ARTWORK BY OUR STUDENTS
Ana Cristina Estrada
Lab of Dr. Jeff Holmes
Alex Keller and Robyn Sherman
Lab of Dr. Brant Isakson
Molecular Physiology and Biophysics
Lab of Dr. Richard Price
Lab of Dr. Douglas W. Desimone
WHAT’S NEW WITH OUR STUDENTS?
Awards and Fellowships:
Congratulations: 2016 Wagner Fellowship Awardees
We are thrilled to announce that the Wagner Fellowship fund was able to support 12 BIMS students this year due to the incredible generosity of Dr. Robert Wagner and his wife Mary. Dr. Wagner served as Professor and Chair of Microbiology from 1967-1994 and contributed in so many ways to the School of Medicine, UVA, and the scientific community at large. These fellowships are a lasting tribute to his dedication to student training, his encouragement of young scientists, and his love of UVA. Please join us in congratulating the 2016 Wagner Fellows.
Rising 3rd year students:
- Andrew Grainger
- Paige Kulling
- Anthony Rodriguez
- Scott Seki
- Jacqueline Stevens
Rising 4th/5th year students:
- CJ Anderson
- Kelly Barford
- Bryan Barker
- Elizabeth Hoffman
- Molly Kelly-Goss
- Brian Mead
- Stephanie Ragland
Congratulations to the 2016 winner of the Peach Award:
Congratulations to the 2016 winner of the Hungerford Prize:
From left to right: Jim Casanova (mentor), Nancy Hungerford, Charles Hungerford, Emily Billings (sitting)
http://uvaconnect.com/featurestory/2014/04/03/new-tool-can-check-cells-batteries/UVA Develops New Tool to Check Cells’ ‘Batteries’By Illuminating Mitochondria, Researchers Shed Light on Disease, Human HealthCHARLOTTESVILLE, Va., April 3, 2014 – Under the microscope, they glow like streetlights, forming tidy rows that follow the striations of muscle tissue. They are mitochondria, the powerhouses of cells, and researchers at the University of Virginia School of Medicine have created a method to illuminate and understand them in living creatures like never before. Not only can the researchers make the mitochondria fluoresce, to glow for the microscope, but they can discern from that fluorescence the mitochondria’s age, their health, even their stress level. And ultimately that glow, in its soft reds and greens, will shed light on human health and a massive array of illnesses, from diabetes to Parkinson’s disease to cancer.”Mitochondrial health is important for physiology and disease. That is well known. However, the whole field of mitochondrial health is largely unexplored, in large part because of the lack of useful tools. This has hindered the understanding of the importance of mitochondria in disease development,” said UVA researcher Zhen Yan, PhD, of the UVA Cardiovascular Research Center. “With this study we have, for the first time, shown that we can use a reporter gene to measure mitochondrial health robustly in vivo. We believe this tool will allow us to get into the field of mitochondrial biology like never before.””Before, we could see the mitochondria under an electron microscope. That showed us only what they looked like,” Yan said. “Now we can measure the health of millions of mitochondria at the click of a button.”Health and Stress
Yan and his team based the new tool on a reporter gene, a type of gene used in scientific research to determine the activity and function of other genes. The reporter gene produces a protein that glows green when newly made; the protein then transitions to red as it ages. By giving the reporter gene specific targeting directions, the UVA researchers were able to instruct the protein to enter the mitochondria, setting them aglow. “So now we have fluorescent mitochondria, which are fluorescent green initially and then, as the mitochondria age or become oxidized, they transition to red, so that we can assess the oxidation status,” said Rhianna Laker, PhD, a postdoctoral fellow in Yan’s lab and the lead author of a new paper detailing the work.The researchers have put their tool to the test in flies, worms and mice. They found that mice fed a high-fat diet had more red mitochondria, meaning the mitochondria were stressed or oxidized, while mice that exercised had more green mitochondria, Laker said. That finding speaks both to the importance of exercise and to the potential diagnostic power of the new tool, dubbed the MitoTimer.The Big Picture
Taking advantage of the wide-ranging expertise at the School of Medicine, Yan’s lab collaborated with Jeff Saucerman, PhD, of the Department of Biomedical Engineering, to take the work to the next level. Saucerman’s team has developed a computer program that can analyze the degree of mitochondrial fluorescence to assess both individual mitochondria and the overall ratio of red to green in a particular area. That ratio speaks to the health of the cells. “The mitochondria are both the powerhouse of the cell and a sensor of metabolic state and stress,” Yan said.The findings have been published online in the Journal of Biological Chemistry and will appear in a forthcoming print edition. The article was authored by Rhianna C. Laker, Peng Xu, Karen A. Ryall, Alyson Sujkowski, Brandon M. Kenwood, Kristopher H. Chain, Mei Zhang, Mary A. Royal, Kyle L. Hoehn, Monica Dirscoll, Paul N. Adler, Robert J. Wessells, Jeff Saucerman and Zhen Yan.
WHAT’S NEW WITH OUR FACULTY?
Fluorescence micrograph of primary human neutrophils infected with the bacterium Neisseria gonorrhoeae, showing that some bacteria remain viable intracellularly. Internal viable bacteria appear green, internal nonviable bacteria appear red, external viable bacteria appear turquoise (blue and green), and external nonviable bacteria appear magenta (blue and red). Neutrophil nuclei also fluoresce red. N. gonorrhoeae can survive within neutrophils by residing in immature phagosomes that do not fuse with primary (azurophilic) granules.
Two modes of binding of DinI to RecA filament provide new insights into the regulation of the SOS response by the DinI protein.
The TetR family transcriptional regulator TM1030 from the hyperthermophile Thermotoga maritima is shown in a complex with DNA. The crystals in the background were grown in temperatures ranging from 4 – 50°C. Crystallization at elevated temperatures is uncommon, even for proteins from mesophilic and thermophilic organisms. The series of structures reported in this manuscript show that such proteins can be stable at elevated temperatures and that the quality of the crystallographic data and subsequent refined structures do not depend on the crystallization conditions.