Motors too small to see with the eye may soon have the power to drive innovations in chemistry, biology and computing. Three creators of such nanoscopic machines were honored October 5 with the Nobel Prize in chemistry.

Sharing the prize of 8 million Swedish kronor (about $930,000) equally are Jean-Pierre Sauvage, J. Fraser Stoddart and Bernard Feringa. “If you had to choose three people at the top of the field, that’s it. These are the men,” says James Tour, a na
Recognition of the burgeoning field of molecular motors will draw more money and inspire children to become scientists, says Donna Nelson, an organic chemist at the University of Oklahoma in Norman and the president of the American Chemical Society. “It will benefit not only these three chemists, it will benefit the entire field of chemistry.”
Chemists and physicists have envisioned molecular machines since at least the 1960s, but were never able to reliably produce complex structures. Then in 1983, Sauvage, of the University of Strasbourg in France, devised a method for making interlocking molecular rings, or catenanes. Sauvage’s molecular chain set the stage for the rest of the field (SN: 9/8/90, p. 149).

Stoddart, of Northwestern University in Evanston, Ill., improved the efficiency so that he could produce large quantities of molecular machines, starting in 1991 with rings clipped around a central axle. That structure is known as a rotaxane. He and colleagues learned to control the slide of the rings along the axle, making a simple molecular switch. Such switches could be used to create molecular computers or drug delivery systems. Stoddart showed in 2000 that it was possible to make molecular “muscles” using interlocking rings and axles. Stoddart and colleagues have since devised molecular elevators and pumps based on the same molecules.
Feringa, of the University of Groningen in the Netherlands, ramped things up another notch in 1999 by building the first molecular motor. Things move so differently at the molecular scale that many researchers weren’t sure anyone could precisely control the motion of molecular motors, says R. Dean Astumian of the University of Maine in Orono. Feringa’s innovation was to devise asymmetric molecules that would spin in one direction when hit with a pulse of light.

Up to 50,000 of the motors could span the width of a human hair, says Tour. Alone, one of the spinning motors doesn’t pack much punch (SN: 2/7/04, p. 94), but harnessed together in large numbers the little motors can do big work, he says. Groups of the whirring motors powered by light can rotate a glass rod thousands of times their size and do other work on a macroscopic scale. Feringa also harnessed his motors into a four-wheel-drive “nanocar” (SN: 12/17/11, p. 8).

The process of making molecular machines has improved drastically over recent decades, thanks in large part to the work of the three newly christened laureates, says Rigoberto Advincula, a chemist at Case Western Reserve University in Cleveland. Scientists have a better understanding of how to construct molecules that more reliably bend, loop and connect to form shapes. “You don’t have tweezers to put them together,” he says. “You template the reaction so that the thread to goes through the ring. That then makes it easier for the two thread ends to meet each other.” New techniques have also allowed the production of more intricate shapes. Further development will bring these processes to even bigger scales, allowing for the design of molecular machines for everything from energy harvesting to building protein complexes, Advincula says.
Such applications are still on the horizon and no one really knows what sorts of machines chemists can make from molecules yet. When people question Feringa about what his molecular motors can be used for, he “feels a bit like the Wright brothers” when people asked them after their first flight why they needed a flying machine, he said during a telephone call during the announcement of the prize. There are “endless opportunities,” including nanomachines that can seek and destroy tumor cells or deliver drugs to just the cells that need them, Feringa speculated.

Stoddart, who was born in Edinburgh and moved to the United States in 1997, applauded the Nobel committee for recognizing “a piece of chemistry that is extremely fundamental in its making and being.” Sauvage, in particular, created a new type of molecular bond in order to forge his chain, Stoddart said during a news conference. “New chemical compounds are probably several thousand a day worldwide,” he said. “New chemical reactions, well, maybe a dozen or two a month. Maybe I go over the top there. But new bonds, they are few and far between. They are really the blue moons. So I think that’s what’s being recognized, more than anything.”

Two trillion galaxies. That’s the latest estimate for the number of galaxies that live — or have lived — in the observable universe, researchers report online October 10 at arXiv.org. This updated headcount is roughly 10 times greater than previous estimates and suggests that there are a lot more galaxies out there for future telescopes to explore.

Hordes of relatively tiny galaxies, weighing as little as 1 million suns, are responsible for most of this tweak to the cosmic census. Astronomers haven’t directly seen these galaxies yet. Christopher Conselice, an astrophysicist at the University of Nottingham in England, and colleagues combined data from many ground- and space-based telescopes to look at how the number of galaxies in a typical volume of the universe has changed over much of cosmic history. They then calculated how many galaxies have come and gone in the universe.

