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The Catfish that Strands Itself to Kill Pigeons

In Southwestern France, a group of fish have learned how to kill birds. As the River Tarn winds through the city of Albi, it contains a small gravel island where pigeons gather to clean and bathe. And patrolling the island are European catfish—1 to 1.5 metres long, and the largest freshwater fish on the continent. These particular catfish have taken to lunging out of the water, grabbing a pigeon, and then wriggling back into the water to swallow their prey. In the process, they temporarily strand themselves on land for a few seconds.

Other aquatic hunters strand themselves in a similar way, including bottlenose dolphins from South Carolina, which drive small fish onto beaches, and Argentinian killer whales, which swim onto beaches to snag resting sealions. The behaviour of the Tarn catfishes is so similar that Julien Cucherousset from Paul Sabatier University in Toulouse describes them as “freshwater killer whales”.


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Pygmy Mole Crickets Leap from Water with Spring-Loaded Oars

When Malcolm Burrows first heard the sound of a pygmy mole cricket leaping from water, he was enjoying a sandwich. Burrows, a zoologist from the University of Cambridge, was visiting Cape Town and had snuck out the back of the local zoology department to eat his lunch by a pond. “I heard sporadic thwacking noises coming from the water,” he says. “When I looked more closely I could see small black insects jumping repeatedly from the water and heading towards the bank.”

They were pygmy mole crickets, a group of tiny insects just a few millimetres long. Despite their name, they’re more grasshoppers than crickets, and are some of the most primitive members of this group. They’re found on every continent except Antarctica.

Pygmy mole crickets cannot fly, but they can certainly jump. Burrows collected some of the individuals from the pond, and took them back to the lab to film them with high-speed cameras. When they take off, they often spin head-over-tail, but what they lack in elegance they make up for in distance. They can jump over 1.4 metres, more than 280 times their own body length.

Doing this on land is one thing, but as Burrows saw at the pond, these insects can also jump from water. This ability serves them well—they live in burrows near to fresh water, which frequently flood. Their leaps send them back to terra firma, saving their lives.

Burrows found that these insects jump from water in a completely new way. Animals like pond-skaters and the basilisk lizard can walk on water by relying on surface tension—the tendency of the surface of water to resist an external force. But the mole cricket extends its hind legs so quickly that they break right through the surface.

As the legs move through the water, three pairs of flat paddles and two pairs of long spurs flare out from each one. These structures have a concave shape, much like an oar. As they flare out, they increase the surface area of the mole cricket’s leg by around 2.4 times, allowing it to push down on a much larger volume of water. And once the legs are fully extended, the paddles retract to reduce the drag on the airborne insect. From water, the mole crickets can only jump for 3 centimetres or so. That’s pathetic compared to their land-based attempts, but still more than 5 times their body length, and enough to save them from drowning.

When Burrows shone ultraviolet light onto the paddles, they glowed with a bright blue colour at their bases. That’s the signature of resilin, an incredibly elastic protein that powers the jumps and wingbeats of many insects. Its presence on the mole cricket suggests that the paddles and spurs are spring-loaded.

“It just shows what amazing things can be found close to where we live and work,” says Burrows. “Instead of spending time exploring the more exotic parts of South Africa, I spent most of my visit there essentially looking outside my back door.”

Reference: Burrows & Sutton. 2012. Pygmy mole crickets jump from water. Current Biology 22: R990

All photos and video by Malcolm Burrows

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DNA Lego Bricks Produce Nano-Sculptures

For tens of thousands of years, humans have created sculptures by carving pieces from a solid block. They have chipped away at stone, metal, wood and ceramics, creating art by subtracting material. Now, a group of scientists from Harvard University have figured out how to do the same thing with DNA.

First, Yonggang Ke builds a solid block of DNA from individual Lego-like bricks. Each one is a single strand of the famous double helix that folds into a U-shape, designed to interlock with four neighbours. You can see what happens in the diagram below, which visualises the strands as two-hole Lego bricks. Together, hundreds of them can anneal into a solid block. And because each brick has a unique sequences, it only sticks to certain neighbours, and occupies a set position in the block.

This means that Ke can create different shapes by leaving out specific bricks from the full set, like a sculptor removing bits of stone from a block. Starting with a thousand-brick block, he carved out 102 different shapes, with complex features like cavities, tunnels, and embossed symbols. Each one is just 25 nanometres wide in any direction, roughly the size of the smallest viruses.


