Two beagles called Alfie and Bailey lack the main protein that causes allergic reactions to dogs, thanks to CRISPR gene editing. The dogs will be 2 years old in September and show no signs of adverse effects, according to , the company behind them.

“I’ve lived with allergies my whole life. They prevented me and my family from ever having a dog,” says Kindred co-founder Matt Walker. “And my wife, Maggie, has always wanted a dog.” Walker previously worked as a researcher studying neuron development in worms by using CRISPR gene editing to disable specific genes. He realised it might be possible to use the technique to prevent dogs causing allergies, and founded Kindred in 2020.

How were Alfie and Bailey created?

Previous studies have found that the main allergen that triggers reactions to dogs is a protein called Can f 1. It is secreted by the tongue and by glands in the skin, so it is present both in the fur of dogs and in their saliva.

The Kindred team took skin cells from a female beagle and used the gene-editing tool CRISPR Cas9 to mutate the Can f 1 gene – the result was an extra DNA letter at the start of the gene that shifts the way the recipe for making the Can f 1 protein is read by cells, turning it into gibberish. Once the team members had confirmed they had made the desired change without introducing unwanted mutations, they cloned the cells. Altogether, the team transferred 25 embryos to a surrogate, of which two implanted and developed to term.

Does removing this protein really prevent allergies?

Bailey is Walker’s pet dog, and he says he has no reaction to her at all. She was cavorting in the background when New Scientist spoke to him. Kindred has also showing that Can f 1 is undetectable in Alfie and Bailey, and that there are no allergic reactions to samples from them in skin-prick tests, whereas samples from normal dogs do provoke a reaction.

However, Can f 1 isn’t the only protein in dogs that can trigger allergic reactions – there are also so-called minor allergens, such as Can f 2. “If we do find that there’s a substantial population that is still responding to the dogs, then that is something we could address,” says Walker.

And could the process be harmful to dogs?

We don’t know for sure what the function of Can f 1 is, but Walker says he was confident from experiments on mice that there would be no serious consequences from deleting it. So far, both dogs appear normal and healthy, he says. “Of course, that’s something that we’re monitoring very closely, and will continue to monitor over the animals’ lives.”

Isn’t it already possible to buy “hypoallergenic” dogs?

Some breeds, such as poodles and goldendoodles, are said to be less likely to trigger allergic reactions, but Walker says he responds just as much to the goldendoodle his parents bought after he left home as he does to any other dog. In the paper, his team shows that Can f 1 is detectable in both breeds, and that samples from them trigger reactions in skin-prick tests.

This is in line with independent evidence. The American Academy of Asthma, Allergy and Immunology says some “hypoallergenic” breeds .��

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When will these dogs be commercially available?

Not for some time. Kindred first needs regulatory approval from the US Food and Drug Administration. If it gets that, it then needs to create lots more of these dogs. For each dog breed, the company will have to create a genetically diverse set of “founder” dogs that can then be bred normally. Walker couldn’t say how many founder dogs would be required per breed.

Is it ethical to genetically engineer dogs just to prevent allergies?

“We aren’t using gene editing for novelty or some cosmetic reason,” says Walker. “Allergies are a real health problem. They affect a significant portion of the population, and lead to serious conditions such as asthma triggering asthmatic attacks.”

By contrast,��conventional dog breeding is often done purely for the sake of appearance, and can introduce mutations that cause serious harm, such as those found in��breeds like pugs��.��Nevertheless, Kindred is altering dogs for the benefit of humans rather than the benefit of the animals themselves. In response to this, Walker says��people discovering they are allergic to dogs is a leading reason for animals having to be rehomed.��

Is Kindred planning to gene-edit cats, too, to prevent allergies?

“Right now, we’re focused exclusively on dogs,” Walker says. The main allergen in cats, called fel d 1, is encoded by two genes rather than one, so getting rid of the protein is more complex. Another company called InBio announced plans to create cats free of fel d 1 in 2022.

