Category: 8. Health

Researchers at the Icahn School of Medicine at Mount Sinai have identified three monoclonal antibodies against monkeypox (also commonly referred to as mpox) that block viral spread and protect against severe disease. The findings provide a potential basis for developing targeted therapies for orthopoxvirus infections.

The findings, published in Cell, reveal that the antibodies – isolated from an individual previously infected with mpox – target a protein called A35. In laboratory studies, the antibodies not only halted viral spread but also shielded rodents from severe illness and prevented death entirely. Importantly, analysis of patient samples showed that people who had been infected with mpox naturally carry high levels of these antibodies and that their presence is linked to milder disease and fewer hospitalisations.

A virus in urgent need of treatment

Mpox has been a global health concern since a multi-country outbreak in 2022. The virus, a close relative of smallpox, is transmitted primarily through direct contact and causes rash, lymphadenopathy and fever. Although most cases resolve, infection can result in permanent scarring and, in severe instances, be life threatening.

Despite repeated warnings from the World Health Organization, which has declared mpox a public health emergency of international concern twice since 2022, there is still no approved drug to treat the disease. Clinical trials of the most advanced candidate therapy have failed to demonstrate effectiveness, highlighting the urgent need for alternatives.

That urgency is precisely what drove the Mount Sinai team.

“A previous study published in 2023 by our team showed that human antibodies targeting the viral protein A35 were unusually increased in sera in response to mpox infection compared with vaccination for smallpox or antibodies against other viral proteins,” explained Dr Camila Coelho, Assistant Professor of Microbiology at Icahn Mount Sinai.

“Based on this earlier finding, we hypothesised that antibodies targeting A35 from mpox-infected individuals would be highly protective against orthopoxviruses, since the viruses in this family share high genetic similarity. We aimed to address the urgent unmet need for effective treatments for orthopoxviruses, and with the help of our outstanding collaborators, I am very proud to say that we are close to achieving that goal.”

What makes the discovery particularly compelling is the antibodies’ binding site. The researchers found that the antibodies latch onto a region of A35 that is highly conserved across not just orthopoxviruses – including mpox – but the entire poxvirus family. As this site is unlikely to mutate, the antibodies are less vulnerable to immune escape, making them robust drug candidates.

“Ours is the first report of the crystal structure of a human antibody bound to an mpox virus protein, providing a detailed map of a vulnerability in the virus,” said Dr Raianna Fantin, postdoctoral researcher and first author of the study.

“It is also the first time that monoclonal antibodies against orthopoxviruses were quantified in human sera. We were surprised by how consistently people recovering from mpox infection produced antibodies targeting the same A35 epitope of the virus as the antibodies we discovered.”

Next steps towards therapy

The Icahn School of Medicine has already patented the antibodies, signalling confidence in their potential clinical use. However, the team is clear that the work is still in its early stages. The antibodies must undergo rigorous preclinical safety checks and eventually human clinical trials before becoming available as a therapy.

For now, the researchers are focusing on two tracks: advancing the antibodies through further testing and leveraging their insights into the immune response to guide future strategies. Their dual approach could yield not only a treatment for mpox but also a foundation for tackling related viruses.

The discovery comes at a critical time. Mpox cases continue to be reported globally and no approved treatments are available. The identification of targeted antibodies offers a potential path toward effective therapy.

Usually, this 8 percent of your DNA — the viral bits — are kept silent. Scientists call it part of the “dark matter” in your genome.

Now scientists at La Jolla Institute for Immunology (LJI) have published a first look at a key viral protein. In a study published in Science Advances, LJI researchers revealed the first three-dimensional structure of a protein from one of these ancient “human endogenous retroviruses (HERVs).”

The team mapped the surface envelope glycoprotein (Env), the antibody target of the most active HERV, marking a milestone in structural biology. “This is the first human HERV protein structure ever solved — and only the third retroviral envelope structure solved overall, after human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV),” says Erica Ollmann Saphire, Ph.D., MBA, LJI President, CEO, and Professor.

This discovery opens the door to new strategies for diagnosing and treating disease. Back in the evolutionary past, HERV-K Env proteins studded the outside of the HERV-K retroviruses. But in modern humans, HERV-K Env proteins show up on the surface of certain tumor cells and in patients with autoimmune and neurodegenerative diseases, making them a valuable target for developing novel diagnostics and therapies.

“In many disease states, like autoimmune diseases and cancer, these genes re-awaken and start making pieces of these viruses,” says Saphire. “Understanding the HERV-K Env structure, and the antibodies we now have, opens up diagnostic and treatment opportunities.”

