Project description:Comparison of Campylobacter proteome in MH media with and without deoxycholic acid, in presence of FBS or after being exposed to INT 407 and Caco2 intestinal epithelial cells.
Project description:Many pathogenic bacteria of the family Enterobacteriaceae use type III secretion systems to inject virulence proteins, termed "effectors," into the host cell cytosol. Although host-cellular activities of several effectors have been demonstrated, the function and host-targeted pathways of most of the effectors identified to date are largely undetermined. To gain insight into host proteins targeted by bacterial effectors, we performed coaffinity purification of host proteins from cell lysates using recombinant effectors from the Enterobacteriaceae intracellular pathogens Salmonella enterica serovar Typhimurium and Citrobacter rodentium. We identified 54 high-confidence host interactors for the Salmonella effectors GogA, GtgA, GtgE, SpvC, SrfH, SseL, SspH1, and SssB collectively and 21 interactors for the Citrobacter effectors EspT, NleA, NleG1, and NleK. We biochemically validated the interaction between the SrfH Salmonella protein and the extracellular signal-regulated kinase 2 (ERK2) host protein kinase, which revealed a role for this effector in regulating phosphorylation levels of this enzyme, which plays a central role in signal transduction. IMPORTANCE During infection, pathogenic bacteria face an adverse environment of factors driven by both cellular and humoral defense mechanisms. To help evade the immune response and ultimately proliferate inside the host, many bacteria evolved specialized secretion systems to deliver effector proteins directly into host cells. Translocated effector proteins function to subvert host defense mechanisms. Numerous pathogenic bacteria use a specialized secretion system called type III secretion to deliver effectors into the host cell cytosol. Here, we identified 75 new host targets of Salmonella and Citrobacter effectors, which will help elucidate their mechanisms of action.
Project description:Utilized sensitive, high throughput multiplexed ion mobility-mass spectrometry (IM-MS) to characterize the serum proteome of tuberculosis patients prior to and at 8 weeks of antibiotic treatment. Goal is to identify a serum protein signature indicative of treatment effect.
Project description:Data includes proteomics analysis of P450-ABP (2EN, ATW8, ATW12), FP-2, and ATP-ABP labeled mouse lung lysate S9. Lungs from the following developmental stages were used in the study: gestational day 17, post natal days 0, 21, and 42. Also included are global analyses of the same mice lungs.
Project description:Proteomic data from mouse lung; Treated with wild-type and mutant H7N9 and mockulum; Time points 1, 2, 4 & 7 days; 5 biological replicates
Project description:Ischemia/Reperfusion (I/R) results in altered metabolic and molecular responses. Phosphorylation, a posttranslational modification, is one of the most noted regulatory mechanisms and differential phosphorylation affects numerous regulatory and signaling mechanisms. To further understand the phosphoproteomic changes that occur in the heart during I/R we utilized iTRAQ-based quantitative proteomic and LC-MS/MS techniques to obtain a profile of phosphopeptides expressed under control and I/R conditions. A total of 1896 phosphopeptides were identified, and 116 were assessed as significant. The 116 phosphopeptides represented 87 unique proteins. Analysis of the phosphopeptides using Motif-x identified 2 predominant motifs: arginine and proline-directed serine phosphorylation sites. Two proteins known to be altered by I/R were among the dataset obtained, phospholamban and pyruvate dehydrogenase, and were used to confirm validity of the profile. Functional characterization of the phosphopetides identified in this study could lead to further understanding of the signaling mechanisms involved during I/R damage in the heart, as well as identifying new areas to target therapeutic strategies.
Project description:Characterization of proteins critical to fungal cellulosome assembly for Anaeromyces robustus, Neocallimastix californiae and Piromyces finnis (cellulosomes are multi-protein complexes that tether plant biomass degrading enzymes together). These findings suggest that the fungal cellulosome is an independently evolved fungal complex that co-opted useful activities from bacterial neighbors within the herbivore rumen microbiome.
Project description:Micromonas implements a sustained non-photochemical quenching response to phosphate limitation, driven by light harvesting family protein LHCSR. This protein, allows stable growth under P-limitation and increased growth without major LCH adjustment as phosphate becomes more available. Proteomics results show this alga integrates unique strategies to optimize growth under dynamic ocean nutrient conditions.