The 2019 UConn College of Liberal Arts and Sciences undergraduate graduation took place at Gampel Pavilion on Sunday, May 12.
Following commencement, the Molecular and Cell Biology Department hosted the annual reception for graduating seniors in biology.
Awards were given out to students in the 4 areas of concentration. Dr. Michael Lynes, head of MCB handed out awards to Brian Aguilera and Jennifer Messina for Outstanding Senior in MCB. Kevin Lee and Tony Patelunas each received an award for Outstanding TA award.
David R. Benson, Ph.D., Professor of Microbiology, retired on June 1 after more than 40 years at UConn. Dr. Benson’s distinguished career includes service as Head of the Molecular and Cell Biology Department from 2007-2012. During that time, he oversaw the expansion of the department personnel, doubled undergraduate course enrollment, built administrative protocols and brought national visibility to MCB, and increased graduate student recruitment. Dr. Benson’s guidance encouraged department members to participate in public and community outreach thereby highlighting awareness of the department.
Friend and colleague, Dr. Peter Gogarten describes Benson as “an encouraging mentor, advisor and co-advisor, an effective cheerleader for students, colleagues, and the department.” As colleagues mutually interested in the use of anciently duplicated genes in unraveling the early history of life, Gogarten says, “Our collaborations on the comparative genomics of Frankia strains, transposable elements, and the secretome of Frankia grown under different conditions launched several students onto successful scientific careers.”
Dr. Benson received his doctoral degree from Rutgers University in Microbiology and Biochemistry and did postdoctoral work at the University of Wisconsin, Madison in biochemistry before coming to UConn in 1980. Benson's research and teaching expertise are in the Microbial genomics, microbial biogeography and ecology, physiology and molecular biology of bacteria, symbiosis, psychrophile evolution, food microbiology, bio-security He is particularly interested in genomic and biochemical characteristics that align with the distribution of microorganisms in environments.
Dr. Benson served as a Jefferson Science Fellow to the U.S. Department of State from 2012-2017. As a Jefferson Fellow, he served as a Senior Science Advisor to the Biological Policy Staff in the Bureau of International Security and Non-proliferation. In addition, he is a Fellow of both the American Association for the Advancement of Science (AAAS) and the American Academy of Microbiology and was twice elected as the Chair and Councilor of the General Microbiology Division of the American Society for Microbiology and has served on the Editorial Board of the journal Applied and Environmental Microbiology. He has been elected to the Connecticut Academy of Arts and Sciences and served as visiting professor at the University of Waikato, New Zealand.
Dr. Michael Lynes, professor and current head of the Molecular and Cell Biology Department said, “I celebrate David’s career – for his achievements and the investments he made in other faculty and their success, his contributions to the scientific community in MCB, his teaching of content critical to our students, and for his role as a thoughtful and cheerful colleague.” Dr. Benson has been appointed by the UConn Board of Trustees as Professor Emeritus, Molecular and Cell Biology.
The following MCB employees have reached important milestones in their service to the state and the University. Though the celebration of these achievements will be delayed until all employees are back working in person on campus, it is important that we recognize and applaud their commitment and dedication to UConn and MCB. Thank you!
Celebrating 10 years - Colleen Spurling, Mark Longo
15 years - Craig Nelson, Elaine Mirkin, Victoria Robinson
The Department of Molecular and Cell Biology is pleased to announce that Stephen Hesler and Sean Gosselin have been selected as Outstanding MCB TA for 2019-2020. This award recognizes their outstanding contributions, professional dedication to inspiring student learning and their commitment to education. Congratulations!
Atomwise Partnership Enables UConn Researcher to Investigate COVID-19 Drug Target
University of Connecticut professor of molecular and cell biology James Cole is working on identifying new therapeutics for COVID-19.
June 22, 2020-Anna Zarra Aldrich '20 (CLAS), Office of the Vice President for Research
University of Connecticut professor of molecular and cell biology James Cole is working on identifying new therapeutics for COVID-19.
Through a collaboration with Atomwise, a California-based company which uses artificial intelligence to advance small molecule drug discovery, Cole is one of the 15 researchers looking at different coronavirus protein targets for COVID-19 treatment.