An unexpected “twist”

Until now, HERV proteins had been invisible. They’ve proven too mobile — and too twitchy — to be seen with even the most sophisticated imaging techniques. Solving the structure of HERV-K Env was especially challenging because the LJI team needed to capture the protein’s delicate “pre-fusion” state.

Envelope proteins are full of potential energy — they’re essentially spring-loaded to merge with a host cell to start the infection process. This means pre-fusion proteins are prone to spontaneous switching to their later, post-fusion state. “You can look at them funny, and they’ll unfold,” says LJI Postdoctoral Fellow Jeremy Shek, who spearheaded the study as co-first author with LJI Postdoctoral Fellow Chen Sun, Ph.D.

To study the three-dimensional structure of HERV-K Env, the researchers introduced small substitutions to lock the protein’s structure in place, while preserving its natural shape. Saphire and her team have used this approach before to reveal the structures of key proteins on Ebola virus, Lassa virus, and more. The researchers also discovered and characterized specific antibodies that helped anchor different versions of the viral proteins.

After stabilizing their HERV-K Env structures, the LJI team used a high-resolution imaging technique called cryo-electron microscopy to capture 3D images of HERV-K Env at three key moments: cell surface, in the act of driving infection, and when it locks together with antibodies.

Many viral envelope glycoproteins have a trimer structure, but HERV-K Env is different from anything scientists had seen before, including trimers from other retroviruses. Unlike the shorter, squatter trimers made by HIV and SIV, the HERV-K Env is tall and lean. Further, the protein’s fold — the weaving together of strands and coils that build the working machine — is unlike any other retrovirus.

A new path for clinical research

The new LJI study opens the door to using HERV-K Env to our advantage. Understanding the HERV-K Env structure, and how antibodies target it, may prove useful for developing diagnostic tools or new therapeutics.

For example, many types of cancer cells — from breast cancers to ovarian cancers — but not healthy cells, are dotted with HERV-K Env proteins. This means antibodies against HERV could distinguish cancer cells from healthy cells. As Sun explains, scientists could develop cancer immunotherapies that zero in on HERV-K Env to track down tumor cells. “We can use it as a strategy to specifically target cancer cells,” says Sun.

People with autoimmune diseases such as lupus or rheumatoid arthritis also express HERV-K Env on their cells. Some scientists suspect that patients’ immune cells see these strange proteins and think the body is under attack. Just like during a normal viral infection, their B cells start making antibodies against HERV-K Env proteins.

“Understanding how antibodies recognize these proteins was challenging because there was no structure and precious few good antibodies yet available,” says Saphire.

So the LJI team made their own panel of antibodies to reveal how the immune system can target the different subunits of the molecule in all its different shapes. Once scientists understand how these antibody attacks work, they can try to intervene and stop harmful inflammation.

The scientists also tested the idea that their antibodies may also be useful tools for diagnosing many autoimmune diseases. They used the antibodies to try and hunt down immune cells in samples from patients with rheumatoid arthritis and lupus. When Saphire and her colleagues tagged these antibodies with a molecular flag, they were able to quickly detect HERV-K Env on neutrophils, a type of immune cell that can cause inflammation.

“These antibodies marked aberrant HERV display on neutrophils from rheumatoid arthritis and lupus patients, but not healthy controls,” says Saphire.

The interest in HERVs is quickly growing, and scientists are finding more and more diseases where HERV-K Env crops up. “We can really pick whatever disease we’re interested in and go down that route,” says Shek.

These projects may someday advance clinical care — and our fundamental understanding of human biology. After all, we’re all part virus. It’s time to get to know that part of ourselves.

Additional authors of the study, “Human endogenous retrovirus K (HERV-K) envelope structures in pre- and postfusion by cryo-EM,” were Elise M. Wilson, Fatemeh Moadab, Kathryn M. Hastie, Roshan R. Rajamanickam, Patrick J. Penalosa, Stephanie S. Harkins, Diptiben Parekh, Chitra Hariharan, Dawid S. Zyla, Cassandra Yu, Kelly C.L. Shaffer, Victoria I. Lewis, Ruben Diaz Avalos, and Tomas Mustelin,

This study was supported by a Curebound Discovery Grant (13502-01-000-408) and by LJI & Kyowa Kirin, Inc. (KKNA-Kyowa Kirin North America; and a Kirin North America Accelerator Grant [18030-01-000-408]).

Nutrition professionals significantly influence consumer choices, and recent research looks at how perceptions of plant-based dairy alternatives shape their inclusion in a healthy diet. We speak to the European Food Information Council (EUFIC) to learn about challenges and opportunities in this space.

