Publisher Health

A new study by investigators from Brigham and Women’s Hospital, a founding member of the Mass General Brigham healthcare system, demonstrated that shingles, also known as herpes zoster, is associated with an almost 30% higher long-term risk of a major cardiovascular event such a stroke or heart attack. Their results are published in the Journal of the American Heart Association.
“Our findings suggest there are long-term implications of shingles and highlight the importance of public health efforts for prevention,” said lead author Sharon Curhan, MD, ScM, a physician and epidemiologist in the Channing Division of Network Medicine at Brigham and Women’s Hospital. “Given the growing number of Americans at risk for this painful and often disabling disease and the availability of an effective vaccine, shingles vaccination could provide a valuable opportunity to reduce the burden of shingles and reduce the risk of subsequent cardiovascular complications.”
Shingles often causes a painful rash and can occur anywhere on the head or body. Shingles is caused by the varicella zoster virus, the same virus that causes chickenpox. After a person has chickenpox, the virus stays in their body for the rest of their life. Years and even decades later, the virus may reactivate as shingles. Almost all individuals aged 50 years and older in the US have been infected with the chicken pox virus and are therefore at risk for shingles.
Approximately 1 in 3 individuals will develop shingles in their lifetime, with more cases projected as the population ages and more people have compromised immunity due to disease or medication use.
The most common complication from shingles is postherpetic neuralgia. This condition affects nerve fibers and skin, causing burning pain that lasts long after the rash and blisters of shingles disappear. However, a growing body of evidence suggests that reactivation of the virus may have even longer lasting side effects. The virus may play a role in the development of cardiovascular disorders, including stroke and coronary artery disease. The virus has been detected in large and small blood vessels, which overtime can cause inflammation as well as chronic vascular changes. These changes can increase the risk of blockages in the blood vessels, restricted blood flow, and cardiovascular events such as strokes and heart attacks.
The prospective, longitudinal study followed three large U.S. cohorts of more than 200,000 women and men: the Nurses’ Health Study (~79,000 women), the Nurses’ Health Study II (~94,000 women) and the Health Professionals Follow-Up Study (~31,000 men). Participants did not have a prior history of stroke or coronary heart disease. The team collected information on shingles, stroke and coronary heart disease using questionnaires collected every two years and confirmed the diagnoses with medical record review. The team followed the participants for up to 16 years and evaluated whether those who had developed shingles were at higher risk for stroke or coronary heart disease years after the shingles episode.
The researchers tracked incidence of stroke and coronary heart disease — defined as having a non-fatal or fatal myocardial infarction (heart attack) or a coronary revascularization procedure (CABG, coronary artery bypass graft or percutaneous transluminal coronary angioplasty). Researchers also evaluated a combined outcome of cardiovascular disease, which included either stroke or coronary heart disease, whichever came first.
The results showed that people who had previously developed shingles were at 30% higher long-term risk of a major cardiovascular event compared with those who had not had shingles, and the elevated risk may persist for 12 years or more after having shingles.
Due to timing, much of the study took place in the period before the shingles vaccines became widely available. Even after their introduction, the uptake of vaccination has been generally low. Because of these limitations, researchers were not able to evaluate whether vaccination status may influence the association of shingles and long-term risk of a major cardiovascular event.
As more people choose to receive the shingles vaccine, future studies could examine whether vaccination influences the relation of shingles and risk of cardiovascular disease. Curhan adds, “We are currently collecting vaccination information among our participants and hope to conduct these studies in the future.”
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A new MRI study revealed that consumption of alcohol even in low to moderate amounts during pregnancy can change the baby’s brain structure and delay brain development. Results of the study will be presented next week at the annual meeting of the Radiological Society of North America (RSNA).
“Fetal MRI is a highly specialized and safe examination method that allows us to make accurate statements about brain maturation prenatally,” said study senior author Gregor Kasprian, M.D., associate professor of radiology from the Department of Biomedical Imaging and Image-guided Therapy of the Medical University of Vienna in Austria.
Alcohol consumption during pregnancy can expose the fetus to a group of conditions called fetal alcohol spectrum disorders. Babies born with fetal alcohol spectrum disorders could develop learning disabilities, behavioral problems or speech and language delays.
