Publisher Health

Researchers identify two sugar-binding proteins that impede the viral entry of circulating SARS-CoV-2 variants. The team, spearheaded by researchers at IMBA — Institute of Molecular Biotechnology of the Austrian Academy of Sciences — may have found the “Achilles’ heel” of the virus, with potential for pan-variant therapeutic interventions. The findings are now published in the EMBO Journal.
Amidst the ongoing COVID-19 pandemic, it is paramount to find new ways to contain the spread of SARS-CoV-2. To this end, the Spike (S) protein is of particular interest as it mediates the main entry mechanism of the virus into host cells. Thus, the interaction of the SARS-CoV-2 S protein with the host cells’ angiotensin converting enzyme 2 (ACE2) determines the infectivity of the virus. The importance of the S protein for the survival and spread of the virus dictates the presence of a camouflage mechanism. Hence, the virus uses so-called glycosylation as a cloaking mechanism to form a sugar coat at specific sites of the Spike protein in order to hide from the host’s immune response.
Spotting the wolf by its sheep’s clothing
The reasoning might seem simple at first sight, but one obvious question immediately surfaced in the team around IMBA group leader Josef Penninger, who is also the director of the Life Sciences Institute at the University of British Columbia (UBC), Vancouver, Canada. Namely: what about the lectins, the sugar-binding proteins? “We intuitively thought that the lectins could help us find new interaction partners of the sugar-coated Spike protein,” says co-first author David Hoffmann, a former PhD student in the Penninger lab at IMBA. The attractivity of this question lies precisely in how spot on it is: the glycosylation sites of the SARS-CoV-2 Spike protein remain highly conserved among circulating variants. Thus, by identifying lectins that bind these glycosylation sites, the researchers could be well on their way to developing robust therapeutic interventions.
Indeed, the team developed and tested a library of over 140 mammalian lectins. Among these, two were found to strongly bind to the SARS-CoV-2 S protein: Clec4g and CD209c. “We now have tools at hand that can bind the virus’ protective layer and thereby block the virus from entering cells,” summarizes Stefan Mereiter, co-first author and postdoctoral researcher in the Penninger lab. Mereiter then exclaims: “This mechanism could indeed be the Achilles’ heel scientists have been longing to find!”
The road from SARS-CoV-2’s “immunity shield” or “sheep’s clothing” to its Achilles’ heel involved several state-of-the-art research techniques. In collaboration with Peter Hinterdorfer of the Institute of Biophysics at the University of Linz, Austria, the team used high-tech biophysical methods to analyze how the lectin binding takes place in detail. For example, the researchers measured which binding forces and how many bonds occur between the lectins and the Spike protein. This also made it clear to which sugar structures Clec4g and CD209c attach.
Therapeutic interventions on the horizon
More good news: the team found that the two lectins bind to the N-glycan site N343 of the Spike protein. This specific site is so crucial to the Spike that it can never be lost in any infectious variant. In fact, a deletion of this glycosylation site renders the Spike protein unstable. In addition, other groups have also shown that viruses with mutated N343 were non-infectious. “This means, that our lectins bind to a glycan site that is essential for Spike function — it is therefore very unlikely that a mutant could ever arise that lacks this glycan,” explains Mereiter.
And the story does not end here. To the team’s excitement, the two lectins also decreased SARS-CoV-2 infectivity of human lung cells. For Josef Penninger and the whole team, these findings hold promise for pan-variant therapeutic interventions against SARS-CoV-2.
Penninger sums up: “The approach compares to the mechanism of the drug candidate ‘APN01’ [Apeiron Biologics], which is undergoing advanced clinical trials. This is a bioengineered human ACE2 that also binds to the Spike protein. When the Spike protein is occupied by the drug, the gateway into the cell is blocked. Now, we identified naturally occurring, mammalian lectins that are capable of doing just that!”
The production of the recombinant SARS-CoV-2 Spike protein under controlled conditions was carried out at the Institute of Biochemistry of the University of Natural Resources and Life Sciences (BOKU), Vienna and coordinated by Prof. Lukas Mach as part of the BOKU Covid initiative. This production respected the precise localization of the conserved sugar chain that allow endogenous lectins to attach the virus. This highly specialized form of glycoprotein analysis has been the research focus of Friedrich Altmann’s group at BOKU for decades. “Although the analysis of the spike glycoprotein is already quite a considerable challenge under normal conditions, it was only possible to perform the necessary measurements in these special times of home-office, distance-learning and hard lock-downs due to the great teamwork of everyone. I would like to express my sincere thanks to all the people involved,” says Johannes Stadlmann, project lead in the Altmann research group at BOKU.