The galactic population has dwindled over time, as most of those 2 trillion galaxies collided and merged to build larger galaxies such as the Milky Way, the researchers suggest. That’s in line with prevailing ideas about how massive galaxies have been assembled. Seeing many of these remote runts, however, is beyond the ability of even the next generation of telescopes. “We will have to wait at least several decades before even the majority of galaxies have basic imaging,” the researchers write.

Crucial immune system proteins that make it harder for viruses to replicate might also help the attackers avoid detection, three new studies suggest. When faced with certain viruses, the proteins can set off a cascade of cell-to-cell messages that destroy antibody-producing immune cells. With those virus-fighting cells depleted, it’s easier for the invader to persist inside the host’s body.

The finding begins to explain a longstanding conundrum: how certain chronic viral infections can dodge the immune system’s antibody response, says David Brooks, an immunologist at the University of Toronto not involved in the research. The new studies, all published October 21 in Science Immunology, pin the blame on the same set of proteins: type 1 interferons.
Normally, type 1 interferons protect the body from viral siege. They snap into action when a virus infects cells, helping to activate other parts of the immune system. And they make cells less hospitable to viruses so that the foreign invaders can’t replicate as easily.

But in three separate studies, scientists tracked mice’s immune response when infected with lymphocytic choriomeningitis virus, or LCMV. In each case, type 1 interferon proteins masterminded the loss of B cells, which produce antibodies specific to the virus that is being fought. Normally, those antibodies latch on to the target virus, flagging it for destruction by other immune cells called T cells. With fewer B cells, the virus can evade capture for longer.

The proteins’ response “is driving the immune system to do something bad to itself,” says Dorian McGavern, an immunologist at the National Institute of Neurological Disorders and Stroke in Bethesda, Md., who led one of the studies.

The interferon proteins didn’t directly destroy the B cells; they worked through middlemen instead. These intermediaries differed depending on factors including the site of infection and how much of the virus the mice received.
T cells were one intermediary. McGavern and his colleagues filmed T cells actively destroying their B cell compatriots under the direction of the interferon proteins. When the scientists deleted those T cells, the B cells didn’t die off even though the interferons were still hanging around.
Another study found that the interferons were sending messages not just through T cells, but via a cadre of other immune cells, too. Those messages told B cells to morph into cells that rapidly produce antibodies for the virus. But those cells die off within a few days instead of mounting a longer-term defense.

That strategy could be helpful for a short-term infection, but less successful against a chronic one, says Daniel Pinschewer, a virologist at the University of Basel in Switzerland who led that study. Throwing the entire defense arsenal at the virus all at once leaves the immune system shorthanded later on.

But interferon activity could prolong even short-term viral infections, a third study showed. There, scientists injected lower doses of LCMV into mice’s footpads and used high-powered microscopes to watch the infection play out in the lymph nodes. In this case, the interferon stifled B cells by working through inflammatory monocytes, white blood cells that rush to infection sites.

“The net effect is beneficial for the virus,” says Matteo Iannacone, an immunologist at San Raffaele Scientific Institute in Milan who led the third study. Sticking around even a few days longer gives the virus more time to spread to new hosts.

Since all three studies looked at the same virus, it’s not yet clear whether the mechanism extends to other viral infections. That’s a target for future research, Iannacone says. But Brooks thinks it’s likely that other viruses that dampen antibody response (like HIV and hepatitis C) could also be exploiting type 1 interferons.

Joining a gang doesn’t necessarily make a protein a killer, a new study suggests. This clumping gets dangerous only under certain circumstances.

A normally innocuous protein can be engineered to clump into fibers similar to those formed by proteins involved in Alzheimer’s, Parkinson’s and brain-wasting prion diseases such as Creutzfeldt-Jakob disease, researchers report in the Nov. 11 Science. Cells that rely on the protein’s normal function for survival die when the proteins glom together. But cells that don’t need the protein are unharmed by the gang activity, the researchers discovered. The finding may shed light on why clumping proteins that lead to degenerative brain diseases kill some cells, but leave others untouched.
Clumpy proteins known as prions or amyloids have been implicated in many nerve-cell-killing diseases (SN: 8/16/08, p. 20). Such proteins are twisted forms of normal proteins that can make other normal copies of the protein go rogue, too. The contorted proteins band together, killing brain cells and forming large clusters or plaques.