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The world’s shiniest living thing is an African fruit that looks like a pointillist bauble

In the forests of central Africa, there’s a plant that looks like it’s growing its own Christmas decorations. Shiny baubles sprout from between its leaves, shimmering in a vibrant metallic blue. Look closer, and other colours emerge – pinpricks of red, orange, green and violet. It looks as if Seurat, or some other pointillist painter, had turned their hand to sculpture.

But these spheres, of course, are no man-made creations. They’re fruit. They are the shiniest fruits in the world. Actually, they are the shiniest living materials in the world, full-stop.

They belong to a plant called Pollia condensata, a tropical metre-tall herb that sprouts its shiny berry-like fruits in clusters up to 40-strong. These little orbs are iridescent – they use special layers of cells, arranged just so, to reflect colours with extraordinary intensity. This trick relies on the microscopic physical structures of the cells, rather than on any chemical pigments. Indeed, the fruits have no blue pigment at all.

In the animal kingdom, such tricks are commonplace – you can see them at work on the wings of a butterfly, the shells of jewel beetles, or the feathers of pigeons, starlings, birds or paradise and even some dinosaurs. But in the plant world, pigments dominate and structural colours were thought to be non-existent are much rarer.


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Everything you never wanted to know about the mites that eat, crawl, and have sex on your face

New Scientist published a story yesterday stating that rosacea – a common skin disease characterised by red blotches on one’s face – may be “caused” (more on this later) by “tiny bugs closely related to spiders living in the pores of your face.” Tiny bugs that “crawl about your face in the dark”, lay eggs in your pores, and release a burst of faeces when they die.

This is the terrifying world of the Demodex mite. And by “terrifying world”, I mean your face. For anyone who wants to know more, and who isn’t currently clawing at their cheeks or bleaching their head (health tip: don’t), here’s everything you never wanted to know about your face-mites.


Say hello to my little friend

Mites are relatives of ticks, spiders, scorpions and other arachnids. Over 48,000 species have been described. Around 65 of them belong to the genus Demodex, and two of those live on your face. There’s D.folliculorum, the round-bottomed, bigger one (top image, above) and there’s D.brevis, the pointy-bottomed, smaller one (bottom image, above). These two species are evolution’s special gift to you. They live on humans and humans alone. Other Demodex mites have similarly specific preferences: D.canis, for example, is a dog-lover.

Both species are sausage-shaped, with eight stubby legs clustered in their front third. At a third of a millimetre long, D.folliculorum is the bigger of the two. It was discovered independently in 1841 by two scientists, but only properly described a year later by Gustav Simon, a German dermatologist. He was looking at acne spots under a microscope when he noticed a “worm-like object” with a head and legs. Possibly an animal? He extracted it, pressed it between two slides, and saw that it moved. Definitely an animal. A year later, Richard Owen gave the mite its name, from the Greek words ‘demo’, meaning lard, and ‘dex’, meaning boring worm. The worm that bores into fat. I can only assume that Simon and Owen spent the rest of their lives feeling a little itchy.

These mites are our most common ectoparasites (those that stay on the surface of our bodies, rather than burrowing inside). They’ve been found in every ethnic group where people have cared to look, from white Europeans to Australian aborigines to Devon Island Eskimos. In 1976, legendary mite specialist William Nutting wrote:

“One can conclude that wherever mankind is found, hair follicle mites will be found and that the transfer mechanism is 100% effective! (One of my students noted it was undoubtedly the first invertebrate metazoan to visit the moon!)”

But it’s hard to say exactly how common they are. The first estimate came from a 1903 study, which found the critters in 49 out of 100 French cadavers. The next count, from 1908, found them in 97 out of 100 German cadavers. The nationalities are probably a red herring. What’s clearer is that age matters. The mites aren’t inherited at birth, so each generation picks them up anew, probably from direct contact with our parents. Thanks, parents! If you’re under 20, good news! A French study from 1972 says that you’ve only got a 4 percent chance of carrying Demodex. If you’re old, bad news! You’ve almost certainly got Demodex somewhere.

The mites spend most of their time buried head-down in our hair follicles – the stocking-shaped organs that enclose and produce our hairs. They’re most commonly found in our eyelids, nose, cheeks, forehead and chin. That’s not to say they’re restricted to the face: Demodex has been found in the hairs of the ear canal, nipple, groin, chest, forearm, penis, and butt too. Generally, dry skin is a turn-off for them. They prize bodily real estate that’s flooded with oils (sebum). This explains why they love your face. It might also explain why their numbers are apparently higher in the summer, when hot temperatures ramp up sebum production.

