In a new study, researchers show how a critical Lassa virus protein, called polymerase, drives infection by harnessing a cellular protein in human hosts. Their work suggests future therapies could target this interaction to treat patients.
Helical nucleocapsids in infected cells are composed of Marburg viral genomic RNA and nucleoproteins, or NPs, that are structurally similar to those of the Ebola virus. Future drug development may be possible based on the targeting of nucleocapsid formation, which may inhibit the Marburg virus' ability to replicate.
A new tool can quickly and reliably identify the presence of Ebola virus in blood samples, according to a study by researchers at Washington University School of Medicine in St. Louis and colleagues at other institutions.
Ebola virus polymerase hijacks a cellular protein called GSPT1. An experimental drug that targets GSPT1 for degradation can also halt Ebola virus infection in human cells.
The team's latest study, published in Cell, shows that two clever human antibodies can target two ebolavirus species at once: Ebola virus and Sudan virus. These two species are responsible for the biggest, deadliest outbreaks. The new report suggests researchers could combine these two potent antibodies to make a powerful antiviral therapy.
A new study by UCLA researchers and colleagues demonstrates that the Ebola vaccine known as rVSVΔG-ZEBOV-GP results in a robust and enduring antibody response among vaccinated individuals in areas of the Democratic Republic of Congo (DRC) that are experiencing outbreaks of the disease. Among the more than 600 study participants, 95.6% demonstrated antibody persistence six months after they received the vaccine. The study is the first published research examining post–Ebola-vaccination antibody response in the DRC, a nation of nearly 90 million. While long-term analyses of the study cohort continue, the findings will help inform health officials’ approach to vaccine use for outbreak control, the researchers said.
• Researchers have identified a set of receptors shared across human, mosquito, and other animal cells for the eastern equine encephalitis virus (EEEV) and two related viruses, a crucial first step for developing preventive and curative treatments. • In experiments with cells and mouse models with a related virus, the scientists were able to prevent infection and disease progression using decoy molecules to hamper viral entry into cells. • In a 2019 outbreak of eastern equine encephalitis (EEE, or triple E) in New England, 30 percent of infected people died and half of those who survived had long-term neurologic damage. • Done between major outbreaks, this type of research into highly pathogenic viruses with pandemic potential can help improve preparedness for future outbreaks.
A nationwide team of researchers, led by scientists at University of Utah Health and The Rockefeller University, has determined how a genetic mutation found in mice and monkeys interferes with viruses such as HIV and Ebola. They say the finding could eventually lead to the development of medical interventions in humans.
A family of proteins best known for their role in diminishing HIV infectivity may have the goods to outwit other emerging and re-emerging viruses, scientists have found.
Expert Q&A: Do breakthrough cases mean we will soon need COVID boosters? The extremely contagious Delta variant continues to spread, prompting mask mandates, proof of vaccination, and other measures. Media invited to ask the experts about these and related topics.
The Global Virus Network (GVN), representing 63 Centers of Excellence and 11 Affiliates in 34 countries comprising foremost experts in every class of virus causing disease in humans, and the Institut de Recherche en Santé, de Surveillance Epidémiologique et de Formation [Institute for Health Research, Epidemiological Surveillance and Training], or the IRESSEF, announced the addition of the IRESSEF as GVN’s newest Center of Excellence.
Mount Sinai researchers have uncovered the complex cellular mechanisms of Ebola virus, which could help explain its severe toll on humans and identify potential pathways to treatment and prevention. In a study published in mBio, the team reported how a protein of the Ebola virus, VP24, interacts with the double-layered membrane of the cell nucleus (known as the nuclear envelope), leading to significant damage to cells along with virus replication and the propagation of disease.
Scientists have a general idea of how viruses invade and spread in the body, but the precise mechanisms are actually not well understood, especially when it comes to Ebola virus. Olena Shtanko, Ph.D., a Staff Scientist at the Texas Biomedical Research Institute (Texas Biomed), has received more than $1 million from the National Institutes of Health (NIH) to explore different aspects of Ebola virus infection.
Researchers are developing a new sensor that can detect Ebola in a single drop of blood and provides results in just an hour. With further development, the technology might also enable fast and inexpensive detection of other viruses, including the virus that causes COVID-19.
&T's National Biodefense Analysis and Countermeasures Center designed and conducted a study to optimize methods for collecting and measuring very small amounts of Ebola virus in the air.
In a new Cell Reports study, researchers at La Jolla Institute for Immunology demonstrate how Ebola virus has found a different way to get things done. The virus encodes only eight proteins but requires dozens of functions in its lifecycle. The new study shows how one of Ebola virus’s key proteins, VP40, uses molecular triggers in the human cell to transform itself into different tools for different jobs.
S&T Past Research with anthrax bacteria, Ebola virus and other pathogens informs current and future pandemic response.
A novel computer algorithm that could create a broadly reactive influenza vaccine for swine flu also offers a path toward a pan-influenza vaccine and possibly a pan-coronavirus vaccine as well, according to a new paper published in Nature Communications.
Researchers have identified a previously unknown site on the filovirus glycoprotein to which small drug molecules can bind and prevent infection -- blocking both sites may be more a more effective treatment with reduced risk of side effects.
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