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Rohit V. Pappu, Ph.D.

AIMBE College of Fellows Class of 2016
For outstanding contributions to protein engineering and design and the molecular basis of neurodegeneration through advances in computational biology

New clues found to common respiratory virus

Via Washington University in St. Louis | June 30, 2017

By age 2, most children have been infected with respiratory syncytial virus (RSV), which usually causes only mild cold symptoms. But people with weakened immune systems, such as infants and the elderly, can face serious complications, including pneumonia and – in some cases – death.

Now, scientists studying the virus, led by researchers at Washington University School of Medicine in St. Louis, have found clues to how RSV causes disease. They mapped the molecular structure of an RSV protein that interferes with the body’s ability to fight off the virus. Knowing the structure of the protein will help them understand how the virus impedes the immune response, potentially leading to a vaccine or treatment for this common infection.

“We solved the structure of a protein that has eluded the field for quite some time,” said Daisy Leung, an assistant professor of pathology and immunology, and of biochemistry and molecular biophysics at Washington University School of Medicine in St. Louis, and the study’s co-senior author. “Now that we have the structure, we’re able to see what the protein looks like, which will help us define what it does and how it does it. And that could lead, down the road, to new targets for vaccine or drug development.”

To test their hypothesis, the researchers created different versions of the NS1 protein, some with the alpha 3 helix region intact, and some with it mutated. In collaboration with others – Rohit Pappu, the Edwin H. Murty Professor of Biomedical Engineering, Michael Holtzman, MD, the Selma and Herman Seldin Professor of Medicine, Maxim Artyomov, an assistant professor of pathology and immunology, and Christopher Basler of Georgia State University – they tested the functional impact of helix 3 and created a set of viruses containing the original or the mutant NS1 genes, and measured the effect on the immune response when they infected cells with these viruses.

They found that the viruses with the mutated helix region did not suppress the immune response while the ones with the intact helix region did… Continue reading.

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Detecting Diluteness

Via Washington University in St. Louis | June 26, 2017

New experimental and theoretical approaches ‘dive into the pool’ of membranes organelles

Inside each and every living cell, there are miniscule structures called membraneless organelles. These tiny powerhouses use chemistry to cue the inner workings of a cell — movement, division and even self-destruction.

A collaboration between engineers at Princeton University and Washington University in St. Louis has developed a new way to observe the inner workings and material structure of these vitally important organelles. The research, published today in Nature Chemistry, could lead to a host of new scientific applications, as well as a better understanding of diseases such as cancer, Huntington’s and ALS.

“They’re like little drops of water: They flow, they have all the properties of a liquid, similar to raindrops,” said Rohit Pappu, the Edwin H. Murty Professor of Engineering at Washington University’s School of Engineering & Applied Science. “However, these droplets are comprised of protein that come together with RNA (ribonucleic) molecules.”

In the past, peering into organelles has proven difficult, due to their tiny size. Clifford Brangwynne, associate professor in chemical and biological engineering at Princeton’s School of Engineering and Applied Science, and his collaborators, developed a new technique — called ultrafast scanning fluorescence correlation spectroscopy or usFCS — to get an up-close assessment of the concentrations within and probe the porosity of facsimiles of membraneless organelles. The approach uses sound-waves to control a microscope’s ability to move and then obtain calibration-free measurements of concentrations inside membraneless organelles… Continue reading.

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Rohit V. Pappu, Ph.D. To be Inducted into Medical and Biological Engineering Elite

Via AIMBE | August 21, 2017

WASHINGTON, D.C.— The American Institute for Medical and Biological Engineering (AIMBE) has announced the pending induction of Rohit V. Pappu, Ph.D., Edwin H. Murty Professor of Engineering, Biomedical Engineering, Washington University in St. Louis, to its College of Fellows. Dr. Pappu was nominated, reviewed, and elected by peers and members of the College of Fellows For outstanding contributions to protein engineering and design and the molecular basis of neurodegeneration through advances in computational biology.

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