Scientists don’t fully understand why these mobs resort to violence or how they kill cells. Part of the difficulty in reconstructing the cells’ murder is that researchers aren’t sure what jobs, if any, many of the proteins normally perform (SN: 2/13/10, p. 17).

A team led by biophysicists Frederic Rousseau and Joost Schymkowitz of Catholic University Leuven in Belgium came up with a new way to dissect the problem. They started with a protein for which they already knew the function and engineered it to clump. That protein, vascular endothelial growth factor receptor 2, or VEGFR2, is involved in blood vessel growth. Rousseau and colleagues clipped off a portion of the protein that causes it to cluster with other proteins, creating an artificial amyloid.

Masses of the protein fragment, nicknamed vascin, could aggregate with and block the normal activity of VEGFR2, the researchers found. When the researchers added vascin to human umbilical vein cells grown in a lab dish, the cells died because VEGFR2 could no longer transmit hormone signals the cells need to survive. But human embryonic kidney cells and human bone cancer cells remained healthy. Those results suggest that some forms of clumpy proteins may not be generically toxic to cells, says biophysicist Priyanka Narayan of the Whitehead Institute for Biomedical Research in Cambridge, Mass. Instead, rogue clumpy proteins may target specific proteins and kill only cells that rely on those proteins for survival.

Those findings may also indicate that prion and amyloid proteins, such as Alzheimer’s nerve-killing amyloid-beta, normally play important roles in some brain cells. Those cells would be the ones vulnerable to attack from the clumpy proteins.
The newly engineered ready-to-rumble protein may open new ways to inactivate specific proteins in order to fight cancer and other diseases, says Salvador Ventura, a biophysicist at the Autonomous University of Barcelona. For instance, synthetic amyloids of overactive cancer proteins could gang up and shut down the problem protein, killing the tumor.

Artificial amyloids might also be used to screen potential drugs for anticlumping activity that could be used to combat brain-degenerating diseases, Rousseau suggests.

The stories of dinosaurs’ lives may be written in fossilized pigments, but scientists are still wrangling over how to read them.

In September, paleontologists deduced a dinosaur’s habitat from remnants of melanosomes, pigment structures in the skin. Psittacosaurus, a speckled dinosaur about the size of a golden retriever, had a camouflaging pattern that may have helped it hide in forests, Jakob Vinther and colleagues say.
The dinosaur “was very much on the bottom of the food chain,” says Vinther, of the University of Bristol in England. “It needed to be inconspicuous.”
Identifying ancient pigments can open up a wide new world of dinosaur biology and answer all sorts of lifestyle questions, says zoologist Hannah Rowland of the University of Cambridge. “You might be able to take a fossil … and infer a dinosaur’s life history just from its pigment patterns,” she says. “That’s the most exciting thing.”

Not so fast, says paleontologist Mary Schweitzer of North Carolina State University in Raleigh. Evidence for ancient pigments can be ambiguous. In some cases, microscopic structures that appear to be melanosomes may actually be microbes, she says. “Both hypotheses remain viable until one is shot down with data.” Until then, she says, inferring dinosaur lifestyles from alleged ancient pigments is impossible.

Vinther’s work, published in the Sept. 26 Current Biology, is the latest in a long-simmering debate in the field of paleo color, the study of fossil pigments and what they can reveal about ancient animals. Disputes over his team’s findings and what’s needed to clearly identify fossilized melanosomes point to current pitfalls of the field.

But the promise is clear: Paleo color could paint a vivid picture of a dinosaur’s life, offering clues about behavior, habitat and evolution.

“This is a crucial new piece in the puzzle of how the past looked,” Vinther says.
Color me dino
Psittacosaurus (model shown) was a parrot-beaked herbivore about the size of a large dog. Researchers found signs of pigmentation (black specks) on its tail region, back leg and elsewhere that hint at its habitat.

Tap the image below to see signs of pigmentation from Psittacosaurus fossils.
A field emerges
Scientists have been puzzling over animals of the past for centuries, but eight years ago, paleontology got a wake-up call. That’s when Vinther and colleagues proposed that microscopic structures in a roughly 125-million-year-old fossil feather were actually a type of melanosome (SN: 8/2/08, p. 10). These pigment pouches rest inside pigment cells and, in this particular fossil feather, might have delivered a blackish hue, like a blackbird’s.

Scientists had noticed similar structures inside fossilized skin and feathers since the early 1980s. But people assumed that these structures were remnants of bacteria — perhaps decomposers that feasted on the dead animals, says paleontologist Martin Sander of the University of Bonn in Germany.