“Unfortunately, many pregnant women are unaware of the influence of alcohol on the fetus during pregnancy,” said lead author Patric Kienast, M.D., a Ph.D. student in the Department of Biomedical Imaging and Image-Guided Therapy, Division of Neuroradiology and Musculoskeletal Radiology at the Medical University of Vienna. “Therefore, it is our responsibility not only to do the research but also to actively educate the public about the effects of alcohol on the fetus.”
For the study, researchers analyzed MRI exams of 24 fetuses with prenatal alcohol exposure. The fetuses were between 22 and 36 weeks of gestation at the time of MRI. Alcohol exposure was determined via anonymous surveys of the mothers. The questionnaires used were the Pregnancy Risk Assessment Monitoring System (PRAMS), a surveillance project of the Centers for Disease Control and Prevention and health departments, and the T-ACE Screening Tool, a measurement tool of four questions that identify risk drinking.
In fetuses with alcohol exposure, the fetal total maturation score (fTMS) was significantly lower than in the age-matched controls, and the right superior temporal sulcus (STS) was shallower. The STS is involved in social cognition, audiovisual integration and language perception.

A daily cup of tea could help you to enjoy better health late in life — however if you’re not a tea drinker, there are other things you can add to your diet.
The key is flavonoids, which are naturally occurring substances found in many common foods and beverages such as black and green tea, apples, nuts, citrus fruit, berries and more.
They have long been known to have many health benefits — however new Edith Cowan University (ECU) research shows they may be even better for us than previously thought.
The Heart Foundation supported a study of 881 elderly women (median age of 80), which found they were far less likely to have extensive build-up of abdominal aortic calcification (AAC) if they consumed a high level of flavonoids in their diet.
AAC is the calcification of the abdominal aorta — the largest artery in the body which supplies oxygenated blood from the heart to the abdominal organs and lower limbs — and is a predictor of cardiovascular risk such as heart attack and stroke.
It has also been found to be a reliable predictor for late-life dementia.

The emergence of unpredictable variants and their stronger infectivity make the COVID-19 pandemic neverending — over 300 Omicron variants have been reported so far. Will there ever be a universal cure for the COVID-19 by neutralizing the various mutated strains of the virus?
A research team led by Professor Seung Soo Oh (Department of Materials Science and Engineering) has developed a tailored COVID-19 neutralizer that can adapt to all kinds of mutations in the virus in treating the viral infection. This neutralizing agent is designed to exhibit stronger effect by utilizing the same mechanism that viruses use to become stronger in infection through evolutionary processes.
The reason behind the increasing infectivity of the coronavirus with repeated mutations is that the virus can change its structure and thus increase the strength of its interaction with the angiotensin-converting enzyme (hACE2) receptor, a cell surface protein. Conventional treatments and neutralizing technologies fail to immediately respond to these newly emerging variants.
The research team found an innovative way to suppress cell infection by mimicking the principle of hotspot interaction between the virus and the hACE2 receptor. The newly developed hybrid neutralizer, consisting of a protein fragment and nucleic acids, can strongly bind to the coronavirus, which causes the virus not to interact with the hACE2 receptor, eventually inhibiting its penetration into the cells.
This neutralizer draws attention as it was based on the research team’s proprietary expertise in in vitro evolution technology called Hotspot-Oriented Ligand Display (HOLD). The HOLD is an evolutionary technology that automatically selects the most suitable material out of the 10 trillion candidate materials for binding to the virus, and the principle of the HOLD resembles the theory of natural selection, which postulated that individuals adapting to the changing environment have a high rate of survival.
The study reported that this hybrid agent has an excellent neutralizing effect not only against the Alpha, Beta, Gamma, and Delta variants but also the Omicron variant, which is known to be the most contagious. The neutralizing performance of this agent against the Omicron variant (equilibrium dissociation constant) was found to be 1.209 nanomoles (nM; 1 nM = 1 billionth of a mole), which is about 5 times higher than the observed neutralizing performance against the earlier strain of coronavirus (5.702 nM).
Professor Seung Soo Oh explained, “It is significant that we have developed the world’s first self-evolving neutralizer-developing platform that shows increasingly better performance with the occurrence of viral mutations.” He added, “We plan to develop it into a core technology that can respond to the next-generation pandemic viruses, such as influenza and Hantavirus.”