A mite-y existence

How do Demodex mites spend their time? They eat! Some say they eat sebum, but Nutting thought that such a diet wouldn’t be nutritious enough. Instead, he said that they feast on the cells that line the follicle, sucking out their innards with a retractable needle in the middle of a round mouth. On either side of the mouth, D.folliculorum has a seven-clawed organ (a “palpus”) for securing itself to what it’s eating. “All of the structures formed a sharp, offensive weapon,” writes Xu Jing, who first looked at them under an electron microscope. (D.brevis, with its five-clawed palpus, was branded as “less offensive”.)

They crawl! They move about in darkness and freeze in bright lights. The fact that mites have been found on the surface of the skin suggests that they emerge from follicles at night for shadowy strolls across our faces. With their stumpy legs, they’re hardly fast. It would take almost half a day for Demodex to cover the distance from your ear to your nose.*

They don’t poo! The mite has no anus, and stores its waste in large cells within its gut. Nutting saw these as adaptations for a life spent head-down in a tightly closed space. When the mite dies, its body disintegrates and the waste is released. More on this later.

And they have sex! On your face! Their favourite hook-up spots are the rims of your hair follicles. Males outnumber females by three to five times, but this detail aside, Demodex sex lacks much of the horror found throughout the arachnid clan. No traumatic insemination. No cannibalism. The penis and vulva are hidden within the pairs of legs. (Jing wrote that D.folliculorum’s penis “looks like a small candle when it was elongated”. He failed to see D.brevis’s.)

After sex, the female buries into the follicle (if it’s D.folliculorum), or into a nearby sebaceous gland (if it’s D.brevis). Half a day later, she lays her eggs. Two and a half days later, they hatch. The young mites take six days to reach adulthood, and they live for around five more. Their entire lives play out over the course of two weeks.

People with rosacea should look away now

Are they parasites, or something more benign? For the most part, it seems that they eat, crawl and mate on your face without harmful effects. They could help us by eating bacteria or other microbes in the follicles, although there’s little evidence for this. Their eggs, clawed legs, spiny mouthparts, and salivary enzymes could all provoke an immune response, but this generally doesn’t seem to happen.

But like many of our body’s microscopic residents, Demodex appears to be an opportunist, whose populations bloom to detrimental numbers when our defences are down. Several studies, for example, have found that they’re more common in people with HIV, children with leukaemia, or patients on immunosuppressive drugs. Perhaps changes to the environment of the skin also allow the mites to proliferate beyond their usual levels.

In dogs, an overabundance of D.canis can trigger a potentially lethal condition called demodectic mange, or demodicosis. In humans, these blooms have been linked to skin diseases like acne, rosacea and blepharitis (eyelid inflammation). The New Scientist piece will undoubtedly bring this to many people’s attention, but scientists have been talking about such connections for decades. The rosacea link was first put forward in 1925!

Dermatologists have since repeatedly found that Demodex is more common in the cheeks of people with rosacea. In one study, those with the condition had an average of 12.8 mites per square centimetre of skin, compared to 0.7 in unaffected people. And according to an analysis of 48 separate studies, people with rosacea are eight times more likely to have a Demodex infestation. Obviously, correlation not causation, blah blah blah, you know the drill.

There’s plenty of anecdotal evidence about mite-killing treatments and clinical improvements (here’s the latest involving tea-tree oil), but very little in the way of hard clinical trial evidence. An example: metronidazole is sometimes used to treat Demodex infestations, and there’s evidence from three clinical trials that it’s effective at treating rosacea (a Cochrane review, and everything!). Then again, Demodex can survive high concentrations of metronidazole, so maybe the mites are irrelevant to the substance’s actions.

In the new review, covered by New Scientist, Kevin Kavanagh suggests that rosacea may be caused not by the mites themselves, but by the bacteria in their faeces. After all, antibiotics that kill the bacteria, but are harmless to the mites, can sometimes successfully treat rosacea. But again: more correlations. The bacterial angle is fascinating, though. We know so little about these creatures that colonise our bodies, and now we must contend with our even greater ignorance of the creatures that colonise their bodies. Down the rabbit-hole we go!