This work involved an international team of researchers including Ali Mirazimi at Karolinska Institutet in Stockholm, Sweden. In addition, several senior researchers in Austria contributed to this work: Johannes Stadlmann, Chris Oostenbrink, Lukas Mach and Friedrich Altmann at BOKU, Peter Hinterdorfer at the Johannes Kepler University Linz, as well as Gerald Wirnsberger at Apeiron Biologics, Vienna.

A team in the PRISMA+ cluster of excellence at the Johannes Gutenberg University in Mainz succeeded in computing how atomic nuclei of the Calcium element behave in collisions with electrons. Results agree very well with available experimental data. For the first time, a calculation based on a fundamental theory is capable of correctly describing experiments for a nucleus as heavy as Calcium. Of particular relevance is the potential that such calculations could have in the future to interpret neutrino experiments. The journal Physical Review Letters reports on the achieved milestone in its current volume.
The new publication stems from the group lead by Prof. Sonia Bacca, Professor for theoretical nuclear physics in the cluster of excellence PRISMA+ , in collaboration with Oak Ridge National Laboratory. Bacca works with great success in predicting various properties of atomic nuclei deriving them from the interactions among their constituents — the nucleons — which can be described within chiral effective field theory. Her research aims at providing a solid connection between experimental observations and the underlying theory of quantum chromodynamics. In physics, such a procedure is described as an “ab initio calculation,” where “ab initio” means “from the beginning” in Latin.
Also cross sections of atomic nuclei probed by external fields, for example through the interaction with electrons or other particles, can be described within the same theory. This procedure is key to explaining existing data and interpreting future experiments, for example in neutrino physics — an important focus of the PRISMA+ research program.
Understanding neutrinos
Neutrinos are elusive particles that are constantly penetrating our Earth but are very difficult to detect and understand. With new planned experiments, such as the DUNE experiment in the USA, scientists want to investigate their fundamental properties, for example, the phenomenon in which one type of neutrinos transform into another — called in technical jargon, neutrino oscillation. In order to achieve that, they need important information from theoretical calculations. Specifically, the relevant question is: How do neutrinos interact with atomic nuclei in the detector?
Since experimental data on the scattering of neutrinos on atomic nuclei are rare, the team of researchers first looked at the scattering of another lepton — the electron — for which experimental data are available. “Calcium 40 is our test system, so to speak,” explains Dr. Joanna Sobczyk, postdoc in Mainz and first author of the study. “With our new ab initio method we were able to calculate very precisely what happens with electron scattering and how the Calcium atomic nucleus behaves.”
This is a great success: Until now it was not possible to carry out such calculations for an element as heavy as Calcium, which consists of 40 nucleons. “We are very pleased that we have succeeded in basically showing that our method works reliably,” says Sonia Bacca. “Now a new era begins, where the ab initio methods can be used to describe the scattering of leptons — these include electrons and neutrinos — on nuclei, even for 40 nucleons.”
“One of the nicest features of our approach is that it allows us to rigorously quantify uncertainties associated with our calculation. Uncertainty quantification is very time-consuming, but extremely important in order to be able to appropriately compare theory against experiment,” comments Dr. Bijaya Acharya, PRISMA+ postdoc and also co-author of the study.
After they were able to show the potential of their method for Calcium, the research team wants to look at the element Argon and its interaction with neutrinos in the future. Argon will play an important role as a target in the planned DUNE experiment.
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Researchers at the University of Colorado Boulder have developed a platform which can quickly identify common mutations on the SARS-CoV-2 virus that allow it to escape antibodies and infect cells.
Published today in Cell Reports, the research marks a major step toward successfully developing a universal vaccine for not only COVID-19, but also potentially for influenza, HIV and other deadly global viruses.
“We’ve developed a predictive tool that can tell you ahead of time which antibodies are going to be effective against circulating strains of virus,” said lead author Timothy Whitehead, associate professor of chemical and biological engineering. “But the implications for this technology are more profound: If you can predict what the variants will be in a given season, you could get vaccinated to match the sequence that will occur and short-circuit this seasonal variation.”
The research team’s secret ingredient? Baker’s yeast.
