scholarly journals TMT-Based Quantitative Proteomic Analysis of Intestinal Organoids Infected by Listeria monocytogenes with Different Virulence

2020 ◽  
Author(s):  
Jie Huang ◽  
Cong Zhou ◽  
Guanghong Zhou ◽  
Keping Ye
Keyword(s):  
Listeria Monocytogenes ◽  
Proteomic Analysis ◽  
High Performance ◽  
Virulent Strain ◽  
Cellular Protein ◽  
Quantitative Proteomic Analysis ◽  
Intestinal Organoids ◽  
Food Borne ◽  
Differential Proteins ◽  
Fold Change Cutoff

AbstractListeria monocytogenes (Lm) is an opportunistic food-borne pathogen that cause listeriosis. L. monocytogenes belonged to different serovars presents with different virulence in the host and caused different host reactions. To investigate the remodeling of host proteome by differently toxic strains, the cellular protein responses of intestinal organoids were analyzed using TMT labeling and high performance liquid chromatography-mass spectrometry. Quantitative proteomic analysis revealed 6564 differentially expressed proteins, of which 5591 proteins were quantified. The fold-change cutoff was set at 1.3 (Lm vs control), the virulent strain caused 102 up-regulated proteins and 52 down-regulated proteins, while the low virulent strain caused 188 up-regulated proteins and 25 down-regulated proteins. These identified proteins were involved in the regulation of essential processes such as biological metabolism, energy metabolism, and immune system process. Some selected proteins were screened by Real-time PCR and Western blotting. These results revealed that differently toxic L. monocytogenes induced similar biological functions and immune responses while had different regulation on differential proteins in the pathway.

scholarly journals A SILAC-Based Method for Quantitative Proteomic Analysis of Intestinal Organoids

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Alexis Gonneaud ◽  
Christine Jones ◽  
Naomie Turgeon ◽  
Dominique Lévesque ◽  
Claude Asselin ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Quantitative Proteomic Analysis ◽  
Intestinal Organoids

scholarly journals Quantitative Proteomic Analysis of Duck Embryo Fibroblasts Infected With Novel Duck Reovirus

2020 ◽  
Vol 7 ◽  
Author(s):  
Yudong Yang ◽  
Lin Li ◽  
Xingpo Liu ◽  
Meijie Jiang ◽  
Jun Zhao ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Cellular Protein ◽  
Economic Losses ◽  
The Novel ◽  
Quantitative Proteomic Analysis ◽  
Interferon Stimulated Genes ◽  
Proteomic Data ◽  
Pekin Ducks ◽  
Duck Embryo ◽  
Embryo Fibroblasts

The novel duck reovirus (NDRV) can cause hemorrhage and necrosis on the spleen of Pekin ducks; this disease has resulted in great economic losses to the duck industry. However, the molecular pathogenesis of NDRV remains poorly understood. In the current study, the quantitative proteomic analysis of NDRV-infected duck embryo fibroblasts was performed to explore the cellular protein changes in response to viral infection through iTRAQ coupled with the liquid chromatography (LC)–tandem mass spectrometry (MS/MS) method. A total of 6,137 proteins were obtained in cell samples at 24 h post-infection. Of these, 179 differentially expressed proteins (DEPs) were identified (cutoff set to 1.5-fold change), including 89 upregulated and 90 downregulated proteins. Bioinformatics analysis showed that DEPs can be divided into the cellular component, molecular function, and biological process; they were mainly involved in signal transduction, infectious diseases, cell growth and death, and the immune system. The subcellular localization of most proteins was in the cytoplasm. Importantly, the expressions of signal transducer and activator of transcription 1 (STAT1) and various interferon-stimulated genes (ISGs) were upregulated after NDRV infection. The mRNA transcripts of some ISGs were consistent with proteomic data, showing an increased trend. Results of our study suggested that NDRV infection can elicit strong expression changes of cellular proteins and activate the expression of ISGs from the point of quantitative proteomic analysis. The study provides a new insight into the understanding of NDRV pathogenesis.

scholarly journals Refinement of the Listeria monocytogenes σB regulon through quantitative proteomic analysis

Microbiology ◽  
2013 ◽  
Vol 159 (Pt_6) ◽  
pp. 1109-1119 ◽  
Author(s):  
S. Mujahid ◽  
R. H. Orsi ◽  
P. Vangay ◽  
K. J. Boor ◽  
M. Wiedmann
Keyword(s):  
Listeria Monocytogenes ◽  
Proteomic Analysis ◽  
Quantitative Proteomic Analysis

scholarly journals Quantitative Proteomic Analysis of Cellular Protein Modulation upon Inhibition of the NEDD8-Activating Enzyme by MLN4924