This study was published in Science Advances on October 26, 2022 (U.S. local time) and supported by the Samsung Research Funding and Incubation of Samsung Electronics.
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Polychlorinated biphenyls (PCBs) (*1) were widely used in industrial and commercial products including plastics, paints, electronic equipment and insulating fluids. Their manufacture was extensively banned from the late 70s onwards due to their toxicity, however large amounts still remain in our environment and accumulate inside animals’ bodies.
Chiral PCBs (*2) are PCBs that have two mirror-image isomers (*3); these isomers are identical reflections of each other with the same composition. Chiral PCBs are particularly dangerous because they have more chlorine atoms, which are hard for the body to break down, so they can accumulate in the body easily and their isomers are metabolized differently, causing isomer-specific toxicity (particularly neurodevelopmental issues). However, the process behind this selective metabolism was not known. To address this, a research group has illuminated how enzymes produced by the body unevenly metabolize the mirror-image isomers. These results will make it possible to estimate PCB metabolism and detoxification pathways in animals. They will also contribute towards the development of technology to make predictions about chiral PCBs’ mirror isomers, so that we can obtain a better understanding of potential toxicity in humans and other mammals.
These findings were made by a multi-institutional research collaboration, which included Associate Professor INUI Hideyuki (Kobe University Biosignal Research Center), Lead Researcher MATSUMURA Chisato (Hyogo Prefectural Institute of Environmental Sciences), Professor YAMAMOTO Keiko and Professor ITOH Toshimasa (Showa Pharmaceutical University), Associate Professor MORI Tadashi (Osaka University Graduate School of Engineering), and Visiting Professor NAKANO Takeshi (Osaka University Research Center for Environmental Preservation).
These research results were published online in the international academic journals Environmental Science & Technology on July 8, and Chemosphere on September 6, 2022.
Main points In the past, PCBs were utilized in a vast range of industrial and commercial products. These highly carcinogenic chemical compounds remain in our environment and accumulate inside organisms. PCBs have a dioxin-like toxicity and research into PCB metabolism is advancing. However, research had yet to uncover how chiral PCBs’ mirror-image isomers are metabolized. The researchers split the two atropisomers (mirror-image isomers) found in each type of chiral PCB and used them as substrates for CYP enzymes (*4). Even though a pair of atropisomers are physically and chemically identical, there was a big difference in the extent to which they were metabolized. Differences in CYP’s amino acids’ binding inhibition of each atropisomer cause the atropisomers to be metabolized differently. These findings will be useful for measuring the atropisomers of chiral PCBs, which accumulate easily inside animals’ bodies.Research Background
Even though the manufacture and use of PCBs was banned around 50 years ago, they still remain in the environment. It has been discovered that PCBs accumulate inside the bodies of humans and other animals through food consumption. In particular, PCBs with many chlorine bonds are water resistant and do not break down easily. This enables high concentrations of these PCBs to accumulate inside animals’ bodies, which adversely affects their health. PCBs’ toxicity is induced by the aryl hydrocarbon receptor (AhR) (*5), causing similar adverse effects to dioxin (*6) poisoning such as cancer, teratogenesis and immune system damage. Research is being conducted on the particular types of PCB widely known to cause these effects, which are dioxin-like PCBs with one ortho chlorine substitution in the biphenyl ring of their chemical structure, or PCBs with no substitutions. However, if a PCB has more than 3 chlorine substitutions at the ortho position of the biphenyl ring, it becomes a mirror-image isomer called chiral PCB. These chiral PCBs do not demonstrate dioxin-like toxicity but are far more dangerous, binding with the ryanodine receptors (RyR) in organisms to become neurotoxic. The two mirror-image isomers (called atropisomers) in chiral PCB have identical physical and chemical properties and exist at a 1:1 ratio in commercial chiral PCB. However, biased ratios are often observed in the environment and in animals such as earthworms and whales, as well as humans. It is believed that this unbalanced ratio is mainly caused by metabolism and that one of chiral PCB’s atropisomers is more effected by the metabolic reaction thus reducing its concentration.