The new, colorful interpretation sparked a flurry of research, and scientists have since spotted what appear to be melanosomes in all kinds of fossilized animals. Paleontology, in fact, is now awash in colors and patterns. Pigment pods may have painted reddish-brown speckles on the face of a Late Jurassic theropod, brushed chestnut stripes on a long-tailed dino from China and made the plumage of a four-winged dinosaur called Microraptor iridescent. That shimmery dinosaur “probably had a weak, glossy iridescence all over its body,” says evolutionary biologist Matthew Shawkey of Ghent University in Belgium. His team deduced Microraptor’s color from the shape of its melanosomes.
Modern melanosomes generally carry a mixture of two melanin pigments: dark brown-black eumelanin and red-yellow pheomelanin. Scientists have linked color in mammals and birds to melanosome shape — a meatball shape for reddish brown hues, for example, and a sausage shape for darker colors.

In iridescent feathers, melanosomes tend to be even thinner, Shawkey says. Microraptor’s melanosomes looked like skinny sausages — similar to those seen in the feathers of modern crows and ravens, says Shawkey, who reported the findings with Vinther and colleagues in Science in 2012 (SN Online: 3/9/12).

Three years later, Vinther laid out the case for inferring color — and ancient histories — from fossilized pigments in a review in Bioessays. Not only can the distinctive shapes of melanosomes offer clues, he noted, but chemical tests can help detect the presence of melanin itself. Finding this pigment in fossils, he argued, puts the old bacteria hypothesis to rest.

Schweitzer and colleagues disagreed with Vinther’s take in a review published in Bioessays later in 2015. Researchers need to be cautious when deducing the hues of extinct animals, the scientists wrote. Any melanosome look-alikes in fossilized feathers or skin could actually be microbes.
After all, microbes are everywhere. “These animals died in an environment that was not sterile and free from microbes,” Schweitzer says. “Think about it. If you take a piece of chicken and throw it out in your backyard, how long does it take for microbes to overgrow that chicken?”

The tiny organisms are hardy, too. Both microbes and the sticky biofilms they form are preserved in the fossil record. And, Schweitzer says, microbes and melanosomes overlap completely in shape and size, which makes the two tough to tell apart. What’s more, some microbes actually make melanin themselves; detecting the pigment in a fossil is not a rock-solid sign that the ancient animal was black, brown or freckled.

It’s not that Schweitzer or Bioessays coauthor Johan Lindgren, a geologist at Lund University in Sweden, doubt that melanosomes can leave traces in the fossil record. The issue, Lindgren says, is that not all round structures you find are melanosomes.

Chemical tests could help distinguish the two. Bacteria, for example, leave behind traces that can be identified with pyrolysis gas chromatography-mass spectrometry. But that requires samples to be vaporized. “It can mean destroying much of what you are trying to study,” says geochemist Roy Wogelius of the University of Manchester in England. “So it’s not always possible.”

Vinther’s new work isn’t likely to settle the debate. In fact, people were arguing both sides in October at a meeting of the Society of Vertebrate Paleontology in Salt Lake City.

Arindam Roy, a Bristol colleague of Vinther’s, reported size differences between fossilized melanosomes and bacteria growing on decaying chicken feathers in the lab. Alison Moyer, an N.C. State colleague of Schweitzer’s, said that looks weren’t enough. Finding keratin, a protein that typically surrounds melanosomes, could serve as evidence for pigments in fossils.

From color to camouflage
The fossil described in Vinther’s new paper is “spectacular,” Schweitzer says. “It’s got skin all over the place. I can’t think of too many dinosaur specimens that are preserved like this.”

The dinosaur lies on its back, flattened in a slab of volcanic rock. Skin covers a completely intact skeleton, and dozens of long bristles poke from the tail. Psittacosaurus, an herbivore that lived some 120 million years ago, walked on two legs and would have reached about half a meter in height.
“It would have been a supercute animal,” Vinther says. “It’s got this wide face and looks a little bit like E.T.”

Black material speckles the dinosaur’s body, tail and face. Vinther believes the material is the ancient remains of pigment. His team examined samples chipped from the fossil and saw what he considers the telltale orbs of melanosomes — mostly impressions in the rock but also some microbodies, the 3-D structures themselves.