2011 ◽  
Vol 10 (11) ◽  
pp. M111.009183 ◽  
Author(s):  
Hua Liao ◽  
Xiaozhen J. Liu ◽  
Jonathan L. Blank ◽  
David C. Bouck ◽  
Hugues Bernard ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Cellular Protein ◽  
Quantitative Proteomic Analysis

scholarly journals Data-Independent Acquisition-Based Quantitative Proteomic Analysis of m.3243A>G MELAS Reveals Novel Potential Pathogenesis and Therapeutic Targets

2020 ◽  
Author(s):  
Xueli Chang ◽  
Wei Zhang ◽  
Chuanqiang Pu ◽  
Qiang Shi ◽  
Juan Wang ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Proteomic Analysis ◽  
Molecular Networks ◽  
Heme Oxygenase 1 ◽  
Proteomic Profiling ◽  
Quantitative Proteomic Analysis ◽  
Data Independent Acquisition ◽  
Mitochondrial Ribosome ◽  
Differential Proteins ◽  
And Gender

Abstract Background The pathogenesis of mitochondrial myopathy, encephalopathy, lactic acidosis and stroke like episodes (MELAS) syndrome is not completely understood. The m.3243A > G mutation responsible for 80% MELAS patients affects proteins with undetermined functions. Therefore, we performed quantitative proteomic analysis on skeletal muscle specimens from MELAS patients. Methods We recruited 10 patients with definitive MELAS and 10 controls matched by age and gender of MELAS patients for comparison. We performed nanospray liquid chromatography-mass spectrometry (LC-MS) based proteomic analysis in the data-independent acquisition (DIA) modes, followed by the statistical analysis to reveal the differentially expressed proteins. Results We identified 128 differential proteins between MELAS and controls, including 68 for down-regulation and 60 for up-regulation. We studied the differential proteins involved in oxidative stress and indicated a highly significant up-regulation of heat shock protein beta-1 (HSPB1), alpha-crystallin B chain (CRYAB) and heme oxygenase 1 (HMOX1) but a decrease of glucose-6-phosphate dehydrogenase (G6PD) and selenoprotein P (SEPP1). KEGG pathway analysis and gene ontology (GO) evaluation revealed that the phagosome, proliferator-activated receptors (PPAR) signaling pathway and ribosome showed significant enrichment. Conclusions The results revealed that the imbalance between oxidative stress and antioxidant defense, activation of autophagosomes and abnormal metabolism of mitochondrial ribosome proteins played an important role in m.3243A > G MELAS. The combination of proteomic profiling and bioinformatics analysis could contribute novel molecular networks to the pathogenesis of MELAS in a comprehensive manner.

scholarly journals Proteomic Analysis of Human Serum for Patients at Different Pathological Stages of Hepatic Fibrosis

2021 ◽  
Vol 2021 ◽  
pp. 1-16
Author(s):  
Kang Zhao ◽  
Jucun Huang ◽  
Hongmei Xia ◽  
Jianjun Zhang ◽  
Liming Liu
Keyword(s):  
Differential Expression ◽  
Hepatic Fibrosis ◽  
Proteomic Analysis ◽  
High Performance ◽  
Interaction Network ◽  
Go Annotation ◽  
Early Stages ◽  
Differential Proteins ◽  
Early Fibrosis ◽  
Fibrosis Staging

Background. Hepatic fibrosis is a severe liver disease that has threatened human health for a long time. In order to undergo timely and adequate therapy, it is important for patients to obtain an accurate diagnosis of fibrosis. Laboratory inspection methods have been efficient in distinguishing between advanced hepatic fibrosis stages (F3, F4), but the identification of early stages of fibrosis has not been achieved. The development of proteomics may provide us with a new direction to identify the stages of fibrosis. Methods. We established serum proteomic maps for patients with hepatic fibrosis at different stages and identified differential expression of proteins between fibrosis stages through ultra-high-performance liquid chromatography tandem mass spectrometry proteomic analysis. Results. From the proteomic profiles of the serum of patients with different stages of liver fibrosis, a total of 1,338 proteins were identified. Among three early fibrosis stages (control, F1, and F2), 55 differential proteins were identified, but no proteins simultaneously exhibited differential expression between control, F1, and F2. Differential proteins were detected in the comparison between different fibrosis stages. Significant differences were found between advanced fibrosis stages (F2-vs.-F3 and F3-vs.-F4) through a series of statistical analysis, including hierarchical clustering, Gene Ontology (GO) functional annotation, Kyoto Encyclopedia of Genes and Genomes pathway, and protein-protein interaction network analysis. The differential proteins identified by GO annotation were associated with biological processes (mainly platelet degranulation and cell adhesion), molecular functions, and cellular components. Conclusions. All potential biomarkers identified between the stages of fibrosis could be key points in determining the fibrosis staging. The differences between early stages may provide a useful reference in addressing the challenge of early fibrosis staging.

Sign in / Sign up

Export Citation Format

Share Document