The microbiomes in our gut and mouth may determine whether people with a peanut allergy develop a life-threatening reaction. This could help explain why some people with the allergy experience relatively mild reactions, while others develop severe, or even fatal, symptoms.

“There’s a big question around why some patients are more susceptible to more severe reactions,” says at the Autonomous University of Madrid in Spain.

Peanut allergy occurs when the immune system mistakenly identifies proteins in the legume as a threat, causing it to produce excessive amounts of a particular type of antibody. This ramps up inflammation, leading to symptoms such as itching, swelling and vomiting. In extreme cases, peanut exposure causes anaphylaxis, a life-threatening reaction that typically involves breathing difficulties.

Jiménez-Saiz and his colleagues wondered whether the microbes that live on and within us play a role here, given the huge influence that our body’s various microbiomes have on our immune system.

To find out, they inserted a small amount of peanut into the stomachs of three groups of mice without any allergies. The first group was reared to develop no microbiome (known as germ-free mice), while the second had a minimally diverse microbiome, and the third had a microbiome that is typical of a healthy mouse.

Forty minutes later, the team found higher levels of two proteins that play a major role in peanut allergy, known as Ara h 1 and Ara h 2, in the small intestines of the germ-free and minimal-microbiome mice than in those with the most diverse microbiome.

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Further analyses revealed that the latter group carried the highest levels of a group of bacteria called Rothia, especially the strain Rothia R3, which is involved in digesting and degrading peanuts in the gut.

To explore whether Rothia R3 influences anaphylaxis risk, the researchers induced severe peanut allergies in a separate group of mice, which had a minimally diverse microbiome.

They then implanted Rothia R3 into some of their guts, before delivering peanut paste directly into all of the animals’ stomachs. Forty minutes later, all the mice had developed anaphylaxis, but the body temperature of those that received Rothia R3 had dropped by just 2 per cent, on average, compared with 3.5 per cent for the mice that didn’t receive it. Anaphylaxis typically causes a drop in body temperature, which can lead to hypothermia and organ failure.

The Rothia-implanted mice also had about half the levels of an immune molecule called MMCP-1 in their blood, which usually rises during anaphylaxis, compared to the control mice. “The findings are compelling,” says at Imperial College London. “If a similar immunological change occurred in people, you would expect this to reduce the severity of anaphylaxis symptoms.”

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In another experiment involving 19 people with peanut allergies, the team found that those with a greater tolerance of peanuts had substantially higher levels of Rothia bacteria in their saliva than those with more severe allergies. This suggests that the presence of these bacteria in people’s mouths, as well as in their gut, influences their anaphylaxis risk.

Rothia probiotics could one day reduce the severity of anaphylaxis developing during a peanut allergy reaction, says Shamji. “The need for something like this is huge,” he says. It could particularly alleviate fear around accidental exposure to peanuts and reduce the risk of adverse reactions during oral immunotherapy, which aims to treat allergies by gradually exposing people to increasing doses of an allergen, he says.

The team hopes to demonstrate the potential of such a treatment in a clinical trial by giving people with peanut allergies either Rothia probiotics or a placebo, before exposing them to low levels of peanuts, says Jiménez-Saiz.

Mice can be protected from the life-threatening allergic reaction anaphylaxis for at least a year using an experimental vaccine. The hope is that it will work in humans too.

The threat of anaphylaxis constantly hangs over hundreds of millions of people globally, with allergies to foods like peanuts or shellfish one common risk factor. In the UK, for example, around 6 per cent of adults – or 2.4 million people – are .

Eating contaminated food, or , can cause a spike in molecules produced by the immune system called immunoglobulin E (IgE) antibodies, leading to swelling of the tongue or throat, difficulty breathing and a drop in blood pressure. This can result in a hospital visit – even if you have an adrenaline auto-injector like an EpiPen on hand to reverse the symptoms. In severe cases, anaphylaxis can be fatal.

