NEWS : TECH (NFPC)

Artificial Jellyfish Made From Rat Cells

Aside from Frankenstein, previous attempts to make synthetic life have focused on genes. Geneticist Craig Venter and his colleagues, for example, announced in 2010 that they had created a one-celled creature by inserting an artificial genome in an existing cell that reproduced.

Now a separate team of scientists from Harvard University and the California Institute of Technology have built an eight-armed jellyfish by inserting muscle cells from a rat into a sheet of silicone. The resulting "medusoid," as they called it, could offer insights into tissue engineering -- such as re-building a heart. And show that when building tissues, there might be several ways or materials to use other than those found in nature.

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To build the medusoid, the scientists mapped out the protein networks in a real jellyfish's muscle cells. They then looked at how electrical current triggers the muscle contraction.

Another piece of the puzzle was uncovering the mechanics at how jellyfish move. The animals squeezes a muscle to propel itself through the water, but it was important to study the biomechanics of the stroke in order to duplicate it.

The scientists also found that a sheet of cultured heart muscle tissue from a rat would contract when electrically stimulated in a liquid environment. By incorporating the muscle cells with a silicone polymer membrane, they were able to create a jellyfish-shaped body with eight appendages. The artificial creature was put into a container of salt water and hit with an electrical current. It started swimming just like a real animal.

The next step is making a jellyfish that engages in ordinary behaviors, such as seeking food and responding to its environment.

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Study co-author Kevin Kit Parker, professor of bioengineering and applied physics at Harvard, said he got interested in the project in 2007, when he started thinking about muscular pumps such as hearts. Seeing jellyfish at the New England Aquarium inspired him: he saw that there were similarities between jellyfish and human hearts.

Parker worked with Collaborating with Janna Nawroth, a doctoral student in biology at Caltech and lead author. They also worked with Nawroth’s adviser, John Dabiri, a professor of aeronautics and bioengineering at Caltech, and an expert in biological propulsion. The study was published in the journal Nature Biotechnology on July 22.

Credit: Harvard University, Caltech

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Engineered Viruses Could Kill Cancer

The last thing you need is a dangerous viral infection -- unless you have cancer.

Cancer cells divide like mad, crowding out their neighbors and causing tumors, the complications from which eventually kill. But the vigor has a price: cancer cells aren't as good at fighting off viral infections, and theoretically a virus could kill cancer cells without harming the patient.

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A great article in The New York Times by Rachel Nuwer describes medical efforts to commandeer viruses in the fight against cancer.

Those efforts date to 1951 when a 4-year-old child with leukemia caught chicken pox. The cancer went into remission. Unfortunately the moment the chicken pox went away, the leukemia came back and the child died.

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There were some attempts to use this phenomenon to benefit patients. Those early efforts ended in failure and by the 1960s the research focus shifted to other treatments.

But a lot has happened since then. Medical science has made strides in understanding the genetics and mechanisms of viruses and cancer both, and it may be that soon, tailored viruses could cure some cancers.

Dr. Robert Martuza, chief neurosurgeon at the Massachusetts General Hospital and professor of neuroscience at Harvard Medical School, started looking at herpes simplex virus, or HSV-1, as a cancer fighting tool back in 1991. Dr. Martuza took out a few genes from the virus and injected it into mice with brain cancer. Although the cancer went into remission most of the mice died of encephalitis.

Meanwhile, in 1990, Bernard Roizman, a virologist at the University of Chicago, found a gene in the herpes virus that when removed, makes it unable to get past the defenses of healthy cells -- but not cancer. That slowed the growth of cancer cells, though it didn't kill them.

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Six years later, Dr. Ian Mohr, a virologist at New York University, found a way of altering the virus that Roizman engineered. The virus evades the immune system and is better at killing cancer cells.

Herpes isn't the only virus being recruited for anti-cancer duty. Vaccinia was the virus used to protect against smallpox and it's now being tested against liver cancer. Thus far the results are promising, extending survival times in one group of patients. Others are bring used against melanoma, bladder cancer and head and neck cancers.

That doesn't mean it's time to break out the champagne. As the liver cancer trial shows, improving survival isn't the same as a cure, and every cancer is different. A magic bullet that works on every type is unlikely. Gary Hayward, a virologist at the Johns Hopkins Herpesvirus Research Program, told the New York Times that progress is likely to be incremental -- much as it has been for decades.

At the same time, another tool against cancer is always welcome, and it's another step in making cancer a survivable disease.

