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New method for turning genes on and off could enable more complex synthetic biology circuits
MIT researchers have shown that genes on or off in yeast and human cells by controlling, when DNA into RNA - bypokrok that will allow scientists to better understand the function of these genes copy.
This technique can also be easier to control the environment of the cell produkujídrogy or disease realize engineer, says Timothy Lu, assistant professor of electrical engineering and computer science and bio - engineering and lead author of a paper describing the new approach in the journal ACS Synthetic Biology.
"I think it will be much easier to build synthetic circuits" says Lu, a member of the Synthetic Biology Center at MIT. "It should increase the extent and speed with which we can build a number of synthetic circuits in yeast and mammalian cells."
The new method is based on a system of viral proteins have been used recently for the treatment of genomes of bacteria and human cells. Initial system called CRISPR consists of two parts: a protein which binds to DNA and washers and a short strand of RNA, leaders of the protein into the correct position in the genome.
"CRISPR system is so powerful that it can be used for a variety of DNA - binding regions of a simple conversion of this handbook RNA targeted basis" says Lu. "By simply reprogramming the RNA sequence of this protein can be any place you want to call the genome or synthetic circuit."
The main author of the article is Farzadfard Fahim, an MIT graduate student of biology. Samuel Perl, student of Electrical Engineering and Computer Science, is takéautorem.
Targeting transcription
In previous studies CRISPR was used to cut pieces of the gene is switched off or replace it with another gene. Lu and his colleagues decided to use the CRISPR system for a different purpose : control of gene transcription is the process by which DNA sequence into RNA (mRNA ), which goes beyond genes copied instructions.
Transcription is strictly regulated by proteins called transcription factors. These proteins bind to specific DNA sequences in the promoter region of the gene, and either modify or block the enzymes needed for the copy of the gene into mRNA.
Which acts as a transcription factor for this study, the researchers adjust CRISPR system. Firstly, the modified CRISPR normal protein known as time9 so that it no longer cut the DNA bound thereto. They are also added to the protein, the segment that is activated or suppressed by modulating gene expression machinery of cellular transcription.
Time9 to get to the right place, the researchers also corresponds delivered to the target cells, the genes for RNA guides who chtějísekvence DNA activates the promoter of the gene.
Researchers have shown that when the guide RNA and protein time9 connection in the target cell, the target gene přesněpravý atranskripce. To their surprise, the same complex time9 also used to block transcription to be found in other parts of the gene.
"It's nice that allows you to make a positive and negative regulation of the same protein, but with different RNA targeted to various managerial positions in the promoter" says Lu.
"A lot of elasticity"
The new system should be much simpler than other newly developed two systems for the transcription of DNA - binding proteins such as zinc finger transcriptional activator and effector Nucleases ( Talens ) is known, says Lu. Although effective, the construction and assembly of proteins is time- consuming and expensive.
"There is a lot of flexibility with CRISPR, and it really comes from the fact that you do not spend more time in protein engineering. You can only change the sequence of the nucleic acid RNA, " says Lu.
"The fact that this can be used for effective regulation of transcription in both yeast and mammalian cells, it is very encouraging," says Kobi Benenson, Professor of Biosystems Science and Engineering at ETH Zurich, which is not part of the research team." This technology may be used in the very near future genetic engineering and synthetic biology applications for biopharmaceuticals - "Tissue engineering and gene therapy, among other things"
Researchers also transcriptional control designed so that it can be triggered by specific small molecules, which may be included in the cell, such as sugars. For this, the guide RNA genes constructed so that they are only produced Primal molecule is available. No small molecules, there are no guidelines aRNA gene is targeted at rest.
This type of control could be used to explore the role of naturally occurring genes on and off at specific times during development or progression useful, says Lu.
Lu is now working on the development of advanced synthetic circuits for applications such decisions are based on multiple inputs made by the mobile environment. " We want to be able to scale- up the most complex circuits and show that anyone is ever built in yeast and mammalian cells" he says.
Killer Hospital Bacteria: Cracking a Superbug's Armour
There's new hope for development of an antibiotic that can put down a lethal "superbug" bacteria linked to the deaths of hundreds of hospital patients around the world, including a recent case at Edmonton's Royal Alexandra Hospital.