And finally, if all of this sounds unbearably revolting, spare a thought for people with acarophobia – the fear of mites and other “small bugs that cause itching.” What words of solace can we offer to them? Here’s Nutting:

“Those patients with acarophobia (approximately 12 have been seen in our laboratory) seem curable if they follow a prescription which includes a relaxing vacation at the beach. If they insist on a follow-up examination for hair follicle mites, the situation is a bit delicate because most will still be positive. Diplomacy will prevail—only two of our 12 have failed to respond!”

Images: top photos from Nutting, 1976, HAIR FOLLICLE MITES (ACARI: DEMODICIDAE) OF MAN.

* One review I read quoted their speed at 16 centimetres per hour. Another said 16 millimetres. Given the stubby legs, the centimetre value surely cannot be right, so I’m going with millimetres.

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One gait-keeper gene allows horses to move in unusual ways

Icelandic horses can move in an odd way. All horses have three natural gaits: the standard walk; the two-beat trot, where diagonally opposite pairs of legs hit the ground together; and the four-beat gallop, where the four feet hit the ground in turn.  To those, Icelandic horses add the tölt. It has four beats, like the gallop, but a tölting horse always has at least one foot on the ground, while a galloping one is essentially flying for part of its stride. This constant contact makes for a smoother ride. It also looks… weird, like watching a horse power-walk straight into the uncanny valley.

The tölt is just one of several special ambling gaits that some horses can pull off, but others cannot. These abilities can be heritable, to about the same extent that height is in humans. Indeed, some horses like the Tennessee Walking horse have been bred to specialise in certain gaits.

Now, a team of Swedish, Icelandic and American scientists has shown that these special moves require a single change in a gene called DMRT3. It creates a protein used in neurons of a horse’s spine, those which coordinate the movements of its limbs. It’s a gait-keeper.


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Robins start with a magnetic compass in both eyes, and end up with just one

Here’s an amazing fact: Adult robins have a magnetic compass in their right eye that allows them to sense the direction of the Earth’s magnetic field, and navigate when all other landmarks are obscured. Here’s an even more amazing fact: Baby robins have two such compasses, one in each eye. They lose the left one as they grow up.

Robins kick-started the study of magnetic senses in the first place. In the 1950s, a German biologist called Hans Fromme showed that robins would always try to escape from a cage in the same direction when it came time to migrate. Even though they had no visual bearings, they headed south-west, as if sunny Spain lay just beyond their cages. In 1966, the husband and wife team of Wolfgang and Roswitha Wiltschko showed that a powerful magnet could disrupt this constant vector, sending them skittering in all sorts of directions.

The Wiltschkos have been studying the magnetic sense of robins ever since. In the 1980s and 1990s, they showed that their compass depends on light. They need some of it, and blue-green wavelengths in particular, to find their way. And in 2002, they showed that the compass lies in just one eye – the right one. If they wore a one-sided goggle that blocked their left eye, they could navigate just fine within their featureless cages. If their right eye was blocked, they headed in random directions.  It’s not just robins. They right-eye compasses that the Wiltschkos discovered also exist in Australian silvereyes, homing pigeons and domestic chickens.


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Reading your body clock with a molecular timetable, inspired by flowers

What time is it? That’s easy to check: Just look at a watch or a clock. What time is it inside your body? That’s a harder question.

Your body keeps its own time. It has an internal 24-hour “circadian clock” that drives the rise and fall of many molecules. Everything from brain activity to hormone levels waxes and wanes according to these molecular metronomes, which dictate how hungry, hot and sleepy we are.

They also affect how well we respond to medicine. Since the late 1980s, scientists have shown that drugs work better at certain times of the day. For example, the cancer drug cisplatin is more effective and less toxic if it’s given in the evening. Adriamycin is more of a morning drug. In another cancer trial, tailoring chemotherapy to these daily rhythms—a practice known as chronotherapy—made the same drugs more effective and reduced the frequency of toxic side effects.

Chronotherapy would seem to be a no-brainer but it hasn’t caught on widely. That may be partly due to scepticism, but there’s a more practical reason: it’s hard to read a person’s body clock. Some people are larks, others are owls. The ticks and tocks of the clock vary depending on age, sex, health, employment, and more. The clocks of two people can be half a day apart. How do you administer a drug at the right time if you can’t tell that time?

The conventional way would be to take blood samples every hour or so for 24 hours, and measure the concentrations of melatonin—a hormone that rises in darkness and falls in light. Melatonin can be detected in saliva samples but because the hormone is found in such low concentrations, the process can’t be automated. As such, it’s labour-intensive work that takes days and tightly controlled environmental conditions. If you have patients to treat, you rarely have such luxuries.