Credit: Wikimedia Commons / Centers for Disease Control

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Flesh Eating Bacteria Makes Super Molecular Glue

The same bacteria that eats flesh can make a super glue used to bind molecules.

Dr. Mark Howarth, with his graduate student Bijan Zakeri in Oxford University's department of biochemistry, developed an adhesive that sticks molecules together, nearly inseparably.

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They used the bacteria Streptococcus pyogenes, infamous for eating flesh when there is a serious infection and strep throat when it is mild. S. pyogenes makes a protein called FBab that forms a chemical bond between two groups of amino acids. And it does so really, really well.

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So Howarth and Zakeri decided to see if they could get that bond to separate and then come back together again. Their thinking was that if you tack on a molecule to the ends of the protein, you could join them and they would stay together -- just like two pieces of wood, plastic or metal joined by superglue.

The two fragments of the protein were nicknamed "Spycatcher" and "SpyTag." Once the scientists started experimenting with them, they found that the two stuck together and separated just as hoped. On top of that, the proteins didn't stick to anything else. And the molecular bond held at a wide range of temperatures. The bond even stood up to chemical detergents.

More importantly, the two molecules bonded without a lot of the fancy techniques usually used to link biomolecules. Ordinarily you need catalysts, or UV light. The problem is that if you want to stick molecules together in a living cell, that UV might not be a good idea as it can kill living organisms.

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This won't be the kind of glue that repairs your broken plastic bowl or broken glass (at least not yet). The first use will probably be in laboratories where scientists often have to stick biological molecules together, such as enzymes. In the future, though, there is a lot of promise -- one idea is to stick the chemicals in plants that make energy out of sunlight. Another is to join enzymes on an industrial scale.

Image: Wikimedia Commons / Centers For Disease Control and Prevention

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Vroom! World's Fastest Cells Drag Race

Ladies and gentlemen, start your... Petri dishes.

It may not have been the Indy 500, but a line of fetal mesenchymal bone marrow cells from Singapore recently out-dashed dozens of contenders to take the checkered flag at the World Cell Race. Claiming their title as the world's fastest cells, the microscopic racers zoomed across a Petri dish at the whiplash-inducing speed of 5.2 microns per minute, or 0.000000194 miles per hour.

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Results were announced December 3 at the American Society for Cell Biology's annual meeting in Denver, Colo. Fifty participating labs from around the world used 70 cell lines to not only race, but examine cell movement during the development of embryos, organs and cancer.

Teams shipped the cells frozen to designated laboratories in Boston, London, Heidelberg, Paris, San Francisco and Singapore. Once thawed, the cells were placed in "race tracks" that were 400 microns long (0.015748 inches) and coated with a substance that gave the little guys some tire-like traction. Digital cameras recorded the cells for 24 hours to determine, out of the 200 cells, which one was the fastest to reach the end of the track.

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A line of unaltered breast epithelial cells took second place and third place went to the the same cell type only altered to reflect patterns observed in cancerous cells. Researchers responsible for the winning cells received Nikon digital cameras and World Cell Race medals.

[Via Nature]

Credit: Monya Baker

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Poo-Powered Glowing Bacteria Light Up the House

The bioluminescence of fireflies and "Red Tide" are arguably two of nature's most beautiful phenomena, leaving us spellbound in a open field or on the shore with our mouths agape. But have you ever considered lighting your home with this kind of light?

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Dutch electronics company Phillips has. In fact, they've created Bio-light, a greener lighting system that's part of their Microbial Home (MH) system. It isn't powered by electricity or sunlight, but by glowing bioluminescent bacteria that thrive on waste generated in the average home.

The bioluminescent bacteria is housed in hand-blown glass cells, clustered together to form a lamp that could easily be displayed in a modern art museum. Each cell is connected to the lamp's reservoir base by thin silicon tubes that pipe methane gas from composted bathroom solids and vegetable scraps via a kitchen dodad that digests bio-waste.

As long as proper nutrients are supplied, the bio-light's living bacteria can be powered indefinitely. Although the light isn't bright enough to fully replace conventional lighting, it does make people conscious of household forms of wasted energy that could be tapped.

Clive van Heerden, Senior Director of Design-led Innovation at Philips Design, says drastic changes are required to reduce our environmental impact and designers must lead the way.

“Designers have an obligation to understand the urgency of the situation, and translate humanity’s needs into solutions," he said, according to Phillips Design's website. "Energy-saving light bulbs will only take us so far. We need to push ourselves to rethink domestic appliances entirely, to rethink how homes consume energy, and how entire communities can pool resources.”

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Phillips envisions their bio-light technology being used on warning strips on curbs and steps, signs in theaters or clubs, and even night-time road markings.