With the continuous emergence of new variants and the risk of new strains of the virus, the development of innovative therapies against SARS-CoV-2 remains a major public health challenge. Currently, the proteins that are on the surface of the virus and/or are involved in its replication are the preferred therapeutic targets, like the Spike protein targeted by vaccines. One of them, the non-structural protein Nsp1, had been little studied until now. A team from the University of Geneva (UNIGE), in collaboration with University College London (UCL) and the University of Barcelona, has now revealed the existence of a hidden ”pocket’ on its surface. A potential drug target, this cavity opens the way to the development of new treatments against Covid-19 and other coronaviruses. These results can be found in the journal eLife.
The fast rollout of new vaccines and antiviral drugs has helped to contain the Covid-19 pandemic, caused by the SARS-CoV-2 virus. Despite the progress made, the development of new therapies is still an urgent priority: the continuous emergence of new variants — some of which are resistant to current treatments — and the possible appearance of new strains of the virus represent a risk of new pandemics. Proteins are at the forefront of therapeutic targets to combat the virus. The best known is the Spike protein, which is located on the surface of SARS-CoV-2 and gives it its ”spiky” appearance. It is the key to the virus entering our cells. It is the target of Messenger RNA vaccines.
A little-studied key protein
SARS-CoV-2 also makes other proteins — the “non-structural” proteins — using the resources of our cells after entering them. There are sixteen of them. They are essential for the replication of the virus. Some have been studied in the context of the development of new drugs. Others have received less attention. This is the case of the Nsp1 protein. Without obvious cavities on its surface to anchor a potential drug, researchers felt that it could not be a target for treatment.
”Nsp1 is, however, an important infectious agent of SARS-CoV-2,” explains Francesco Luigi Gervasio, full professor at the Section of Pharmaceutical Sciences and the Institute of Pharmaceutical Sciences of Western Switzerland of the UNIGE Faculty of Science, and at the Department of Chemistry and the Institute of Structural and Molecular Biology at UCL. ”This small viral protein selectively blocks ribosomes — the protein factories of our cells — making them unusable by our cells and thus preventing the immune response. At the same time, via ribosomes, Nsp1 stimulates the production of viral proteins.”
Revealed by algorithms
Professor Gervasio’s team, in collaboration with UCL and the University of Barcelona, revealed the existence of a ”hidden” cavity on the surface of Nsp1, which could be the target of future drugs against SARS-CoV-2. ”To uncover this cryptic, partially hidden pocket, we carried out simulations using algorithms that we developed,” explains Alberto Borsatto, research and teaching assistant at the Section of Pharmaceutical Sciences and the Institute of Pharmaceutical Sciences of Western Switzerland of the Faculty of Sciences of the UNIGE, first author of the study. ”Then, in order to confirm that this pocket could be used as a drug target, we used experimental screening and X-ray crystallography techniques.”
The research team tested many small molecules that could potentially bind to the Nsp1 cavity (experimental screening). It identified one in particular — 5 acetylaminoindane or 2E10 — that also allowed the determination of the spatial arrangement of the atoms making up the cavity (by crystallography). These are essential data that form the basis for the development of new drugs.
”These results pave the way for the development of new treatments targeting the Nsp1 protein, not only against SARS-CoV-2 and its variants but also against other coronaviruses in which Nsp1 is present,” says Francesco Luigi Gervasio, the study’s last author. As for the method developed to reveal the hidden pocket of Nsp1, it could be used to discover, on the surface of other proteins, new cavities still unknown to scientists.
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EPFL researchers have discovered that it is not just molecular density, but also pattern and structural rigidity, that control super-selective binding interactions between nanomaterials and protein surfaces. The breakthrough could help optimize existing approaches to virus prevention and cancer detection.
So much of biology comes down to the biophysical process of binding: making a strong connection between one or more groups of atoms — known as ligands — to their corresponding receptor molecule on a surface. A binding event is the first fundamental process that allows a virus to infect a host, or chemotherapy to fight cancer. But binding interactions — at least, our understanding of them — have a ‘Goldilocks problem’: too few ligands on one molecule makes it impossible for it to stably bind with the correct target, while too many can result in undesirable side-effects.
“When binding is triggered by a threshold density of target receptors, we call this “super-selective” binding, which is key to preventing random interactions that could dysregulate biological function,” explains Maartje Bastings, head of the Programmable Biomaterials Laboratory (PBL) in the School of Engineering. “Since nature typically doesn’t overcomplicate things, we wanted to know the minimum number of binding interactions that would still allow for super-selective binding to occur. We were also interested to know whether the pattern the ligand molecules are arranged in makes a difference in selectivity. As it turns out, it does!”