Takeya Kasukawa and Masahiro Sugimoto from the RIKEN Center for Developmental Biology have a better way. Their team have developed a “metabolite timetable”  that plots how dozens of molecules rise and fall in relation to one another. With this timetable, they could accurately read a person’s internal clock with just two blood samples, taken 12 hours apart.


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Unlike humans, chimpanzees only punish when they’ve been personally wronged

When Delta Airlines refused to let Arijit Guha board a plane because his T-shirt made passengers uncomfortable, others made Delta aware of their outrage. When Samsung infringed Apple’s copyright, a jury of independent peers awarded Apple more than $1 billion in damages. When Republican Todd Akin claimed that women could stop themselves from becoming pregnant if raped, people called for his head.

These recent events all illustrate a broad human trait: we seek to punish people who do wrong and violate our social rules, even when their actions don’t harm us directly. We call for retribution, even if we have nothing specific to gain from it and even if it costs us time, effort, status or money to do so. This “third-party punishment” is thought to cement human societies together, and prevents cheats and free-riders from running riot. If you wrong someone, and they’re the only ones who want to sanction you, the price of vice is low. If an entire society condemns you, the cost skyrockets.

Do other animals do the same thing? It’s not clear, but one group of scientists believes that our closest relative – the chimpanzee – does not. Katrin Riedl from the Max Planck Institute for Evolutionary Anthropology in Leipzig, Germany found that chimpanzees will punish individuals who steal food from them, but not those who steal food from others. Even if the victim was a close relative, the third party never sought to punish the thief. These were the first direct tests of third-party punishment in a non-human animal, and the chimps got an F.


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Are those the gut microbes of an unhealthy person, or a pregnant one?

A pregnant woman isn’t just eating for one, but for trillions. Aside from her baby, she’s also home to a multitude of bacteria and other microbes. They have been part of her life since she herself emerged from a womb, and they have influenced her health ever since. Now, as she enters her third trimester, her microbe community is radically changing.

The diversity of species is falling, while certain groups are rising to the fore. Oddly enough, the whole community starts to resemble the microbes of someone with metabolic syndrome – a collection of symptoms that increase the risk of diabetes and heart disease, such as obesity, high blood sugar levels, and inflammation. It’s a good reminder that context matters. These “unhealthy” changes in our gut microbes are actually normal in a different setting, and might even be necessary for a healthy pregnancy.


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Malaria parasites evolve in vaccinated mice to cause more severe disease

Curing disease is really a matter of outfoxing evolution. When we assault bacteria or viruses or cancer cells with drugs, they evolve ways of resisting those drugs. We attack, they counter-attack. Take malaria: the Plasmodium parasites that cause the disease have repeatedly evolved to resist our best anti-malarial drugs. The mosquitoes that carry the parasites have evolved to resist the insecticides we poison them with. And now, Victoria Barclay from Pennsylvania State University has found that some malaria vaccines could drive Plasmodium to become even deadlier than it is now.

Several malaria vaccines are in development, but none have been licensed yet. Barclay vaccinated mice with a protein that’s found in several of these vaccines, and then exposed them to Plasmodium. After a few generations, the parasite became more ‘virulent’ – that is, it caused more severe disease. And it did so via an evolutionary escape route that is rarely considered.


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Cancer drug shocks HIV out of hiding

HIV is an exceptional adversary. It is more diverse than any other virus, and it attacks the very immune cells that are meant to destroy it. If that wasn’t bad enough, it also has a stealth mode. The virus can smuggle its genes into those of long-lived white blood cells, and lie dormant for years. This “latent” form doesn’t cause disease, but it’s also invisible to the immune system and to anti-HIV drugs. This viral reservoir turns HIV infection into a life sentence.

When the virus awakens, it can trigger new bouts of infection – a risk that forces HIV patients to stay on treatments for life. It’s clear that if we’re going to cure HIV for good, we need some way of rousing these dormant viruses from their rest and eliminating them.

A team of US scientists led by David Margolis has found that vorinostat – a drug used to treat lymphoma – can do exactly that. It shocks HIV out of hiding. While other chemicals have disrupted dormant HIV within cells in a dish, this is the first time that any substance has done the same thing in actual people.