[Via GizMag]

Image Courtesy of Philips

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Computers 'Talk' to Yeast

Scientists have used a computer to "talk" to yeast in a Zurich laboratory. In the conversation, the researchers created a communication loop between regular brewers yeast and a computer, giving control to the computer over protein production in the yeast cell. This "feedback control" between the computer and the yeast is the first of its kind and opens the door to use a computer to manage genetically altered microorganisms.

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In 2002, a study in Nature Biotechnology found that when a red light was shone onto basic yeast (called Saccharomyces cerevisiae), it would become active and produce a protein. A deeper red light would deactivate the cells.

Now the team has taken the research a step farther by tying a "reporter molecule" to a gene that activates the production of the protein. When the yeast begins protein production, the fluorescent reporter molecule actives as well. This molecule can be seen by a computer to confirm that the yeast are active. Once the desired level of protein is reached, the computer can flash a deeper red light, deactivating the yeast.

Using this "feedback control" system, the mechanism of control is moved outside of the cell to the computer, which controls the level of protein production in these S. cerevisiaei cells.

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The science is complex, but the idea is straightforward; computerized control of a bacteria could revolutionize biotechnology. Bacteria are used for a number of industrial purposes, from making pharmaceutical products to creating biofuels to digesting trash. By shining lights onto the cells, computers could maximize this bacteria activity.

"There are many people who have tried to do things like this by, for example, coding in the cell itself a synthetic circuit, putting genes and mechanisms in the cell," said John Lygeros at the Automatic Control Laboratory at the Swiss Federal Institute of Technology (ETH) in Zurich told the BBC.

In the past, scientists have used complex "genetic trickery to accomplish similar goals," said Lygeros. Now, rather than using "genetic trickery," they use this external controller. With this new system, scientists hope to create a more stable system.

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Once the communication was established, Professor Lygeros commented it was not simply an on-off switch. He told the BBC, "The fluorescence is not the only thing -- there are half a dozen chemical reactions involved in this process… Experimentally, it's a fairly challenging thing to do."

Implications abound with this technology. Once computers can control cell production and turn genes on and off, the door is open to creating to control production and replication in larger cell groups (read: animals, humans). Someday, we may be able to use technology like this to grow new organs, create stem cells or even tell the brain to rebuild and repair itself.

The paper was published in Nature Biotechnology.

Image: iStockPhoto

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ePetri Could Make Microscopes Obsolete

A team of engineers from the California Institute of Technology (Caltech) say they've created a "smart" Petri dish using a Google smart phone, a cell-phone image sensor and Lego building blocks.

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Their so-called ePetri platform could potentially make cumbersome microscopes a thing of the past. The group also says their prototype reduces human labor time and improves the way in which culture growth can be recorded.

"Our ePetri dish is a compact, small, lens-free microscopy imaging platform. We can directly track the cell culture or bacteria culture within the incubator," explained Guoan Zheng in a Caltech news release. Zheng is lead author of the study and a graduate student in electrical engineering at Caltech.

Cultures are places inside the image-sensor chip while the smart phone's LED screen serves as a scanning light source. After the device is placed in an incubator, the image sensor snaps a photo of the culture. That data is sent to a laptop via a wire running from the incubator to the computer. This allows researchers to capture images of cells as they grow in real time.

The ePetri device is particularly good at capturing images of cells that grow very close together, known as confluent cells.

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"Until now, imaging of confluent cell cultures has been a highly labor-intensive process in which the traditional microscope has to serve as an expensive and suboptimal workhorse," Changhuei Yang, senior author of the study and professor of electrical engineering and bioengineering at Caltech, said in a press release. "What this technology allows us to do is create a system in which you can do wide field-of-view microscopy imaging of confluent cell samples. It capitalizes on the use of readily available image-sensor technology, which is found in all cell-phone cameras."

[Via GizMag]

Credit: Gary Buss/Getty Images and Caltech

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Spies Can Hide Secret Messages in Bacteria

Espionage just got a little more sophisticated and scientific. Invisible ink? Decoder rings? Lemon juice? Puh-lease -- that's mere child's play compared to what double agents scientists at Tufts University just created.

SCIENCE CHANNEL VIDEO: Supernatural Spies. During the Cold War, the Soviets used a psychic technique known as remote viewing.

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Now secret messages can be hidden in genetically engineered bacteria, thanks to a new method called steganography by printed arrays of microbes, or SPAM. Developed by chemistry professor David Walt and his cloak-and-dagger team of researchers, this new method uses an assortment of E. coli strains modified with fluorescent proteins that glow in seven colors.

