications. The raw data from many diverse proteomic experiments are made available in the associated PeptideAtlas repository in several formats. Here we present a summary of our process and details about the Human, Drosophila and Yeast PeptideAtlas build
The PeptideAtlas project
The completion of the sequencing of the human genome and the concurrent, rapid development of high-throughput proteomic methods have resulted in an increasing need for automated approaches to archive proteomic data in a repository that enables the exchange of data among researchers and also accurate integration with genomic data. PeptideAtlas () addresses these needs by identifying peptides by tandem mass spectrometry (MS/MS), statistically validating those identifications and then mapping identified sequences to the genomes of eukaryotic organisms. A meaningful comparison of data across different experiments generated by different groups using different types of instruments is enabled by the implementation of a uniform analytic process. This uniform statistical validation ensures a consistent and high-quality set of peptide and protein identifications. The raw data from many diverse proteomic experiments are made available in the associated PeptideAtlas repository in several formats. Here we present a summary of our process and details about the Human, Drosophila and Yeast PeptideAtlas builds
The Drosophila melanogaster PeptideAtlas facilitates the use of peptide data for improved fly proteomics and genome annotation
<p>Abstract</p> <p>Background</p> <p>Crucial foundations of any quantitative systems biology experiment are correct genome and proteome annotations. Protein databases compiled from high quality empirical protein identifications that are in turn based on correct gene models increase the correctness, sensitivity, and quantitative accuracy of systems biology genome-scale experiments.</p> <p>Results</p> <p>In this manuscript, we present the <it>Drosophila melanogaster </it>PeptideAtlas, a fly proteomics and genomics resource of unsurpassed depth. Based on peptide mass spectrometry data collected in our laboratory the portal <url>http://www.drosophila-peptideatlas.org</url> allows querying fly protein data observed with respect to gene model confirmation and splice site verification as well as for the identification of proteotypic peptides suited for targeted proteomics studies. Additionally, the database provides consensus mass spectra for observed peptides along with qualitative and quantitative information about the number of observations of a particular peptide and the sample(s) in which it was observed.</p> <p>Conclusion</p> <p>PeptideAtlas is an open access database for the <it>Drosophila </it>community that has several features and applications that support (1) reduction of the complexity inherently associated with performing targeted proteomic studies, (2) designing and accelerating shotgun proteomics experiments, (3) confirming or questioning gene models, and (4) adjusting gene models such that they are in line with observed <it>Drosophila </it>peptides. While the database consists of proteomic data it is not required that the user is a proteomics expert.</p