Based on the dinosaur’s pigment patterns, it would have had a dark back that faded to a lighter belly. That type of coloring, called countershading, shows up in animals from penguins to fish and may act as a form of camouflage. It lightens parts of the body typically in shadow, and darkens parts typically exposed to light. “If you want to hide, it makes sense to try and obliterate those shadows,” Rowland says.

Their prediction for diffuse light matched the model painted like Psittacosaurus. “It’s like what we see in forest-living animals,” Vinther says. “This thing was camouflaged.”
Lingering doubts
Going from fossil to forest may be more of a leap than a step, other scientists suggest.

Psittacosaurus’ skin very well may contain ancient pigments, Wogelius says. “I don’t think it’s a crazy idea.” But, he adds, of Vinther’s group: “I don’t think they’ve proved what they claim.”

Vinther’s team, for exampl e, used just four tiny fossil samples to extrapolate the coloring of the whole dinosaur. “I think it’s a bit of an overreach,” Wogelius says.

Schweitzer also notes that the specimen was varnished, presumably to protect the bones and soft tissues. It happened before Vinther and colleagues got their hands on the dinosaur and makes it impossible to perform the chemical tests that would bolster the claim for pigments. “Varnish is horribly destructive to fossils,” she says. “It totally ruins the specimen for other types of analysis.”

Vinther argues that his team has chemically analyzed other fossils and found evidence of melanin — not bacteria. The microbodies in those fossils look just like the ones in Psittacosaurus, he says.

Vinther’s team also saw evidence of just one kind of microbody, and it had a distinct round shape. If the structures were actually bacteria, he says, you’d expect to see a whole range of shapes and sizes. “Some of them would be shaped like corkscrews, some would have flagella, some would be humongous, some would be tiny.”

That’s the tricky part with bacteria, counters Lindgren. “In some cases you can have a huge consortium, but in other cases you can have one single type.”
Vinther’s interpretation has its supporters. “I was skeptical at first,” Sander says, “but now there’s been such an array of these little bodies that it’s pretty clear that at least some of them are not bacteria.” Despite some continuing controversy, Sander says many paleontologists now accept that micro­structures in fossils may be melanosomes.

Additional research, though, “would help the entire community,” he says, “so that there are no longer any lingering doubts.”

Along with chemical tests, Schweitzer suggests, researchers could try transmission electron microscopy, a technique that blasts an electron beam through a thinly sliced sample. With TEM, melanosomes appear as black blobs. Bacteria tend to look different — in some cases, more like fried eggs.

Shawkey, for one, is looking to chemistry. In a paper published online November 14 in Palaeontology, his team used a technique called Raman spectroscopy to help build a case for feather color in a bird that died some 120 million years ago. In the feathers, the researchers spotted the skinny sausages of iridescent melanosomes and chemical signs of the pigment eumelanin. Shawkey thinks the chemical evidence could help “head off any criticism that we might encounter.”

Working through the field’s snags, paleontologists might come together to fill in the hues and tints, and potentially the habits and habitats, of ancient animals that until recently had been known primarily by their bones.

Atom blast for gas

A pair of simultaneous nuclear explosions, one more than 1.6 miles underground and the other 1,000 feet above it, have been proposed as a way to extract huge quantities of natural gas from subterranean rock. Each blast would be … about 2.5 times the size of the bomb used at Hiroshima. By breaking up tight gas-bearing rock formations, a flow of presently inaccessible gas may be made available.… A single-blast experiment, called Project Gasbuggy, is already planned. — Science News, December 17, 1966
Update
On December 10, 1967, Project Gasbuggy went ahead, with a 29-kiloton nuclear explosion deep underground in northwestern New Mexico. The blast released natural gas, but the gas was radio­active. The area is still regularly monitored for radioactive contamination. Today, natural gas trapped below Earth’s surface is often extracted via fracking, which breaks up rock using pressurized fluid (SN: 9/8/12, p. 20). Though less extreme, potential links to drinking water contamination and earthquakes have stoked fears about the technique.

With virtual reality finally hitting the consumer market this year, VR headsets are bound to make their way onto a lot of holiday shopping lists. But new research suggests these gifts could also give some of their recipients motion sickness — especially if they’re women.

In a test of people playing one virtual reality game using an Oculus Rift headset, more than half felt sick within 15 minutes, a team of scientists at the University of Minnesota in Minneapolis reports online December 3 in Experimental Brain Research. Among women, nearly four out of five felt sick.
So-called VR sickness, also known as simulator sickness or cybersickness, has been recognized since the 1980s, when the U.S. military noticed that flight simulators were nauseating its pilots. In recent years, anecdotal reports began trickling in about the new generation of head-mounted virtual reality displays making people sick. Now, with VR making its way into people’s homes, there’s a steady stream of claims of VR sickness.