They developed a genetically modified version of this innocuous material to express some of SARS-CoV-2’s viral spike proteins along the yeast’s surface, with which they can map resulting mutations that form and escape neutralizing antibodies. The resulting roadmap could inform the development of more effective booster vaccines and tailored antibody treatments for patients with severe cases of COVID-19, said Whitehead.
The key to the crown
Spike proteins are sharp bumps that stick out from the surface of viruses in the coronavirus family. Under a microscope, they can appear like a crown, which is where coronaviruses — corona being Latin for “crown” — gain their name, and how they bind to cells like a key in a lock. When antibodies recognize them, latch on, and prevent them from binding to cells, they prevent infection.

In many skin diseases such as atopic dermatitis and acne, the bacterial layer protecting the skin is damaged. “Our goal is to learn the role played in such illnesses by the various kinds of skin bacteria,” says Dr. Martin Köberle, head of the Dermatoinfectology Laboratory at the Klinikum Rechts der Isar of the Technical University of Munich (TUM).
Past efforts by dermatologists to investigate the detailed composition of the microbiome have hit roadblocks. The reason: In conventional cultures grown on agar plates, not all bacteria thrive and multiply equally well. As a result, some slow-growing species can be overlooked entirely. The disadvantage of more recent genetic analytical methods is that large quantities of DNA sequences from skin cells and fragments of dead bacteria are captured. This reduces the information value of the results.
Separating the genetic wheat from the chaff
Dr. Köberle and the biologist Dr. Yacine Amar, both part of Prof. Biedermann’s team at the Clinic and Polyclinic for Dermatology and Allergology at TUM, have developed a method for removing the DNA non-target species in cooperation with an international, interdisciplinary team. They used a special characteristic of the enzyme benzonase. It destroys the nucleotide chains that carry hereditary information in all living things by breaking them down into short fragments. Only live bacteria whose DNA is protected by an outer cell wall escape destruction by the enzyme.
Benzonase has been used for some time, for example to purify proteins: The enzymes break up all foreign DNA and RNA fragments. These can then be removed in a centrifuge, leaving the proteins behind. The selection of skin bacteria functions according to the same principle: Genetic material from skin cells or dead bacteria is broken up by the enzyme and can then be separated from the sample. The remaining bacteria can be destroyed mechanically, permitting the study of their DNA.
“Our experiments showed that, with this method, we can indeed fully eliminate the non-target DNA and select the skin microbiome,” says project leader Yacine Amar. In the lab he initially studied artificial samples containing a mixture of human cells and dead and living bacteria created using a strict protocol and pre-treated with benzonase. “The process then used — known as 16S sequencing — yielded a highly precise picture of the composition of the intact bacteria,” says the researcher. The analysis of real skin swabs was just as successful: No residual DNA from dead bacteria was found in the samples.
Dr. Köberle is confident that this approach will also play a key role in future research: “The enzyme-based selection of living skin bacteria can help us to find microbial biomarkers for certain dermatological illnesses and also to identify the bacteria that have a positive influence on the course of the disease. Perhaps they will be used in treatments one day.” The new method for microbiome analysis is already being used in many cohort studies on skin diseases at the TUM Clinic and Polyclinic for Dermatology.
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Materials provided by Technical University of Munich (TUM). Note: Content may be edited for style and length.

Imagine if you could attach something to your skin without needing glue. A biosensor, a watch, a communications device, a fashion accessory — the possibilities are endless. Thanks to a discovery at Binghamton University, State University of New York, that time could be closer than you think.
Associate Professor Guy German and Zachary Lipsky, PhD ’21, recently published research in the journal Acta Biomaterialia that explores how human skin can control the way cracks form and why tensometers offer imprecise results when measuring the mechanical properties of biological tissues.
Along the way, Lipsky developed a method to bond human skin to rubber-like polymeric materials without an adhesive. Originally a way to make their experiments easier, he and German understood they had made a significant discovery.
“Zach came in one day and said, ‘Yeah, I did it,'” German said. “I was like, ‘How on Earth did you do that? Did you use a glue?’ Because we’d need to account for the mechanical properties of the glue as well. And he said, ‘No, I just stuck it.’ We looked and said: Has this ever been done before? Never been done. So we’re really happy on that front.”
An invention disclosure for the technique has been filed, which could lead to a patent on what he calls “a very simple technique” that could revolutionize biotech.
