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Biophysicist in Profile

Vera Moiseenkova-Bell

Vera Moiseenkova-Bell

Biophysics Week 2020 // 5244

Vera Moiseenkova-Bell was born in a small town outside of Moscow in the Soviet Union. She was able to engage with many of the area’s cultural institutions as a young child. “My parents, a physician and school teacher, put much time and effort into introducing me to museums, theater, literature, and art. My dad had the privilege of owning a car during the Soviet era, which permitted us to travel to Moscow and enjoy the big city and its seemingly endless number of activities,” she says. At age 11, she moved with her family to East Germany when her parents took positions at a Soviet military base outside of Dresden. By the time of the Soviet Union’s collapse and the reunification of East and West Germany, the family had moved to the Berlin area. “Growing up in close proximity to three prominent cities exposed me to different people and cultural environments in Eastern Europe. More importantly, growing up and living in this region during this time made me acutely aware of significant changes taking place in many people’s lives,” she shares. “This experience made me mindful and appreciative of human freedom and the ability to travel and interact with people from cultures and nationalities other than mine. I feel fortunate to have experienced what I did as a young adult during these transformative years. I am grateful to my parents for being brave and adventurous people. Without them, I feel as if I would not be the person that I am today.”

Moiseenkova-Bell loved physics and math as a young person, but was equally enthusiastic about history and archaeology. “I dreamed of becoming an archeologist and digging for woolly mammoth bones in Siberia or discovering mummies in Africa. My parents thought that this would not be a feasible means of employment after the Soviet Union collapsed as we had to return to the uncertainty of a new Russian Federation from reunified Germany.” Thankfully, she had an exceptional physics teacher in high school on the Soviet military base in Germany. “He had a gift like no other as he could teach a tough subject with such ease.  We did experiments with minimal resources, but he still managed to get us all interested in physics and math. Everyone enjoyed the class so much that we all returned to the classroom after school with an appetite for more,” she says.

Upon her family’s return to Moscow, she was accepted to the physics program at M.V. Lomonosov Moscow State University. “Looking back, I'll never regret [following] the advice my parents gave me regarding the decision to pursue physics in college,” she says. “It was a great discipline to learn as it is widely applicable to any STEM category one can imagine.” While Moiseenkova-Bell was studying under Yury Romanovsky in the university’s division of Nonlinear Optics and Wave Processes, she had the opportunity to participate in a project exploring how coherent light produced by lasers interacts with biological tissues and organisms at different wavelengths.

Upon graduation in 1999, she was recruited to the United States as a visiting research fellow to work at the University of Texas Medical Branch in Galveston on a United States Air Force Office of Sponsored Research project. “The project was focused on understanding temperature sensation in reptiles and insects with the goal to simulate these properties for potential military purposes,” she says. “I was using coherent light from lasers to stimulate the infrared sensory organs of venomous pit viper snakes to determine their thermal sensitivity.  While working on this project, I learned about recently cloned Transient Receptor Potential (TRP) channels, membrane protein temperature sensors in the mammalian body, from my future advisor, Dr. Burgess Christensen.”

Around the same time, she was introduced to membrane protein biophysics and structural biology by Ehud Landau, a visiting professor from Switzerland who spoke to her about crystallization of membrane proteins using lipidic cubic phases. “The rest, as they say, is history! I was so fascinated to see my favorite TRP channel at the atomic level and to understand how it works,” she explains. “It has literally made me dedicate my entire career for the last 20 years to this task.”

From 2000 to 2004, Moiseenkova-Bell studied under Christensen, who she calls an outstanding mentor, at University of Texas Medical Branch. “I was his last PhD student before he retired and we spent a lot of time together in the lab.  Moreover, Dr. Christensen’s wife, Monique, was French and thus he knew how to be supportive to a foreign national far away from home,” she says. “He was a very level-headed, respectful, and fair person. He was patient but also knew when I needed a little prodding.” He suggested that she take her PhD thesis project on TRP channels with her to continue as a postdoc at Baylor College of Medicine in Houston. “At Baylor, Dr. Ted Wensel gave me a bench in his laboratory and access to lab reagents and told me that I can work on my TRP channel project that I brought with me to his lab,” she says. “I am profoundly grateful to these two outstanding mentors who allowed me to follow my passion for TRP channels structural biology.”