Bastings and four of her PhD students have recently published a study in the Journal of the American Chemical Society that identifies the optimal ligand number for super-selective binding: six. But they also found, to their excitement, that the arrangement of these ligands — in a line, circle, or triangle, for example — also significantly impacted binding efficacy. They have dubbed the phenomenon “multivalent pattern recognition” or MPR.
“MPR opens up a whole new set of hypotheses around how molecular communication in biological and immunological processes might work. For example, the SARS-CoV-2 virus has a pattern of spike proteins that it uses to bind to cell surfaces, and these patterns could be really critical when it comes to selectivity.”
From coronaviruses to cancer
Because its double helix structure is so precise and well understood, DNA is the perfect model molecule for the PBL’s research. For this study, the team designed a rigid disk made entirely out of DNA, where the position and number of all ligand molecules could be precisely controlled. After engineering a series of ligand-receptor architectures to explore how density, geometry, and nano-spacing influenced binding super-selectivity, the team realized that rigidity was a key factor. “The more flexible, the less precise,” Bastings summarizes.
“Our aim was to carve out design principles in as minimalist a way as possible, so that every ligand molecule participates in the binding interaction. What we now have is a really nice toolbox to further exploit super-selective binding interactions in biological systems.”
The applications for such a “toolbox” are far-reaching, but Bastings sees three immediately valuable uses. “Like it or not,” she says, “the SARS-CoV-2 virus is currently a first thought when it comes to virological applications. With the insights from our study, one could imagine developing a super-selective particle with ligand patterns designed to bind with the virus to prevent infection, or to block a cell site so that the virus cannot infect it.”
Diagnostics and therapeutics such as chemotherapy could also benefit from super-selectivity, which could allow for more reliable binding with cancer cells, for which certain receptor molecules are known to have a higher density. In this case, healthy cells would remain undetected, drastically reducing side effects.
Finally, such selectivity engineering could offer key insights into complex interactions within the immune system. “Because we can now play precisely with patterns of what happens at binding sites, we can, in a sense, potentially ‘communicate’ with the immune system,” Bastings says.

A team of synthetic biologists at the Hong Kong University of Science and Technology (HKUST) has recently discovered a way that could increase synthetic mRNA’s protein production efficiency by up to 10 times, which means the effectiveness of mRNA vaccines and drugs — such as those used against cancer, Covid-19 or other genetic diseases, will be greatly boosted with even less dosage of the mRNAs.
mRNAs can be synthesized to teach our cells in making any kind of proteins, such as antigens, enzymes and hormones which are essential in fighting infections and regulating bodily functions, so mRNA is arguably a preferred options for vaccines and treatment for many different kinds of diseases. However, high dosage and repeated injections are often required for mRNA drugs and vaccines in order to generate sufficient amount of protein in the body, so enhancing mRNA’s effectiveness — such as by increasing its protein production efficiency, is a hot subject among scientists as our immune system, for example, could work better with more certain antibodies.
Now, a team led by Prof. Becki KUANG Yi, Assistant Professor at the Department of Chemical and Biological Engineering at HKUST, discovered a way that could enhance both the life span and efficiency of mRNA. Having engineered different mRNA’s tail sequences, Prof. Kuang’s team eventually discovered optimized sequences that could produce 3 to 10 times as much proteins than unoptimized tail sequences commonly used for synthetic mRNAs on both human cells and on mice. Duration of protein production is also doubled.
This new technology will not only reduce the amount and the number of injections needed for mRNA drugs and vaccines, but will also potentially lower the cost of treatments. It can also be used along with other mRNA enhancement technologies to synergically boost protein production.
“Increasing the protein production of synthetic mRNA is generally beneficial to all mRNA drugs and vaccines,” said Prof Kuang. “In collaboration with Sun Yat-Sen University, our team is now exploring the use of optimized tails for mRNA cancer vaccines on animal. We are also looking forward to collaborating with pharmaceutical companies to transfer this invention onto mRNA therapeutics and vaccines’ development pipelines to benefit society.”
