Latest news with #HormelInstitute
Yahoo
3 days ago
- General
- Yahoo
New high-resolution structures of measles virus enzyme could lead to protective measures
May 30—Using high-resolution cryo-electron microscopy (cryoEM), researchers at The Hormel Institute, University of Minnesota, have revealed the first high-resolution renderings of the measles virus's (MeV) polymerase. This enzyme is crucial for the virus's ability to hijack cells and make copies of itself, which is one aspect that makes the virus so effective at infecting people and spreading throughout the body. For a virus that's been documented since at least the ninth century, there is still plenty we have to learn about the measles virus and how it operates, Associate Professor Bin Liu, PhD, explained as he discussed his new study published in Nature Communications. "Even well-known viruses like measles still have uncharted molecular terrain, and illuminating its structure provides valuable insights for therapeutic development," Liu said. By revealing measles' structure, Liu, along with Postdoctoral Researchers Dong Wang, PhD, and Ge Yang, PhD, have unlocked valuable insights that could help other researchers develop preventative and therapeutic measures to combat this deadly virus that can cause complications ranging from pneumonia to ear infections to encephalitis (inflammation of the brain). "Although an effective vaccine is available, recent measles outbreaks highlight the urgent need for alternative antiviral treatments," Liu said. "Because the polymerase is essential for viral genome replication, it represents a critical target for antiviral intervention." The study presents two new, distinct renderings of MeV polymerase complexes known as Lcore-P and Lfull-P-C. According to Liu, one of the most intriguing findings is the structural role of the measles virus C protein in forming the Lfull-P-C complex with two other proteins, L and P. This is surprising because the C protein was traditionally seen as a regulatory protein, not part of its core replication machinery. Now, it's shown to physically bridge and modulate the L protein's activity, potentially influencing how efficiently the virus replicates. Additionally, the study shows that the C protein widens the polymerase's RNA channel in the polymerase, possibly enhancing the processivity of RNA synthesis. That kind of physical alteration, revealed via cryoEM at near-atomic resolution, is a remarkable mechanistic insight. It suggests that the measles virus has evolved an elegant, multi-protein solution for efficient replication inside host cells. This kind of structural adaptation is a biological engineering marvel, and it highlights how even simple viruses can have complex, dynamic protein machinery. By revealing detailed interactions within the Lfull-P-C complex, the paper opens doors for next-generation antiviral drug designs that halt viral replication. "This shifts the measles conversation from 'solved by vaccines' to 'still relevant for therapeutic innovation,'" Liu concluded.
Yahoo
10-05-2025
- Health
- Yahoo
Cell death and disease study by Institute scientists Sheds light on targeted protein to fight breast cancer
May 9—Roughly 1 in 8 women will be diagnosed with invasive breast cancer over their lifetimes, according to the American Cancer Society—and for the year 2024, it was estimated that more than 300,000 women in the United States would be diagnosed with breast cancer, and more than 40,000 would die from the disease. If we want to reduce these numbers, increasing our understanding of how breast cancer operates in order to improve prevention, detection, and treatment methods is paramount. The lab of Assistant Professor Liang Liu, PhD, at The Hormel Institute, University of Minnesota, has published a paper appearing in the scientific journal Cell Death & Disease that examines how a protein called TXNIP might help fight breast cancer by slowing its growth and spread throughout the body. The scientists focused on two different types of breast cancer cells: MDA-MB-231: Associated with triple-negative breast cancer and naturally high TXNIP levels HCC-1954: Associated with HER2-positive breast cancer, low TXNIP levels They also investigated how TXNIP interacts with other proteins—especially calpastatin (CAST) and interleukin-24 (IL-24)—and how these interactions influence a cancer-promoting cellular signal called STAT3. The study yielded some surprising findings that warrant further scientific exploration. "It's surprising that calpastatin (CAST), a protein TXNIP binds to, actually promotes tumor growth in both cell types tested. CAST was known for a different role (stopping cell damage), so its cancer-helping behavior here is unexpected and worth exploring further," Liu said. "In HCC-1954 cells, extra TXNIP first shrank tumors, but after four weeks, growth sped up. This shift hints that cancer might adapt or resist over time, possibly due to CAST, making TXNIP's effects a puzzle to solve." This study is significant for its contributions to understanding TXNIP's role in breast cancer and its therapeutic potential The study's authors are continuing research in this area to bring these findings closer to real-world use to transform outcomes for breast cancer patients. Beyond cancer, better understanding of TXNIP has applications across multiple health fields. For example, TXNIP helps regulate blood sugar and cell stress, making it significant in diabetes research. The Hormel Institute's Post-Doctoral Associate Jasvinder Singh, PhD; Post-Doctoral Associate Bindeshwar Sah; and Executive Director Robert Clarke, PhD, at The Hormel Institute are also listed as authors of the paper.