Aside from attempting to avoid the allergen, options to prevent such attacks are limited. You can try oral immunotherapy, which involves consuming small, gradually increasing amounts of an allergenic food under supervision to build tolerance, or take a drug called an anti-IgE monoclonal antibody, such as omalizumab, which binds to IgE, stopping it from causing a reaction. But omalizumab is expensive and needs to be injected every few weeks, potentially for life.

Now, at the Toulouse Institute for Infectious and Inflammatory Diseases, France, and his colleagues have developed a vaccine named IgE-K. This primes the immune system to produce antibodies that target IgE, preventing it from binding to its receptors on immune cells, and halting a subsequent runaway allergic reaction.

“We wanted to come up with a solution that could be long-term, because when you are food allergic, you can be exposed anytime by accident, so you really want to be protected all the time,” says Reber.

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In tests on mice modified to produce a human version of IgE, the researchers found that two doses of the vaccine induced the mice to generate neutralising antibodies against IgE.

“It blocks up the molecule that makes us allergic,” says at McMaster University in Ontario, Canada.

The researchers then gave the mice a substance that would cause an allergic reaction. Unvaccinated mice had a strong reaction, but vaccinated ones were protected against anaphylaxis for as long as a year without showing any adverse effects.

“It could be longer, but we haven’t tested longer,” says Reber.

IgE is part of the body’s immune system, and as well as generating allergic reactions, it fires up in response to venoms and some intestinal parasites. “It’s probably an ancestral system that helps fight against toxins,” says Reber.

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Reber says many people at risk of serious allergic reactions have received anti-IgE therapies for years without discontinuation and experienced no ill-effects, so there is good evidence that it is safe to target the molecule long-term. But to see whether dampening down IgE could reduce the body’s effectiveness at fighting parasites, the researchers did an additional experiment in mice. They found that the vaccine didn’t impair the immune response to an infection by Strongyloides ratti, a parasitic nematode worm.

Koenig is optimistic that such a vaccine would be effective in people. “They know that the mouse made the antibody that bound up the human IgE molecule properly. If humans make that same molecule, then I think there’s a pretty high chance that this will work out quite nicely.”

Still, clinical trials are needed to evaluate the vaccine’s safety, efficacy and duration in humans, says Reber. If it does come to market, he thinks it could be a cost-effective way to treat people with severe allergies because it would require far fewer injections than an anti-IgE monoclonal antibody like omalizumab.

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Around one in seven cases of life-threatening allergic reactions seem to be caused by foods not typically labelled as potential allergens on a product’s packaging, prompting researchers to argue policies around this need to change.

Food allergies are becoming more common, but many official allergen lists have not been updated in years. For instance, the European Union’s states the presence of 14 food allergens, like peanuts and soya, must be made clear on products, but is based on data from 2011.

To understand the lesser-known triggers, at Centre Hospitalier Universitaire de Reims in France and her colleagues analysed 2999 cases of food-induced anaphylaxis – a life-threatening reaction – voluntarily reported by doctors to the Allergy-Vigilance Network, which collects data from French-speaking countries, between 2002 and 2023.

They were specifically looking for emerging food allergens, which they defined as any foods that were not on the European mandatory labelling list, but which were individually responsible for at least 1 per cent of cases.

The team found goat or sheep milk and buckwheat triggered 2.8 and 2.4 per cent of cases, respectively. These were followed by peas and lentils, alpha-gal – a sugar that can trigger an allergy to red meat and other mammalian products – pine nuts and kiwi, which each set off between 1 and 2 per cent of incidences. Apples and beehive products like edible pollen, honey and royal jelly caused 1 per cent of cases.

Overall, emerging food allergies were responsible for 413 – roughly 14 per cent – of the reported cases.

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In terms of reaction severity, goat and sheep cheese provoked particularly dangerous reactions, especially in young boys, causing two deaths. Recurrent reactions and hidden exposure – like in a sauce or as a thickener – were most common with goat or sheep milks and cheeses, followed by peas and lentils, buckwheat and pine nuts.