The finding was recently published online in the journal of Molecular Therapy — Nucleic Acids.
mRNA drugs and vaccines have attracted much attention in recent years due to their effectiveness in protecting us against severe conditions of certain communicable diseases such as COVID-19 and their high potential in treating chronic diseases like cancers. An earlier research has shown that the global mRNA therapeutics market size was valued at USD 39.90 billion last year and is expected to expand further in the coming decade.
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A new study released today in Nature Communications from the Department of Biology, University of Oxford has found the first direct evidence of antibiotic resistant bacteria migrating from a patient’s gut microbiome to the lungs. Applying the findings of this study could save lives, as it highlights the importance of preventing pathogenic bacteria from translocating from the gut to other organs where they can cause serious infections.
The study was conducted on a patient that carried the bacterium Pseudomonas aeruginosa as part of their gut microbiome. This species is one of the leading causes of infections in hospitals, and one that is particularly good at resisting antibiotics. Whilst Pseudomonas is generally not considered to be dangerous when it is embedded in a healthy gut microbiome, it can cause serious infections in the lungs of hospitalized patients.
During their stay in hospital the patient was treated with the antibioticMeropenem for a suspected urinary tract infection (UTI). Meropenem treatment caused non-resistant bacteria in the gut and lung to be killed off, andantibiotic resistant mutants of Pseudomonas were able to grow and proliferate.
Pseudomonas was then found to translocate from the gut to the patient’s lungs during antibiotic treatment, where it evolved even higher levels of antibiotic resistance.
With AMR being an increasing concern in hospitals, preventing the spread of AMR bacteria to other vital organs such as the lung is critical in vulnerable patients. However, the origin of bacteria that cause these serious infections can be difficult to determine. This study shows how the gut microbiome can act as a reservoir of AMR pathogens that can translocate to the lung where they have the potential to cause life-threatening illnesses such as pneumonia.
The findings of this study suggest that eliminating AMR pathogens from the gut microbiome of hospitalized patients could help to prevent serious infections, and it highlights how antibiotic use can have profound impacts on bacteria that are not actually the target of antibiotic treatment.
Researchers tested the patient throughout their time in hospital to track the duration of their infection with Pseudomonas. They used a genetic approach, creating a time-calibrated bacterial family tree that allowed them to analyse the progression and location of infection, plus its evolution. They also found high genetic diversity in the gut, which also suggests that the microbiome may be a reservoir for AMR to arise.
Fortunately, the patient in this case had an immune response to the AMR bacteria in their lungs, preventing the infection from causing pneumonia. However, many people in critical conditions, particularly over winter, have a weakened immune system, meaning the body is less able to fight off disease. AMR policies often focus on reducing infection from external sources, but understanding how AMR can develop and spread within a patient is just as vital.
The researchers now intend to assess how frequently gut to lung bacterial translocation occurs in vulnerable patients by collecting samples from a much larger cohort.
Professor Craig MacLean, Professor at the Department of Biology, said:
‘There is a clear need to develop new approaches to the challenges that antimicrobial resistance presents. Our study shows how gut-lung translocation and antibiotic use can combine to drive the spread of AMR within a single patient. Insights such as this are needed in order to develop new interventions to prevent resistant infections. For example, our study highlights a potential benefit of eliminating AMR bacteria like Pseudomonas aeruginosa from the gut microbiome of hospitalized patients, even when these bacteria are not actually causing infection.’
‘AMR pathogens can be difficult to eliminate from patients once they have become established, and our work also underscores the importance of avoiding unnecessary antibiotic use, and in developing antibacterial treatments that only target the bacteria that are actually causing an infection.’
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The Euglena International Network (EIN), founded in 2020, is a global consortium of hundreds of scientists around the world with the collective goal of supporting euglenoid science through collaborative and integrative omics between academics and industry.
The EIN (https://euglenanetwork.org/) has today published a position paper in Biology Open, outlining the case for a concerted effort to generate high quality reference genomes for the nearly 1,000 known species of euglenoids.
Euglenoids are part of the protist group, home to eukaryotic organisms that do not fit into animal, plant, or fungi groups. These diverse single-celled organisms are found in an exceptionally wide range of ecosystems around the world.
Multiple euglenoid species have translational applications, showing great promise in the production of biofuels, nutraceuticals, bioremediation, cancer treatments, and even as robotics design simulators.