At this stage, Margolis’s study just proves the concept – it shows that disrupting HIV’s dormancy is possible, but not what happens afterwards. The idea is that the awakened viruses would either kill the cell, or alert the immune system to do the job. Drugs could then stop the fresh viruses from infecting healthy cells. If all the hidden viruses could be activated, it should be possible to completely drain the reservoir. For now, that’s still a very big if, but Margolis’s study is a step in the right direction.

HIV enters its dormant state by convincing our cells to hide its genes. It recruits an enzyme called histone deacetylase (HDAC), which ensures that its genes are tightly wrapped and cannot be activated. Vorinostat, however, is an HDAC inhibitor – it stops the enzyme from doing its job, and opens up the genes that it hides.

It had already proven its worth against HIV in the lab. Back in 2009, three groups of scientists (including Margolis’ team) showed that vorinostat could shock HIV out of cultured cells, producing detectable levels of viruses when they weren’t any before.

To see if the drug could do the same for patients, the team extracted white blood cells from 16 people with HIV, purified the “resting CD4 T-cells” that the virus hides in, and exposed them to vorinostat. Eleven of the patients showed higher levels of HIV RNA (the DNA-like molecule that encodes HIV’s genes) – a sign that the virus had woken up.

Eight of these patients agreed to take part in the next phase. Margolis gave them a low 200 milligram dose of vorinostat to check that they could tolerate it, followed by a higher 400 milligram dose a few weeks later. Within just six hours, he found that the level of viral RNA in their T-cells had gone up by almost 5 times.

These results are enough to raise a smile, if not an outright cheer. We still don’t know how extensively vorinostat can smoke HIV out of hiding, or what happens to the infected cells once this happens. At the doses used in the study, the amount of RNA might have gone up, but the number of actual viral particles in the patients’ blood did not. It’s unlikely that the drug made much of a dent on the reservoir of hidden viruses, so what dose should we use, and over what time?

Vorinostat’s actions were also very varied. It did nothing for 5 of the original 16 patients. For the 8 who actually got the drug, some produced 10 times as much viral RNA, while others had just 1.5 times more. And as you might expect, vorinostat comes with a host of side effects, and there are concerns that it could damage DNA. This study could be a jumping point for creating safer versions of the drug that are specifically designed to awaken latent HIV, but even then, you would still be trying to use potentially toxic drugs to cure a long-term disease that isn’t currently showing its face. The ethics of doing that aren’t clear.

Steven Deeks, an AIDS researcher from the University of California San Francisco, talks about these problems and more in an editorial that accompanies the new paper. But he also says that the importance of the study “cannot be over­stated, as it provides a rationale for an entirely new approach to the management of HIV infection”.

Reference: Archin, Liberty, Kashuba, Choudhary, Kuruc, Crooks, Parker, Anderson, Kearney, Strain, Richman, Hudgens, Bosch, Coffin, Eron, Hazudas & Margolis. 2012. Administration of vorinostat disrupts HIV-1 latency in patients on antiretroviral therapy. Nature http://dx.doi.org/10.1038/nature11286

Image by Dr. A. Harrison; Dr. P. Feorino

More on HIV:

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Engineering mosquito gut bacteria to fight malaria

A malarial mosquito is a flying factory for Plasmodium – a parasite that fills its guts, and storms the blood of every person it bites. By hosting and spreading these parasites, mosquitoes kill 1.2 million people every year.

But Plasmodium isn’t the only thing living inside a mosquito’s guts. Just as our bowels are home to trillions of bacteria, mosquitoes also carry their own microscopic menageries. Now, Sibao Wang from Johns Hopkins Bloomberg School of Public Health has transformed one of these bacterial associates into the latest recruit in our war against malaria. By loading it with genes that destroy malarial parasites, Wang has turned the friend of our enemy into our friend.

Many groups of scientists have tried to beat malaria by genetically modifying the species of mosquito that carries it – Anopheles gambiae. Marcelo Jacobs-Lorena, who led Wang’s new study, has been at the forefront of these efforts. In 2002, his team loaded mosquitoes with a modified gene so that their guts produce a substance that kills off Plasmodium.


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Urban noise can turn sparrow females into bad mums

When Rachel Carson wrote her famous book Silent Spring, she envisioned a world in which chemical pollutants killed off wildlife, to the extent that singing birds could no longer be heard. Pesticides aside, we now know that humans have challenged birds with another type of pollution, which also threatens to silence their beautiful songs – noise.