Cole is focusing on the NSP15/EndoU ribonuclease enzyme the COVID-19 virus needs to replicate as well as degrade viral RNA to hide it from host cell defenses. Cole is looking for a molecule that can inhibit the enzyme and thus inhibit replication of coronaviruses.
“The virus and the host carry out this war,” Cole says. “The virus has to evade the host’s innate immunity response while the host is trying to stop the virus from replicating.”
By inhibiting this enzyme, the body’s innate immune system would prevent the virus from replicating.
Atomwise is connecting researchers around the globe to their Artificial Intelligence Molecular Screen (AIMS) program. AtomNet, the company’s patented AI screening technology, screens millions of molecules to find those which have the highest probability of being useful for treatment.
AtomNet uses 3D models of various protein drug targets to identify molecules that may bind to them. Atomwise then sends these molecules to researchers who conduct experiments to find compounds that bind or inhibit drug targets.
Earlier this year, scientists published the structure of the NSP15/EndoU enzyme from SARS-CoV-2, the virus responsible for COVID-19, providing the basis for Atomwise’s analysis. Atomwise will search through its database to identify molecules which may bind to the surface of NSP15/EndoU and could potentially be used for drug development.
While there are many potential targets for COVID-19 treatment, NSP15/EndoU is particularly attractive because it is necessary for SARS-CoV-2 replication and is highly conserved among coronaviruses. This means this enzyme is very similar in all coronaviruses.
Successfully targeting NSP15/EndoU would block the virus’ ability to replicate without interfering with normal human cell function.
“There’s no close analog in humans, so it’s unlikely to inhibit things we don’t want it to,” Cole says.
This research may also have ramifications for other coronaviruses which are responsible for other illnesses including SARS and MERS as well as new, emerging coronaviruses.
In addition to partnering with Atomwise for virtual screening with AtomNet, Cole is utilizing UConn’s high-performance computer cluster and the Schrödinger Software Suite to perform additional molecule screenings.
Cole studies how a variety of viral pathogens interact with the host’s innate immune pathways, positioning him well to tackle the challenges presented by COVID-19.
“When the pandemic hit, I was beginning to think we can help with this,” Cole says.
Cole has applied for funding from the National Institutes of Health for this two-year research venture.
“It’s an exciting and new therapeutic target,” Cole says. “It’s a particularly good target and of scientific interest to me.”
Cole holds a Ph.D. from the University of California. He completed his postdoctoral training at Stanford University. His research focuses on using biochemical, biophysical and structural methods to define the key macromolecular interactions that regulate important biological processes, specifically the innate immunity pathway for defense against viral infection.
Misbah Aziz (Mellone Lab) received the Outstanding Senior in MCB award, Kelsey Herbert (Campellone Lab) received the Biology Directors Award, and Alyssa Ferreira received the Excellence in Applied Genetics and Technology Award. Assignment of all awards is made by the Biology Honors Committee following the Biology Undergraduate Research Colloquium held annually during the last week of classes. To learn more about all the awards, visit https://mcb.uconn.edu/biological-sciences-awards/
The Office of Vice President for Research (OVPR) recently announced the award decisions for the UConn Microbiome Research Seed Grant Program. Jonathan Klassen, Metal-Binding Antimicrobial Peptide Mediation of a Fungus-Growing Ant Symbiosis, Co-PI: Alfredo Angeles-Boza and Mark Peczuh, Chemistry, Characterizing the Role of Siderophores in the Euprymna Scolopes – Vibrio Fischeri Symbiosis
Co-PI:Spencer Nyholm were among the four chosen research proposals. Complete story in UConn Today For more information about the competition, visit the program website.
Congratulations to MCB students Taylor Domingue and Sumeet Kadian on becoming 2020-2021 Werth Innovators! Werth Innovators are student ambassadors for entrepreneurship and innovation at UConn who play a central role in building interest and participation in a wide range of programs. They are selected annually from a pool of freshmen applicants based upon their innovative projects and interest in increasing student involvement in entrepreneurship and innovation at the university. These students are awarded a $3,000 scholarship for the 2020-21 school year and receive significant mentoring, programming, and developmental opportunities. During one of their spring breaks, the students will visit Silicon Valley/San Francisco to spend time with UConn alum in the technology and entrepreneurship space.