Researchers from the University of Alberta-based Alberta Glycomics Centre found a chink in the molecular armour of the pathogen Acinetobacter baumannii. The bacteria first appeared in the 1970s and in the last decade it has developed a resistance to most antibiotics.
U of A microbiologist Mario Feldman identified a mechanism that allows Acinetobacter baumannii to cover its surface with molecules known as glycoproteins. That led the researchers to another discovery. "If the superbug cannot produce glycoproteins they become less virulent and less capable of forming biofilms," said Feldman. "The biofilm protects the bacteria from antibiotics."
Acinetobacter baumannii is a particularly insidious and contagious pathogenic bacteria that has plagued hospitals around the world. It spreads from one person to another by physical contact. The bacteria can live on hard surfaces for several days and can cling to hospital equipment like catheter tubes and inhalers. Acinetobacter infection is also spread by coughing and sneezing.
Hospital patients whose immune systems are already worn down are the most susceptible to the bacteria. It infects wounds and can spread to the lungs, blood and brain.
The researchers say more work is required to understand how the bacteria produce glycoproteins. "We're hopeful our work will enable future development of drugs to interrupt the production of glycoproteins to weaken or eliminate the bacteria's shield against antibiotics," said Feldman.
Feldman is a principal investigator for the Alberta Glycomics Centre at the U of A. The list of coauthors includes U of A graduate students Jeremy Iwashkiw and Brent Weber, and research colleagues in Ottawa, Austria and Australia. Their work was published June 7 in the journal PLoS Pathogens.
Lab-Grown Model Brains
Three-dimensional tissues called “cerebral organoids” can model the earliest stages of brain development.
In an Austrian laboratory, a team of scientists has grown three-dimensional models of embryonic human brains. These “cerebral organoids” are made from stem cells, which are simply bathed in the right cocktail of nutrients and grown in a spinning chamber. Over a few weeks, they arrange themselves into pea-sized balls of white tissue, which recapitulate some of the complex features of a growing brain, including distinct layers and regions.
“This demonstrates the enormous self-organizing power of human cells,” said Jürgen Knoblich from the Institute of Molecular Biotechnology of the Austrian Academy of Science, who led the study published in Nature today (August 28). “Even the most complex organ—the human brain—can start to form without any micro-manipulation.”
Knoblich cautioned that the organoids are not “brains-in-a-jar.” “We’re talking about the very first steps of embryonic brain development, like in the first nine weeks of pregnancy,” he said. “They’re nowhere near an adult human brain and they don’t form anything that resembles a neuronal network.”
These models will not help to unpick the brain’s connectivity or higher mental functions but they are excellent tools for studying both its early development and disorders that perturb those first steps. For example, Knoblich’s team produced unusually small organoids using stem cells taken from a patient with microcephaly—a neurodevelopmental disorder characterized by a small brain. Knocking out microcephaly-associated genes in mice does very little because murine brains develop differently than humans’. The organoids could help to bypass the limitations of these animal models, providing a more accurate representation of human brains.
Madeline Lancaster, a member of Knoblich’s group, created the 3-D models from small clusters of stem cells. She bathed the cells in nutrients that nudge them toward a neural state, embedded them inside a gel for structural support, and grew them in a spinning bioreactor to help them absorb more nutrients. It took a huge amount of work to fine-tune the conditions, but once the team did, the organoids grew successfully within just 20 to 30 days.
Using molecular markers tuned to specific parts of the brain, Lancaster showed that the organoids develop a variety of distinctive zones that correspond to human brain regions like the prefrontal cortex, occipital lobe, hippocampus, and retina. They also included working neurons, which were produced in the right way—they were made by radial glial cells at the innermost layers of the cortex, before migrating to the outer layers.
Other scientists have developed organoids that mimic several human organs, including eyes, kidneys, intestines, and even brains. For example, in 2008, Yoshiki Sasai’s team at the RIKEN Center for Developmental Biology showed that stem cells can be coaxed into balls of neural cells that self-organize into distinctive layers. But compared to this earlier attempt, the new organoids are “the most complete to date in terms of features that directly resemble those in the developing human brain,” according to Arnold Kriegstein, a stem cell biologist from the University of California, San Francisco, who was not involved in the study.