A man-made world is a loud one. Between the din of cities and the commotion of traffic, we flood our surroundings with a chronic barrage of sound. This is bad news for songbirds. We know that human noise is a problem for them because some species go to great lengths to make themselves heard, from changing their pitch (great tits) to singing at odd hours (robins) to just belting their notes out (nightingales). We also know that some birds produce fewer chicks in areas affected by traffic noise.

Now, Julia Schroeder from the University of Sheffield has found one reason for this. She has shown that loud noises mask the communication between house sparrow mothers and their chicks, including the calls that the youngsters use to beg for food. Surrounded by sound, the chicks eat poorly. “City noise has the potential to turn sparrow females into bad mothers,” says Schroeder.


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Silk cages preserve vaccines and antibiotics for months without refrigeration

Here is an unfortunate clash of circumstance. Vaccines and antibiotics become useless in heat, but the countries where they are most needed – poor ones where infectious diseases are a major cause of death – are really hot. Because of this, millions of dollars are spent on keeping vaccines cold and millions of lives are affected when they can’t be.

The factory that makes a vaccine can be continents away from the arm of the child who will receive it. Those distant points are separated by the “cold chain” – a network of refrigerators, freezers, insulated vehicles, cold boxes, specially equipped depots, and trained personnel. If the chain fails, and vaccines are allowed to heat up, they rapidly and permanently degrade. This happens even in developed countries, but it’s a huge problem for developing ones, where electricity and refrigeration can be sparse luxuries.

If there was a way of stabilising vaccines so they can withstand high temperatures, it could save millions of both lives and dollars. And Jeney Zhang, a graduate student from Tufts University, has developed one possible method: wrapping vaccines and antibiotics in molecular cages of silk.

Within these prisons, the MMR vaccine and two common antibiotics were still viable after months at high temperature. Matt Cottingham, a vaccine specialist from the University of Oxford, says, “The stability is amazing. No one’s even come close to that. It’s certainly better than anything else that’s currently being used.”

Silk is no stranger to medical applications. Spewed from the salivary glands of silkworm caterpillars, this natural fibre is strong, flexible and biodegradable. It has been used to make surgical sutures, medical implants, and replacement tissues. It can also be used to imprison small molecules. Individual silk molecules come together to form a structure with tightly organised regions, interspersed with looser “pockets”. In these pockets, molecules can be shielded from the elements.

Zhang, working in the lab of silk maestro David Kaplan, showed that silk can stabilise two antibiotics – penicillin and tetracycline – as well as the measles, mumps and rubella (MMR) vaccine.

Wrapped in silk, penicillin spent a month at 60 degrees Celsius with no loss of activity. Normally, it breaks down after a few weeks at room temperature (25C), or just a day at human body temperature (37C) – a month at 60 is unheard of. Tetracycline is even more delicate.  In silk, it lost 20 per cent of its activity after a month at 60C, and was unharmed at lower temperatures.

The MMR vaccine fared similarly well. The vaccine consists of weakened versions of the viruses behind the three diseases. They are shipped as a freeze-dried powder, which has to be dissolved in a special solvent before being injected.

If the powders are kept at 45C, they become completely useless within 20 weeks. If the viruses are wrapped in silk before being freeze-dried, they stay almost good as new, keeping at least 85 per cent of their original potency after 6 months, no matter the temperature. Put it another way: at 37C, it would normally take 9 weeks for the viruses to lose half their original potency, but it takes 94 weeks if they are encased in silk.

How does the silk protect its payload? It’s not clear. The silk may protect the viruses in the vaccines from enzymes that would otherwise destroy the proteins on their outer shells. Without those proteins, the immune system has no way of recognising what the virus looks like, or preparing itself for future infections.  The silk might also act as a physical barrier that constrains the viral proteins and stops them from deforming at warmer temperatures.  And it could keep water away from the vaccines.

There’s clearly still a lot of basic questions left to answer, not least, as Cottingham asks: “Would this be compatible with being injected into babies?” Kaplan expects so. “Silk has been used in medical devices, such as sutures, for decades and the FDA approved it for new medical products more recently,” he says. It’s a promising first step towards making the cold chain a little less brittle.

Reference: Zhang, Pritchard, Hu, Valentin, Panilatitis, Omenetto & Kaplan. 2012. Stabilization of vaccines and antibiotics in silk and eliminating the cold chain. PNAS http://dx.doi.org/10.1073/pnas.1206210109

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