In December 2017, UConn announced the establishment of The Peter J. Werth Institute for Entrepreneurship & Innovation after philanthropist and entrepreneur Peter J. Werth made a historic $22.5 million commitment to UConn. Under University leadership, the Institute brings together student and faculty programs fostering entrepreneurship and innovation that potentially have commercial application and can be used to create new companies. Learn more about the Peter J. Werth Institute for Entrepreneurship and Innovation
Huntington’s. Parkinson’s. Muscular dystrophy. Lou Gehrig’s. These diseases share a common cause that devastatingly robs sufferers of their energy, muscle control, and in the case of Huntington’s, their sanity. But now, a group of researchers from UConn describes how a possible therapy might work.
What all those fearsome diseases have in common is dysfunctional mitochondria. Mitochondria are the body’s tiny power plants. These minuscule, rod-shaped structures inside our cells take in oxygen and nutrients and put out ATP, the body’s fuel (ATP is to cells what gasoline is to cars.) When mitochondria don’t work so well, the dysfunction can cause strange and awful symptoms that are particularly distressing in parts of the body that require lots of energy: particularly muscles, the brain, and nerve tissue.
Mitochondrial diseases tend to worsen with age. Scientists have guessed that mitochondria age as the rest of our body does. Damage acquired over time may contribute to mitochondrial diseases, but they aren’t entirely sure what’s happening or how to stop it.
“They’re insidious diseases because they rob your cells of their energy. They’re so hard to diagnose and the symptoms can be so diverse,” says Nathan Alder, a molecular biophysicist in the Department of Molecular and Cell Biology at UConn.
Alder and other researchers from UConn, the University of Texas, and Alexandria LaunchLabs are researching a group of compounds that seem to protect and even repair damage to mitochondria. The researchers describe the compounds, called SS peptides, and one potential way they may work to heal mitochondria in an upcoming issue of the Journal of Biological Chemistry.
SS peptides are made of amino acids, the building blocks of proteins, but each SS peptide is only four amino acids long. They all have the same basic plan: two amino acids with a positive charge alternating with two aromatic amino acids (“aromatic” is a chemistry term meaning they have a ring-like structure similar to benzene).
Previous research by Hazel Szeto at Cornell University, who first described SS peptides and served as co-author on this study, showed that SS peptides can enter into any cell in the body, and mitochondria suck them up like sponges. Alder and his colleagues wanted to figure out what the peptides were doing when they got in there. Using approaches ranging from computer modeling to studying mitochondria in the lab, they began to see the peptides’ effects. It looks like they can alter and potentially repair mitochondria by tuning the electric properties of their membranes.
Mitochondrial membranes are intricately creviced double-layers of fatty molecules called lipids that surround proteins sticking out of the membrane itself. The outer layer of the membrane “talks” to the rest of the cell, sensing conditions and passing ATP and other molecules back and forth. The labyrinthine inner layer of the membrane holds the ATP factories. One of the special lipids enriched in the inner membrane, cardiolipin, has a strong affinity for SS peptides.
Mitochondria tend to accumulate positively charged things like calcium ions—mitochondria actually serve as storage centers for cellular calcium. Yet calcium overload can cause damage to mitochondria’s cardiolipin-containing membranes over time, ripping into the membrane and causing permanent damage.
SS peptides can prevent that from happening, Alder and his colleagues found. The peptides are positively charged but in a gentler way than calcium; they snuggle up against the mitochondrial membrane and shield it from the smaller, more damaging calcium ions.
“This is probably not the only effect of SS peptides. But it’s an interesting one,” Alder says. The researchers want to understand more about how the peptides interact with the mitochondria and why they appear to have such broad-based efficacy against so many mitochondrial disorders. The team is currently using UConn’s nuclear magnetic resonance facilities to get detailed pictures of SS peptide structural features and how the peptides might alter or maintain the shape of the mitochondrial membranes. “We know they work. We want to know how they work. By understanding the mechanism of action, we can engineer more effective peptide analogs and possibly tailor them to treat specific mitochondrial afflictions,” Alder says.