“It’s a high rate of people that you put in [VR headsets] that are going to experience some level of symptoms,” says Eric Muth, an experimental psychologist at Clemson University in South Carolina with expertise in motion sickness. “It’s going to mute the ‘Wheee!’ factor.”

Oculus, which Facebook bought for $2 billion in 2014, released its Rift headset in March. The company declined to comment on the new research but says it has made progress in making the virtual reality experience comfortable for most people, and that developers are getting better at creating VR content. All approved games and apps get a comfort rating based on things like the type of movements involved, and Oculus recommends starting slow and taking breaks. But still some users report getting sick.

The new study confirms these reports. A team led by Thomas Stoffregen, a kinesiologist who has been studying motion sickness for decades, tested the susceptibility of two sets of 18 male and 18 female undergraduates during two different VR games using an Oculus Rift DK2 headset. The first game, which involved using head motions to roll a virtual marble through a maze, made 22 percent of the players feel sick within the 15 minutes they were asked to play.

Another 36 students played the horror game Affected, using a hand-held controller to navigate a creepy building. This time, 56 percent felt sick within 15 minutes. Fourteen of 18 women, nearly 78 percent, were affected, compared with just over 33 percent of men. Though the study tested only an Oculus Rift, other companies’ VR headsets based on similar technology may have similar issues.
This gender difference shows up in almost any situation that can cause motion sickness, like a moving car or a rocking boat. But Stoffregen says the disparity can’t be explained by the most widely accepted theory of motion sickness, which suggests that it’s caused by a mismatch between the motion your body is sensing and what your eyes are seeing, like when you read in a moving car. With VR, the theory goes, your eyes think you’re moving, but your body feels stationary, and this makes you feel sick.

Stoffregen thinks motion sickness is instead caused by things that disrupt your balance, like a boat pitching over a wave. And if you try to stabilize your body in the virtual world you see — say, by leaning into a virtual turn — instead of in the physical world you’re in, you can lose stability.

Men and women are typically different shapes and sizes, so they differ in the subtle, subconscious movements that keep their bodies balanced, known as postural sway, Stoffregen says. This difference makes women more susceptible to motion sickness, he claims. For the new study, he measured participants’ balancing motions before they played the games and found a measurable difference in sway between those who reported feeling sick and those who didn’t.

Because motion sickness is a complicated set of symptoms, self-reporting by participants may not be a reliable way to measure it, Muth argues. And, he says, “I would say the science isn’t there yet to draw that conclusion” about gender bias, adding he’d like to see the result replicated with a larger group.

Even so, with VR potentially poised to jump from the gaming world into more mainstream aspects of society — Facebook CEO Mark Zuckerberg says he wants “a billion people on Facebook in virtual reality as soon as possible” — a gender disparity could become a real problem, especially if VR enters the workplace, Stoffregen says. “If it were only games, it wouldn’t matter, and nobody would care.”

It was barely more than half a century ago that the Nobel Prize–winning virologist Sir Frank Macfarlane Burnet mused about the demise of contagions. “To write about infectious disease,” he wrote in 1962, “is almost to write of something that has passed into history.”

If only. In the past several decades, over 300 infectious pathogens have either newly emerged or emerged in new places, causing a steady drumbeat of outbreaks and global pandemic scares.

Over the course of 2016, their exploits reached a crescendo. Just as the unprecedented outbreak of Ebola in West Africa was collapsing in early 2016, the World Health Organization declared Zika virus, newly erupted in the Americas, an international public health emergency. What would balloon into the largest outbreak of yellow fever in Angola in 30 years had just begun. A few months later, scientists reported the just-discovered “superbug” mcr-1 gene in microbes collected from humans and pigs in the United States (SN Online: 5/27/16). The gene allows bacteria to resist the last-ditch antibiotic colistin, bringing us one step closer to a looming era of untreatable infections that would transform the practice of medicine. Its arrival presaged yet another unprecedented event: the convening of the United Nations General Assembly to consider the global problem of antibiotic-resistant bugs. It was only the fourth time over its 70-plus-year history that the assembly had been compelled to consider a health challenge. It’s “huge,” says University of Toronto epidemiologist David Fisman.
But even as UN delegates arrived for their meeting in New York City in September, another dreaded infection was making headlines again. The international community’s decades-long effort to end the transmission of polio had unraveled. In 2015, the WHO had declared Nigeria, one of the three last countries in the world that suffered the infection, free of wild polio. By August 2016, it was back. Millions would have to be vaccinated to keep the infection from establishing a foothold.
Three fundamental, interrelated factors fuel the microbial comeback, experts say. Across the globe, people are abandoning the countryside for life in the city, leading to rapid, unplanned urban expansions. In crowded conditions with limited access to health care and poor sanitation, pathogens like Ebola, Zika and influenza enjoy lush opportunities to spread. With more infections mingling, there are also more opportunities for pathogens to share their virulence genes.