The study examined 259 various Spanish nutrition professionals. It shows that they often misunderstand the nutrient value of plant-based dairy alternatives due to their highly variable nutrient profiles, inconsistent fortification levels, and reliance on food-based dietary guidelines.

Their own habits can shape their advice, and they may exclude children and older adults from consuming plant-based dairy alternatives, the study suggests. 

Meanwhile, it warns that nutrition professionals overestimating fortification may cause consumers to miss key nutrients. 

Those who recommend plant-based dairy alternatives believe they are more sustainable and promote a diverse diet, as they are another way of consuming legumes and nuts.

Misunderstandings amok 

EUFIC’s senior research manager, Dr. Katerina Palascha, tells Nutrition Insight why some nutrition professionals may misunderstand plant-based milks.

“Firstly, their nutrient profile is highly variable, as it depends both on the ingredient they are made from (e.g., soy, oats, or coconuts) and the type of product (e.g., drink, yogurt, or cheese), so they cannot be treated as one homogenous group,” she explains.

“Secondly, their level of fortification can be inconsistent across products and brands. Thirdly, some plant-based dairy alternatives in Spain and Portugal contain a mix of different plant-based sources, further increasing the difficulty of making precise recommendations.”

Palascha adds that some of these professionals may focus more on foods included in food-based dietary guidelines because there is more guidance about them. 

The study found that over 70% of professionals want information on fortification, bioavailability, and nutritional composition of plant-based dairy alternatives. Over 60% wanted processing, additives, and environmental impact data.

The availability bias

The research notes that health professionals consider plant-based products compatible with a healthy diet and support their fortification. However, as there is no consensus on their nutritional value compared to dairy products, they believe this brings confusion, including among consumers. 

Palascha explains the availability bias and assures: “If they are professional, they are not likely to give advice that goes against the science. But whatever they are familiar with may come more readily to their minds as a potential option, as it does to everyone.”

“Both our study and previous studies show that health professionals who consume plant-based dairy alternatives themselves are more likely to recommend these products to their clients.”

The study found that those who thought PBDA was nutritionally equivalent to dairy recommended it more frequently than those who were uncertain.

Although 34% of the sample would advise plant-based dairy alternatives to all consumers, the majority of nutritionists would, based on particular demographics, such as adults (52%), those on restricted diets (75%), or those who currently use these products (49%). 

Other target groups include those with allergies, autoimmune diseases, or digestive problems, or those who value sustainability, and menopausal women. 

Age-specific nutrition

Palascha notes that children and older adults need specific nutrients from dairy products, such as protein, calcium, vitamin B12, and iodine. They are also more susceptible to deficiencies in these nutrients.

“Given that milk and dairy tend to provide more bioavailable sources of these nutrients than plant-based dairy alternatives, it needs to be considered whether making PDBA recommendations for these groups may potentially increase the risk of these deficiencies.”

The study shows that most nutrition professionals thought plant-based dairy alternatives were most frequently fortified with calcium (92%), vitamin D (85%), and vitamin B12 (61%), but this is an overestimation. 

According to Palascha, consumers may not be aware that nutrients added to products tend to be less bioavailable than the same nutrient level that is found in food. 

“This is normally not a problem in a balanced, varied diet, but it can be a problem otherwise. But if consumers think they are absorbing more of a nutrient than they are, they may not seek other sources of the same nutrients, which can lead to a nutrient deficiency.”

Previous research shows that animal protein helps early life survival, while plant-based protein is more linked to adult longevity and overall life expectancy.

Question of sustainability

The study reveals that nutrition professionals are curious to learn more about the environmental impact of plant-based dairy alternatives. This highlights the importance of transparency in informing dietary guidelines and supporting professional recommendations.

Those who saw plant-based dairy alternatives as more environmentally friendly than dairy and believed they could completely replace dairy when fortified strongly supported their inclusion in the Spanish dietary guidelines. 

Palascha believes that the decision to use plant-based milk is personal. “Since it is possible to have a nutritious diet that is also environmentally friendly, there is no need to have a trade-off between environmental and personal health.” 

“Effective fortification of plant-based dairy alternatives presents both a challenge and an opportunity to deliver products that are both nutritionally adequate and environmentally friendly,” she concludes.

Alpro funded the research, which was carried out independently by EUFIC from February to August 2025.

In July, the UK called for better plant-based milk fortification. Despite growing consumer interest in these alternatives, the UK’s Scientific Advisory Committee on Nutrition and the Committee on Toxicity of Chemicals in Food, Consumer Products and the Environment concluded that no almond, oat, or soy drink available in the UK was nutritionally equivalent to cow milk as of early 2022.