Off the back of this, the team has suggested these four food types be added to the list of mandatory warning labels in Europe, which states the presence of these ingredients must be emphasised, for instance, by being written in bold on the packaging.

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“Our main goal is to protect allergic consumers and ensure they have access to clear information,” says Sabouraud-Leclerc. “This is all part of good patient care: diagnosis, education, emergency kits and knowing how to read labels.”

While the data came mainly from France, Belgium and Luxembourg, the results would probably be applicable to other countries, with some differences in prevalence depending on local cuisine, says Sabouraud-Leclerc. “If we manage to update the EU list, that might inspire other countries to follow, kind of like a snowball effect,” she says.

People with hay fever could one day benefit from a first-of-its-kind “molecular shield” that blocks pollen from entering the lining of the nose, and is unlikely to cause the side effects seen with standard treatments.

Hay fever is an allergic reaction that occurs when pollen binds to molecules called IgE antibodies in the lining of the nose, mouth and eyes, triggering inflammation that results in symptoms such as sneezing and itchiness. Treatments include antihistamines and steroids, which dampen inflammation, but aren’t always effective and commonly have side effects, such as drowsiness.

To find an alternative, at the Kazakh National Agrarian Research University in Kazakhstan and his colleagues first collected blood samples from mice. They then extracted an antibody that isn’t involved in allergic reactions, but still binds to the main allergen in mugwort pollen, a major cause of hay fever. This binding then blocked the allergen from attaching to IgE antibodies in a lab dish. “It acts like a molecular shield,” says Tabynov.

To see if this reduces irritation, the researchers induced mugwort pollen allergies in 10 mice by injecting them with the allergen and a chemical that trained their immune systems to react to it.

A week later, they put a small droplet of liquid containing the pollen-blocking antibody into the noses of half the mice, doing so a total of three times over five days. The remaining animals were given droplets of saline solution instead. One hour after each droplet was administered, the mice were exposed to mugwort pollen at levels similar to those that people are exposed to during the plant’s peak hay fever season, says Tabynov.

After the final droplet, the mice given the preventive antibody rubbed their noses 12 times, on average, over 5 minutes, versus 92 times in the saline group.

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The researchers expected that the antibody reduced inflammation, which they confirmed when imaging nose tissue samples collected from the mice at the end of the study. This also showed that the treatment had effects deeper within the body, not just where the droplets were applied. “Our study is the first to demonstrate that an allergen-specific monoclonal antibody can be applied intranasally to achieve both local and systemic protection in the context of plant pollen allergies,” says Tabynov.

Although the researchers didn’t measure potential side effects, they don’t expect the approach to cause the adverse events seen with oral hay fever drugs, because it works at the site of allergen entry.

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“This study is an important milestone, highlighting the potential of intranasal therapies for allergic rhinitis [hay fever] and helps pave the way for early clinical trials investigating the potential of this approach in humans,” says at Stanford University in California.

But success in mice may not translate to efficacy in people and the antibody will need to be adapted to work in humans to ensure it doesn’t provoke its own immune reaction, says Tabynov. If all goes smoothly, the team hopes to trial the approach as a nasal spray in people within the next two to three years, he says.

Such sprays may also work against other types of pollen that cause hay fever. “We envision a future in which customised antibody sprays could be available for people allergic to different types of pollens,” says Tabynov.

Adults with peanut allergy reduced their risk of reactions by eating a little peanut protein every day as part of a trial. This approach is already approved in the US for children with the condition.

Peanut allergy occurs when the immune system mistakenly identifies proteins in the legume as a threat. It responds by producing more IgE antibodies, which are a vital part of the immune response, but go into overdrive with allergic reactions. As a result, inflammation ramps up, causing symptoms such as swelling, itching and vomiting. In extreme cases, it can lead to anaphylactic shock, a life-threatening reaction that can affect someone’s breathing or their heart rate.