Following her time at Baylor, she served as a Visiting Postdoctoral Fellow in the Department of Cellular and Molecular Physiology at Yale University from 2005 to 2009. She then set up her independent lab at Case Western Reserve University, where she worked from 2009 to 2018. Sudha Chakrapani met Moiseenkova-Bell when they overlapped at Case, where Chakrapani has maintained her lab. “We were colleagues for eight years. During this time, we interacted on a regular basis discussing science, collaborative projects, and just had a lot of fun together with our labs. Vera and her group were instrumental in getting us started with Cryo-EM,” Chakrapani says. “Vera is a powerhouse of energy and enthusiasm! It’s been a blast working with her. She is a great colleague, collaborator, and friend.”

Moiseenkova-Bell first met collaborator Marta Filizola, Icahn School of Medicine at Mount Sinai, in 2017 when Filizola gave a talk in her department at Case. They started to collaborate immediately, and have published two papers together since. “The project she got me intrigued by was focused on understanding the structural basis of TRPV5 channel inhibition by small molecules,” Filizola shares. “Currently, we are waiting for her to share new structural information her lab is still refining. Vera is the most tenacious and perseverant person I have been working with. Her handling of the review process concerning the latest paper we published together was remarkable.”

Moving to the University of Pennsylvania in 2018, she now serves as both Associate Professor in the Department of Systems Pharmacology and Translational Therapeutics, and as Faculty Director for the Electron Microscopy Resource Laboratory and Beckman Center for Cryo Electron Microscopy. Her lab is interested in “understanding structure and function of TRP channels which have been implicated in a diverse range of cellular processes, including pain sensation, neuronal development, cardiovascular and renal pathophysiology, and cancer,” currently focusing on two main areas of research: to determine the structural basis of TRP channel activation, inhibition, and desensitization mechanisms by utilizing cryo-EM; and to understand how TRP channels regulate cellular functions and the role of their dysregulation in human disease.

Tibor Rohacs, Rutgers University, first met her at the Ion Channel Keystone meeting in 2007, where Moiseenkova-Bell presented her unpublished work on the cryo-EM structure of the heat- and capsaicin-sensitive TRPV1. “This was well before the resolution revolution, so I asked her, ‘Are you also trying to get the crystal structure?’ ‘Of course,’ she said. ‘Are you going for pieces, or the whole thing?’ She looked at me and said, ‘The whole thing, of course.’ She did not get the crystal structures then, but persistence paid off, and years later she determined several full-length high-resolution TRP channel structures,” Rohacs recalls. “This story illustrates her most memorable quality: her relentless enthusiasm and optimism about getting great data.”

When asked about her scientific role models, Moiseenkova-Bell recalls when, soon after starting her own lab, her first graduate student found a new endogenous regulator of TRP channels. “Following up on this lead, I decided to contact Dr. Paul Greengard, a Nobel Prize winner and a world renowned neuroscientist who had studied this regulatory protein. By email I introduced myself and our project and politely requested his assistance. Much to my surprise he replied immediately and agreed to help providing all the necessary reagents, tools and advice,” she shares. “He was very supportive and followed up with my laboratory on several occasions to make sure that we were on the right track. This type of positive interaction with a person of Dr. Greengard’s stature is unfortunately rare. Dr. Greengard’s actions towards me as a new investigator that he never met profoundly impacted me. I would say that my positive experience with this extraordinary individual, whom coincidently was also extremely supportive of women in science, is the underlying reason for my supporting and collegial academic personality that I deploy daily with all of my trainees, colleagues, and staff.”