“I didn’t know we’d end up there, but that’s sometimes how science works,” German said with a laugh.

Phosphate glass is a versatile compound that has generated interest for its use in fuel cells and as biomaterials for supplying therapeutic ions. P2O5-the compound that forms the structural network of phosphate glass, is made up of phosphorus, an element that can adopt many different bonding configurations in combination with oxygen.
The physicochemical properties crucial for the real-life applicability of phosphate glass — for instance, the hydration reaction dictating how quickly a phosphate glass-based biomaterial will dissolve inside the body — depends on the diffusion of ions into the glass. Thus, to improve the physicochemical properties of phosphate glasses, it is important to understand the relationship between the structure and ion diffusion. However, studying such interactions at the atomic level is extremely difficult, prompting scientists to search for a suitable approach to illuminate the details of the ion diffusion process.
Recently, a team of researchers from Nagoya Institute of Technology, led by Dr. Tomoyuki Tamura, has theoretically deciphered the ion diffusion mechanism involved in the hydration reaction process of phosphate glasses. Their study has been published in the Physical Chemistry Chemical Physics journal.
In fully connected P2O5-based phosphate glass, three of the oxygen atoms in each phosphate unit are bonded to neighboring phosphorus atoms. To study the dynamics of ions in the phosphate glass during the hydration process, the researchers used a model made of phosphates with QP2 and QP3 morphologies, that contain two and three bridging oxygens per PO4 tetrahedron, respectively, along with six coordinated silicon structures.
The researchers implemented a theoretical computational approach known as “first-principles molecular dynamic (MD) simulation” to investigate the diffusion of proton and sodium ions into the glass. Explaining the rationale for their unconventional approach, Dr. Tamura says, “First-principles MD simulation enabled us to assume the initial stage of water infiltrating and diffusing into silicophosphate glass and elucidate the diffusion of protons and inorganic ions for the first time.”
Based on their observation, the researchers proposed a mechanism where the protons “hop” and are adsorbed onto the non-bridging oxygen or “dangling” oxygen atom of nearby phosphates through hydrogen bonds. However, in the phosphate glass model they used, the QP2 phosphate units contributed more strongly to the diffusion of protons than the QP3 phosphate units. Thus, they found that the morphology of the phosphate network structure, or the “skeleton” of the glass, greatly affects the diffusion of ions. They also noticed that when a sodium ion was present in the vicinity, the adsorption of a proton onto a QP2 phosphate unit weakened the electrostatic interaction between sodium andoxygen ions, inducing the chain diffusion of sodium ions.
The demand for new biomaterials for effective prevention and treatment is on the rise, and phosphate glasses are well-poised to fulfill this growing need. A large proportion of the population, comprising both elderly and younger people, suffers from diseases related to bone and muscle weaknesses. As Dr. Tamura surmises, “Water-soluble silicophosphate glass is a promising candidate for supplying drugs or inorganic ions that promote tissue regeneration, and our study takes the research in glass technology one step nearer towards realizing the goal.”
Thus, the researchers’ novel insights are bound to have profound real-life impact and lead to breakthroughs in research on fuel cells and bioresorbable materials!
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Scientists at the University of Nottingham have confirmed that an autumn ‘booster’ dose of a Covid-19 vaccine will be an effective way to protect people from existing, and potentially future, variants of concern.
The team of experts found that neutralising antibodies generated by a single dose of the Pfizer vaccine were less effective at neutralising key variants of concern, for example the beta (first identified in South Africa) variant. However, the second dose, especially in those volunteers who had previously been infected with SARS-CoV-2, dramatically increased virus variant neutralising antibody responses (and therefore potential protection) to a level comparable to those seen for the original strain of SARS-CoV-2.
This suggests that an additional boost, even using vaccines containing the original strain of coronavirus, will increase protection against variants of concern.?
The findings, which are published today in Science Translational Medicine, were part of a wider study — PANTHER — looking at healthcare workers over a long period of time and their exposure to Covid-19, and the impact of that past infection and vaccination on their immunity.
The study was funded by a Covid-19 rapid response grant from UKRI and, with the support of the NIHR Nottingham Biomedical Research Centre, made it possible to follow a cohort of healthcare workers from Nottingham University Hospitals Trust since the beginning of the pandemic.
The team identified a smaller group of healthcare workers (within the PANTHER cohort) who were vaccinated with the Pfizer jab. Around half of them were pre-exposed naturally to the virus, and half were not. The team then compared the antibody response in these people.