Until recently, the only solution was to avoid peanuts, but an intervention called oral immunotherapy was approved for children with the allergy in the US in 2020. This involves training the immune system to tolerate the allergen by exposing it to gradually increasing doses of peanut proteins.

However, it was unclear if the approach also worked in adults. “Most of the life of a peanut allergic individual is spent as an adult, but we’ve had no treatment to reduce their underlying reactivity to peanuts,” says at King’s College London. “There are some grounds for suspecting that adults would be more hard to desensitise than children because your immune system is easier to modify when you’re younger.”

To fill this knowledge gap, Till and his colleagues recruited 21 adults with peanut allergy. At the start of the study, the participants were only able to eat up to an eighth of a peanut, on average, before having an allergic reaction.

The team had each participant eat the protein equivalent of one 40th of a peanut every day for two weeks. This dose was slightly increased every two weeks for several months, until they could safely and consistently eat the protein equivalent of four large peanuts every day for a month.

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Three participants dropped out of the study due to allergic reactions, while three others left due to reasons unrelated to the treatment. “This dropout number is acceptable for this kind of treatment,” says at the Swiss Institute of Allergy and Asthma Research.

The remaining 15 participants took part in an allergy test where they ate increasing doses of peanut protein under the researchers’ supervision. All but one of them was able to eat the equivalent of five peanuts without having an allergic reaction.

In another part of the experiment, the team analysed blood samples collected from the participants before and after they received oral immunotherapy. This revealed that the intervention caused them to have higher levels of IgG antibodies, which counteract the effects of IgE antibodies.

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“It is very promising,” says Akdis. “This approach could mean that adults with peanut allergy can be relieved of the anxiety of eating food contaminated with peanuts.”

But this was a relatively early-stage trial, and larger ones are needed to verify the results and establish how long the protection lasts, he says. “I’d expect you’ll need to take daily or regular doses of peanuts in the long term to maintain the tolerance to the allergen,” says Akdis. “People take pills every day, so I think people affected by peanut allergies may well be fine adhering to this sort of method.”

Speak to your doctor before seeking new treatments for medical conditions.

There is no strong evidence that people with peanut allergies are at risk of a severe reaction from others eating peanuts and the allergens circulating through the air while on board a plane. While peanuts are technically legumes, it is thought the findings will also apply to nuts and other foods that people are commonly allergic to.

People with food allergies may experience symptoms such as rashes, nausea and breathlessness after being exposed to allergens through eating, skin contact or inhalation. In severe cases, this can cause a life-threatening reaction called anaphylaxis, which can lead to swelling of the throat, dizziness and more serious breathing difficulties.

Some airlines have banned the sale of nuts on flights and their staff make announcements asking passengers not to eat them if they know someone on board has an allergy.

To explore the evidence behind the inhalation risk, at Imperial College London and his colleagues focused on peanuts, reviewing the results of five studies.

One study looked for peanut particles in air samples during a commercial flight where the snack was being served. The researchers found none in nearly all the samples they collected. That is because these aircraft have filters that remove peanut particles in the air before they spread through the cabin, says Turner.

The exception was air samples collected immediately around tray tables where peanuts were being consumed, but these allergens were at such low levels that they would probably be insufficient to cause an allergic reaction, says Turner.

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Four other studies looked at airborne allergen levels as people ate or shelled peanuts, either in their homes or a lab. They similarly found very low levels of allergens within about half a metre of someone shelling or eating peanuts. At most, this would cause mild allergic reactions, such as watery eyes, says Turner.

But higher levels of allergens were found on seats, trays and the floor of the first study’s aircraft. Wiping down these surfaces would probably remove much of the risk, says Turner, whose team is working with UK airlines to make flying safer for people with allergies.

The same results would probably apply to other allergens, such as nuts, seafood and eggs, says Turner.

“This report summarises what has been well established for years, in that peanut is highly unlikely to aerosolise and pose an airborne risk to passengers,” says at the University of Colorado.