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396 results on '"Forrest, Lucy R."'

4. Intestinal serotonin and fluoxetine exposure modulate bacterial colonization in the gut

Author

Fung, Thomas C, Vuong, Helen E, Luna, Cristopher DG, Pronovost, Geoffrey N, Aleksandrova, Antoniya A, Riley, Noah G, Vavilina, Anastasia, McGinn, Julianne, Rendon, Tomiko, Forrest, Lucy R, and Hsiao, Elaine Y

Subjects
Microbiology, Biological Sciences, Genetics, Prevention, Depression, Digestive Diseases, Nutrition, Mental Health, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, Underpinning research, Aetiology, Oral and gastrointestinal, Infection, Administration, Oral, Animals, Bacteria, Feces, Female, Firmicutes, Fluoxetine, Gastrointestinal Microbiome, Genetic Variation, Host Microbial Interactions, Intestines, Male, Mice, Mice, Inbred C57BL, Serotonin, Serotonin Receptor Agonists, Selective Serotonin Reuptake Inhibitors, Specific Pathogen-Free Organisms, Medical Microbiology
Abstract

The gut microbiota regulates levels of serotonin (5-hydroxytryptamine (5-HT)) in the intestinal epithelium and lumen1-5. However, whether 5-HT plays a functional role in bacteria from the gut microbiota remains unknown. We demonstrate that elevating levels of intestinal lumenal 5-HT by oral supplementation or genetic deficiency in the host 5-HT transporter (SERT) increases the relative abundance of spore-forming members of the gut microbiota, which were previously reported to promote host 5-HT biosynthesis. Within this microbial community, we identify Turicibacter sanguinis as a gut bacterium that expresses a neurotransmitter sodium symporter-related protein with sequence and structural homology to mammalian SERT. T. sanguinis imports 5-HT through a mechanism that is inhibited by the selective 5-HT reuptake inhibitor fluoxetine. 5-HT reduces the expression of sporulation factors and membrane transporters in T. sanguinis, which is reversed by fluoxetine exposure. Treating T. sanguinis with 5-HT or fluoxetine modulates its competitive colonization in the gastrointestinal tract of antibiotic-treated mice. In addition, fluoxetine reduces the membership of T. sanguinis in the gut microbiota of conventionally colonized mice. Host association with T. sanguinis alters intestinal expression of multiple gene pathways, including those important for lipid and steroid metabolism, with corresponding reductions in host systemic triglyceride levels and inguinal adipocyte size. Together, these findings support the notion that select bacteria indigenous to the gut microbiota signal bidirectionally with the host serotonergic system to promote their fitness in the intestine.

Published
2019

20. Membrane Protein Simulations: Modelling a Complex Environment

Author

Bond, Peter J., Cuthbertson, Jonathan, Deol, Sundeep S., Forrest, Lucy R., Johnston, Jennifer, Patargias, George, Sansom, Mark S.P., Barth, Timothy J., editor, Griebel, Michael, editor, Keyes, David E., editor, Nieminen, Risto M., editor, Roose, Dirk, editor, Schlick, Tamar, editor, Leimkuhler, Benedict, editor, Chipot, Christophe, editor, Elber, Ron, editor, Laaksonen, Aatto, editor, Mark, Alan, editor, Schütte, Christoph, editor, and Skeel, Robert, editor

Published
2006
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24. Osmotic stress response in BetP: How lipids and K+ team up to overcome downregulation

Author

Heinz, Veronika, primary, Gueler, Guennur, additional, Leone, Vanessa, additional, Madej, M. Gregor, additional, Maksimov, Stanislav, additional, Gaertner, Rebecca M., additional, Rudi, Olga, additional, Hamdi, Farzad, additional, Kastritis, Panagiotis L., additional, Maentele, Werner, additional, Kraemer, Reinhard, additional, Forrest, Lucy R., additional, Perez, Camilo, additional, and Ziegler, Christine, additional

Published
2022
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32. Interpreting hydrogen-deuterium exchange experiments with molecular simulations: Tutorials and applications of the HDXer ensemble reweighting software [Article v1.0]

Author

Lee, Paul Suhwan, primary, Bradshaw, Richard T., additional, Marinelli, Fabrizio, additional, Kihn, Kyle, additional, Smith, Ally, additional, Wintrode, Patrick L., additional, Deredge, Daniel J., additional, Faraldo-Gómez, José D., additional, and Forrest, Lucy R., additional

Published
2022
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38. Interpretation of spectroscopic data using molecular simulations for the secondary active transporter BetP

Author

Robertson, Janice, Leone, Vanessa, Waclawska-Krzeminski, Izabela Jadwiga, Kossmann, Katharina, Koshy, Caroline, Sharma, Monika, Prisner, Thomas F., Ziegler, Christine, Endeward, Burkhard, Forrest, Lucy R., Robertson, Janice, Leone, Vanessa, Waclawska-Krzeminski, Izabela Jadwiga, Kossmann, Katharina, Koshy, Caroline, Sharma, Monika, Prisner, Thomas F., Ziegler, Christine, Endeward, Burkhard, and Forrest, Lucy R.

Abstract

Mechanistic understanding of dynamic membrane proteins such as transporters, receptors, and channels requires accurate depictions of conformational ensembles, and the manner in which they interchange as a function of environmental factors including substrates, lipids, and inhibitors. Spectroscopic techniques such as electron spin resonance (ESR) pulsed electron–electron double resonance (PELDOR), also known as double electron–electron resonance (DEER), provide a complement to atomistic structures obtained from x-ray crystallography or cryo-EM, since spectroscopic data reflect an ensemble and can be measured in more native solvents, unperturbed by a crystal lattice. However, attempts to interpret DEER data are frequently stymied by discrepancies with the structural data, which may arise due to differences in conditions, the dynamics of the protein, or the flexibility of the attached paramagnetic spin labels. Recently, molecular simulation techniques such as EBMetaD have been developed that create a conformational ensemble matching an experimental distance distribution while applying the minimal possible bias. Moreover, it has been proposed that the work required during an EBMetaD simulation to match an experimentally determined distribution could be used as a metric with which to assign conformational states to a given measurement. Here, we demonstrate the application of this concept for a sodium-coupled transport protein, BetP. Because the probe, protein, and lipid bilayer are all represented in atomic detail, the different contributions to the work, such as the extent of protein backbone movements, can be separated. This work therefore illustrates how ranking simulations based on EBMetaD can help to bridge the gap between structural and biophysical data and thereby enhance our understanding of membrane protein conformational mechanisms.

Published
2020

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