The calories that children and adolescents consumed from ultraprocessed foods jumped from 61% to 67% of total caloric intake from 1999 to 2018, according to a new study from researchers at the Friedman School of Nutrition Science & Policy at Tufts University. Published August 10, 2021, in JAMA, the study analyzed dietary intake from 33,795 children and adolescents nationwide.
“Some whole grain breads and dairy foods are ultraprocessed, and they’re healthier than other ultraprocessed foods. Processing can keep food fresher longer, allows for food fortification and enrichment, and enhances consumer convenience,” said senior and corresponding author Fang Fang Zhang, nutrition epidemiologist at the Friedman School. “But many ultraprocessed foods are less healthy, with more sugar and salt, and less fiber, than unprocessed and minimally processed foods, and the increase in their consumption by children and teenagers is concerning.”
The largest spike in calories came from such ready-to-eat or ready-to-heat dishes as takeout and frozen pizza and burgers: from 2.2% to 11.2% of calories. The second largest spike in calories came from packaged sweet snacks and desserts, the consumption of which grew from 10.6% to 12.9%.
There was a larger increase in the consumption of ultraprocessed foods among non-Hispanic Blacks (10.3%) and Mexican Americans (7.6%) than non-Hispanic Whites (5.2%). Trends in other racial/ethnic groups were not assessed due to lack of sufficient data that allow for nationally representative estimates across survey cycles.
There were no statistically significant differences in the overall findings by parental education and family income. “The lack of disparities based on parental education and family income indicates that ultraprocessed foods are pervasive in children’s diets,” said Zhang. “This finding supports the need for researchers to track trends in food consumption more fully, taking into account consumption of ultraprocessed foods.”
Over the study period, calories from often healthier unprocessed or minimally processed foods decreased from 28.8% to 23.5%. The remaining percentage of calories came from moderately processed foods such as cheese and canned fruits and vegetables, and consumer-added flavor enhancers such as sugar, honey, maple syrup, and butter.

A University of South Florida (USF Health) preclinical study unexpectedly identified the gene Foxo1 as a potential treatment target for hereditary lymphedema. The research, published July 15 in The Journal of Clinical Investigation, was done with colleagues from Tulane University and the University of Missouri.
Lymphedema — a chronic condition in which lymphatic (lymph) fluid accumulates in soft tissue under the skin, usually in the arms and legs — causes minor to painfully disfiguring swelling. Primary, or hereditary, lymphedema is rare, present at birth and caused in part by genetic mutations that regulate normal lymphatic valve development. Secondary, or acquired, lymphedema is caused by damage to the lymphatic system from surgery, radiation therapy, trauma, or parasitic infection. In the U.S., lymphedema most commonly affects breast cancer patients, with prevalence ranging from 10 to 40% after lymph node removal and radiation therapy.
While lymphedema can be managed with massage and compression garments, no treatment exists to address its underlying cause: the build-up of fluid that eventually backs up in the lymph system like an overflowing sink with a blocked drain. This stagnant lymph triggers an inflammatory response that can induce connective and fatty tissue to form and harden the skin, restricting movement and increasing the risk of recurrent infections.
“The later fibrosis stage of lymphedema cannot be massaged away,” said study principal investigator Ying Yang, PhD, assistant professor of molecular pharmacology and physiology at the USF Health Morsani College of Medicine. “Targeting lymph valves early in the disease is one critical aspect in identifying an effective treatment for lymphedema. If the disease progresses too far, it’s difficult to reverse.”
Valve loss or dysfunction that disrupts the flow of lymph fluid is strongly associated with lymphedema in patients. But no one has discovered whether new valves can be grown or if defective ones can be fixed.
The USF Health-led study shows that both are possible.
Dr. Yang’s group hypothesized that the protein encoded by the gene Foxo1 plays a key role in lymph valve formation based on an earlier USF Health discovery of cell signaling processes controlling formation of lymph valves. The researchers showed that deleting a single gene — lymphatic vessel-specific Foxo1 — promoted the growth of markedly more valves in both young postnatal mice and adult mice than in control littermates without Foxo1 deletion. Furthermore, deleting Foxo1 in a mouse model mimicking human lymphedema-distichiasis syndrome fully restored the both the number of valves and valve function.