Multiply that number by the two colors each message character is encoded with, and spies like us have more than 49 possible code combinations. That's enough for the alphabet, plus digits 0 to 9, with room left over for a few extra symbols.

The secret microbial messages are first grown in petri dishes. The cultures are then transferred to a thin film and ready to be sent to the desired undercover recipient. To unlock the message, the recipient must transfer the bacteria to a genetically modified growth medium, which acts as the secret key.

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For example, the bacteria could be engineered to react only with a certain antibiotic, therefore allowing the message to be revealed only when in contact with that specific chemical. If any other chemical key is used, the message would be scrambled.

Self-destructing messages could also be created by using bacteria that loses its fluorescence over time.

[Via NewScientist]

Image: Tufts University 2011

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Networking Website Matches People by Gut Bacteria

eHarmony says they match you according to your personality and Facebook lets you connect with others according to common interests. MyMicrobes wants to match you according to your gut bacteria.

A non-profit operation, MyMicrobes is asking people to sign up and get their gut bacteria sequenced. Yes, you have to provide a stool sample, but you can also use the site to share your stories of digestive distress.

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This sounds like an opener to comedy skit, but there is a serious purpose. The research team is part of the Metagenomics of the Human Intestinal Tract (MetaHIT) Consortium. They published a paper in Nature that says people seem to fall into three "enterotypes" -- basically three categories of gut bacteria. It's rather like dividing the world into different biomes or habitats.

DNEWS VIDEO: SYNTHETIC LIFE, ENGINEERING TISSUE AND MORE …

What makes this important? Your gut bacteria respond to different drugs or diets. Finding a way to classify the kind of gut bacteria you have -- essentially figuring out what is "normal" for a given type of person -- will go a long way to helping diagnose problems. And those bacteria are important. They perform many functions that people need, extracting useful nutrients such as vitamins.

People certainly do want answers. Peer Bork, a biochemist at the European Molecular Biology Laboratory and a co-founder of the site told Nature he got the idea for MyMicrobes after getting nearly 100 emails from people concerned about their digestive problems. Plainly people are seeking answers.

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Hence MyMicrobes. To join up you pay $2,100, which seems steep -- Facebook is free, after all -- but it covers the cost of sequencing the genomes of the critters in your guts. Members get a stool-sample kit. The sample gets sent to a lab in Paris, where the DNA is extracted. The DNA goes to Bork's lab in Germany.

There are about 100 participants so far, and the researchers' estimate is that they need about 5,000 to perform more meaningful studies. It's possible gut bacteria might show responses to non-digestie ailments as well. In the small sample that was cited in the Nature paper there were 12 genes in the gut bacteria that correlated well with age, for instance. 

Via Nature.

Image: Wikimedia Commons via National Institutes of Health

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How Bacteria Clean Up Nuclear Waste

Bacteria can clean up toxins, oil spills and nuclear waste, essentially by eating the stuff. But until now nobody was quite sure how they did it. Gemma Reguera and her team at Michigan State University found that the key is a structure called the pilus, a hair-like appendage that acts like a wire.

The bacteria, called Geobacter sulfurreducens, transfer electrons via the pilus to the metals that they feed off of. Transferring the electrons gives the bacteria energy. It also changes the ionization state of the metal, changing it to a form that precipitates out of water. A colony of Geobacter living near a pile of nuclear waste would extract the uranium, making it easier to handle and remove.

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That was all very well, and the electron transfer has even been proposed as a way to build biological batteries. But an outstanding question was how Geobacter kept the uranium (and other chemicals) in nuclear waste away from their cellular walls, where the waste could cause damage. To see what role they played it was necessary to get a bunch of bacteria to grow lots of them in a lab. Reguera's team did that by exposing the bacteria to much harsher conditions than they were used to, stimulating them to grow more pili.

What they found was that the pili act as a buffer between the bacteria and the metallic compounds. The pili are quite long relative to the bacteria, and form a conductive barrier. That barrier is also a big part of the reason Geobacter can live in environments that would kill many other organisms.

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The team published their work in the Proceedings of the National Academy of Sciences. In the paper they note that knowing how Geobacter species work makes it easier to come up with strategies to clean up toxic spills. It might even allow researchers to design tiny robots to do the job, or come up with ways to grow better toxin-eating bacteria.

Photo: Geobacter cell (in orange) with the nanowires (in yellow) interspersed through the uranium (black material). Credit: Dena Cologgi and Gemma Reguera (Michigan State University).

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