At the same time, global demand for meat has quadrupled over the last five decades by some estimates, driving the spread of industrial livestock farming techniques that can allow benign microbes to become more virulent. The use of colistin in livestock agriculture in China, for example, has been associated with the emergence of mcr-1, which was first discovered during routine surveillance of food animals there. Genetic analyses suggest that siting factory farms full of chickens and pigs in proximity to wild waterfowl has played a role in the emergence of highly virulent strains of avian influenza. Crosses of Asian and North American strains of avian influenza caused the biggest outbreak of animal disease in U.S. history in 2014–2015. Containing that virus required the slaughter of nearly 50 million domesticated birds and cost over $950 million. Worryingly, some strains of avian influenza, such as H5N1, can infect humans.
The thickening blanket of carbon dioxide in the atmosphere resulting from booming populations of people and livestock provides yet another opportunity for pathogens to exploit. Scientists around the world have documented the movement of disease-carrying creatures including mosquitoes and ticks into new regions in association with newly amenable climatic conditions. Climate scientists predict range changes for bats and other animals as well. As the organisms spread into new ranges, they carry pathogens such as Ebola, Zika and Borrelia burgdorferi(a bacterium responsible for Lyme disease) along with them.
Since we can rarely develop drugs and vaccines fast enough to stanch the most dangerous waves of disease, early detection will be key moving forward. Researchers have developed a welter of models and pilot programs showing how environmental cues such as temperature and precipitation fluctuations and the insights of wildlife and livestock experts can help pinpoint pathogens with pandemic potential before they cause outbreaks in people. Chlorophyll signatures, a proxy for the plankton concentrations that are associated with cholera bacteria, can be detected from satellite data, potentially providing advance notice of cholera outbreaks.

Even social media chatter can be helpful. Innovative financing methods, such as the World Bank’s recently launched Pandemic Emergency Financing Facility — a kind of global pandemic insurance policy funded by donor countries, the reinsurance market and the World Bank — could help ensure that resources to isolate and contain new pathogens are readily available, wherever they take hold. Right now, emerging disease expert Peter Daszak points out, “we wait for epidemics to emerge and then spend billions on developing vaccines and drugs.” The nonprofit organization that Daszak directs, EcoHealth Alliance, is one of a handful that instead aim to detect new pathogens at their source and proactively minimize the risk of their spread.

Burnet died in 1985, two years after the discovery of HIV, one of the first of the latest wave of new pathogens. His vision of a contagion-free society was that of a climber atop a foothill surrounded by peaks, mistakenly thinking he’d reached the summit. The challenge of surviving in a world of pathogens is far from over. In many ways, it’s only just begun.

SAN FRANCISCO — One climate doomsday scenario can be downgraded, new research suggests.

Decades of atmospheric measurements from a site in northern Alaska show that rapidly rising temperatures there have not significantly increased methane emissions from the neighboring permafrost-covered landscape, researchers reported December 15 at the American Geophysical Union’s fall meeting.

Some scientists feared that Arctic warming would unleash large amounts of methane, a potent greenhouse gas, into the atmosphere, worsening global warming. “The ticking time bomb of methane has clearly not manifested itself yet,” said study coauthor Colm Sweeney, an atmospheric scientist at the University of Colorado Boulder. Emissions of carbon dioxide — a less potent greenhouse gas — did increase over that period, the researchers found.
The CO2 rise “is still bad, it’s just not as bad” as a rise in methane, said Franz Meyer, a remote sensing scientist at the University of Alaska Fairbanks who was not involved in the research. The measurements were taken at just one site, though, so Meyer cautions against applying the results to the entire Arctic just yet. “This location might not be representative,” he said.