“It was exciting to see that Foxo1 is the only gene so far reported that, when deleted, induces more lymphatic valves to form, instead of inhibiting valve growth,” Dr. Yang said. “We actually reversed valve loss and repaired the structure and function of defective valves in a genetic mutation model of lymphedema…That type of discovery makes a study clinically relevant.”
The lymphatic circulatory system — a parallel of the blood vessel circulatory system — helps maintain healthy fluid balance in the body by collecting and controlling the flow of extra lymph fluid that leaks from tissue. This complex network propels watery lymph fluid carrying proteins, nutrients and toxin-destroying immune cells through the body in one direction before returning the fluid to circulating blood. Small valves inside lymph vessels open and close in response to force exerted by the lymph fluid, moving it forward and preventing backward flow into tissues.
Among the key study findings: The protein FOXO1 (encoded by gene Foxo1) inhibits lymph valves from developing by suppressing many genes, which collectively contribute to the multi-step process of making a mature valve. FOXO1 behaves like a brake on a set of valve-forming genes, Dr. Yang said. “Once the brake is removed, all those genes can now be expressed so that new valves can successfully grow.” Inactivation (knockout) of Foxo1 in lymphatic endothelial cells (LEC) of young postnatal mice promoted valve formation at multiple stages. Likewise, deleting LEC-specific Foxo1 in adult mice also increased valve formation, compared to control mice without the gene knockout. A mouse model of lymphedema-distichiasis syndrome had 50% fewer lymphatic valves and the remaining valves closed abnormally and exhibited fluid backflow. But when Foxo1 was deleted, the number of valves increased to the same levels as those in healthy control mice and the structure of defective valves was restored to normal. Further analysis showed that the loss of Foxo1 also significantly improved valve function in this mouse model of human primary lymphedema disease.This study was supported by grants from the National Heart, Lung, and Blood Institute, a part of the National Institutes of Health.
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Materials provided by University of South Florida (USF Health). Original written by Anne DeLotto Baier. Note: Content may be edited for style and length.

Major disruptions to our health and quality of life are front of mind in an era when wildfires, floods, and the ongoing COVID-19 pandemic impact Earth’s population daily. Amid these glaring threats, the slow but rising creep of air and water pollution that humans encounter and even ingest may be easy to overlook, but research continues to reveal new data proving these exposures do impact human health.
In Biophysics Reviews, from AIP Publishing, researchers from the Technical University of Munich review recent scientific literature about the effects of particle contaminants on the mucosal system, an internal membrane that serves as the body’s lubricant and the first line of defense from infections and toxins. These data establish a clear link between exposure to airborne or waterborne particulate matter and several health conditions.
“Mucosal barriers are really important to protect various body systems, but that mucosal function is only there if we don’t damage it,” said co-author Oliver Lieleg. “Sadly, our native mucosal systems are being compromised by micro- and nanoparticles present in our environment.”
Pollution in the air and water has four major effects on the mucosal system. Structural changes can create holes, making the mucosal barrier leaky. Pathogens and toxins can piggyback on the particles and enter the body. Cells can produce too much or too little mucus, and neither is good for preserving optimal function (e.g., when lubricating the eye to protect from abrasion upon blinking). Finally, the quality (e.g., stiffness) of the mucus itself can become altered.
“Mucus is a complex mixture of components, and keeping the composition right is important,” said Lieleg. “Imagine if you add too much flour to the recipe when making a dough. The bread would come out hard and brittle. Contaminating mucus with black carbon or microplastic has similar negative effects and can alter mucus structure and function.”
Natural processes, such as volcanic eruptions, and human activities can both result in problematic particles and produce air contaminants, like soot, and water contaminants, like the microplastics that are ubiquitous in waterways worldwide. Simply breathing, eating, and drinking exposes the body to these contaminants. Some food sources, like honey, may even be surprising in their potential to be tainted, and the effects from these foods could be underestimated.
Recent research on humans and animals demonstrates exposure to particulate matter is often correlated with the development or progression of respiratory and heart diseases as well as various types of cancer, and impaired embryonic development. The mechanisms by which these occur are still largely uncertain, but the effects of particle exposure on mucosal structure and function are likely contributors to various negative health outcomes.
“This is a topic we have to deal with and soon. That is clear as of today,” said Lieleg. “Still, we need more research to better understand which particles pose a threat and why. Those further insights are needed, so we can figure out how best to mitigate these effects.”
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Materials provided by American Institute of Physics. Note: Content may be edited for style and length.