Across the Arctic, the top three meters of permafrost contain 2.5 times as much carbon as the CO2 released into the atmosphere by human activities since the start of the Industrial Revolution. As the Arctic rapidly warms, these thick layers of frozen soil will thaw and some of the carbon will be converted by hungry microbes into methane and CO2, studies that artificially warmed permafrost have suggested. That carbon will have a bigger impact on Earth’s climate as methane than it will as CO2. Over a 100-year period, a ton of methane will cause about 25 times as much warming as a ton of CO2.

A research station in Alaska’s northernmost city, Barrow, has been monitoring methane concentrations in the Arctic air since 1986 and CO2 since 1973. An air intake on a tower about 16.5 meters off the ground constantly sniffs the air, taking measurements. Barrow has warmed more than twice as fast as the rest of the Arctic over the last 29 years. This rapid warming “makes this region of the Arctic a great little incubation test to see what happens when we have everything heating up much faster,” Sweeney said.

Over the course of a year, methane concentrations in winds wafting from the nearby tundra rise and fall with temperatures, the Barrow data show. Since 1986, though, seasonal methane emissions have remained largely stable overall. But concentrations of CO2 in air coming from over the tundra, compared with over the nearby Arctic Ocean, have increased by about 0.02 parts per million per year since 1973, the researchers reported.

The lack of an increase in methane concentrations could be caused by the thawing permafrost allowing water to escape and drying the Arctic soil, Sweeney proposed. This drying would limit the productivity of methane-producing microbes, potentially counteracting the effects of warming.
Tracking Arctic wetness will be crucial for predicting future methane emissions in the region, said Susan Natali, an Arctic scientist at the Woods Hole Research Center in Falmouth, Mass. Studies have shown increased methane emissions from growing Arctic lakes, she points out. “We’re going to get both carbon dioxide and methane,” she said. “It depends on whether areas are getting wetter or drier.”

NEW ORLEANS, La. – Skin that mostly hangs loose around hagfishes proves handy for living through a shark attack or wriggling through a crevice.

The skin on hagfishes’ long, sausage-style bodies is attached in a line down the center of their backs and in flexible connections where glands release slime, explained Douglas Fudge of Chapman University in Orange, Calif. This floating skin easily slip-slides in various directions. A shark tooth can puncture the skin but not stab into the muscle below. And a shark attack is just one of the crises when loose skin can help, Fudge reported January 5 at the annual meeting of the Society for Integrative and Comparative Biology.
Hagfishes can fend off an attacking shark by quick-releasing a cloud of slime. Yet video of such events shows that a shark can land a bite before getting slimed. To figure out how hagfishes might survive such wounds, Fudge and colleagues used an indoor guillotine to drop a large mako shark tooth into hagfish carcasses. With the skin in its naturally loose state, the tooth readily punched through skin but slipped away from stabbing into the body of either the Atlantic (Myxine glutinosa) or Pacific (Eptatretus stoutii) hagfish species.
But when the researchers glued the skin firmly to the hagfish muscle so the skin couldn’t slip, the tooth typically plunged into inner tissue. For comparison, the researchers tested lampreys, which are similarly tube-shaped but with skin well-fastened to their innards. When the guillotine dropped on them, the tooth often stabbed directly into flesh.
The finding makes sense to Theodore Uyeno of Valdosta State University in Georgia, whose laboratory work suggests how loose skin might work in minimizing damage from shark bites. He and colleagues have tested how hard it is to puncture swatches of skin from both the Atlantic and Pacific species. As is true for many other materials, punching through a swatch of hagfish skin held taut didn’t take as long as punching through skin patches allowed to go slack, he said in a January 5 presentation at the meeting. Even a slight delay when a sharp point bears down on baggy skin might allow the hagfish to start dodging and sliming.

But Michelle Graham, who studies locomotion in flying snakes at Virginia Tech, wondered if puncture wounds would be a drawback to such a defense. A hagfish that avoids a deep stab could still lose blood from the skin puncture. That’s true, said Fudge, but the loss doesn’t seem to be great. Hagfish have unusually low blood pressure, and video of real attacks doesn’t show great gushes.

Hagfish blood also plays a part in another benefit of loose skin — an unusual ability to wiggle through cracks, Fudge reported in a second talk at the meeting. One of his students built an adjustable crevice and found that both Atlantic and Pacific hagfishes can contort themselves through slits only half as wide as their original body diameter. Videos show skin bulging out to the rear as the strong pinch of the opening forces blood backward.

The cavity just under a hagfish’s skin can hold roughly a third of its blood. Forcing that reservoir backward can help shrink the body diameter. Fortunately the inner body tapers at the end, Fudge said. So as blood builds up, “they don’t explode.”