“They really highlight the ability just nudge these human embryonic cells and allow them to self-assemble,” Kriegstein added. “So much of the signalling that goes on and the actual specification of different parts of the brain occur intrinsically in these cells.”
Having refined their technique, the team created a “personal organoid” from a Scottish patient with severe microcephaly, who had several mutations in a gene called CDK5RAP2. They took skin cells from the patient, reprogrammed them into a stem-like state, and used them to grow organoids that ended up much smaller than usual. By dissecting the organoids, the team discovered the reason for this stunted size.
When healthy brains develop, radial glial cells first divide symmetrically to increase their numbers before dividing asymmetrically to produce neurons. In the microcephalic organoids, this switch happens prematurely, and neurons start forming when the pool of radial glial cells is too low. As a result, the brains do not develop enough neurons and end up small. CDK5RAP2 is responsible for this premature switch; when the team added the protein back into the mutant microcephalic organoids, they grew to a normal size.
Wieland Huttner, a neurobiologist from the Max Planck Institute of Molecular Cell Biology and Genetics, said that these results merely confirm what others had already suspected about CDK5RAP2. However, the organoids could be more useful for understanding other microcephaly genes whose roles are still unclear.
For example, mutations in the ASPM gene can shrink a human brain by a third of its normal size, but barely make a dent in the size of a mouse brain. “The mouse brain isn’t good enough for studying microcephaly,” said Huttner. “You need to put those genes into an adequate model like this one. It is, after all, human. It definitely enriches the field. There’s no doubt about that.”
Knoblich cautioned that organoids are unlikely to replace animal experiments entirely. “We can’t duplicate the elegance with which one can do genetics in animal models,” he said, “but we might be able to reduce the number of animal experiments, especially when it comes to toxicology or drug testing.”
In the future, he hopes to develop larger organoids. For the moment, the models cannot get any bigger without a blood supply, and their interiors are dead zones comprised of starving, choking cells. If the team can solve this problem and coax the organoids to continue growing, they might be able to capture later events in brain development, which may be relevant to other disorders, like autism. “That would be a gigantic step forwards,” said Knoblich.
Scientists 'grown' tiny brains in laboratory
Miniature "human brains" were grown in a laboratory and scientists hope that this will change the understanding of neurological diseases.
Structures with dimensions of pea achieved the same level of growth as in fetal nine weeks, but are not mental abilities.
Research scientists published in the journal "Nature" is already used for the understanding of rare diseases.
Neurologists defined discovery as amazing and wonderful. The human brain is one of the most complex structures in the universe. But scientists from the Institute of Molecular Biotechnology of the Austrian Academy of Sciences were able to reproduce some of the earliest stages of development of the body in a laboratory.
They used or embryonic stem cells, or cells from the skin of adults to produce part of the embryo that develops into the brain and spinal cord - neuroectoderm. It was placed in the gel droplets to create a scaffold for the development of the tissue, and then in a rotating bioreactor, "food bath", which supplies nutrients and oxygen.
Cells were able to develop and organize in specific areas of the brain such as the cortex, retina and rarely in primary hippocampus, which is closely related to memory in a fully developed brain of an adult. Scientists are convinced that this is similar to a nearby extent (but far from perfect) brain development of an embryo until the ninth week. Tissues reached a maximum of about 4 mm after two months.
"Mini brains" survived nearly one year and not more increased because no blood flow and brain tissue only, so that the nutrients and oxygen can not penetrate to the center of the structure resembling the brain.
"Our organelles are useful for showing the pattern of brain development and to study the causes of the problem in development. Want to move on to the more common disorders such as schizophrenia and autism. They usually occur only in adults, but it was shown that hidden defects occur during brain development, "said one of the researchers, Dr Juergen Noblih.
The technique can be used to replace the mouse and rat in the study of drugs, since the new drugs can be tested on an actual brain tissue. Scientists have managed to create brain cells in a lab before, but this is the closest model to which one is reached in the creation of a human brain.
Nanosensors can help in the production of drugs
Experts in the field of engineering, chemical compounds from MIT (Massachusetts Institute of Technology, MIT, USA) showed that the matrix consisting of billions of nanoscale sensors have unique properties that can enhance the safety and efficiency of various drugs, particularly drugs, based on antibodies.
With these sensors, the scientists were able to characterize the different types of interactions of drugs based on antibodies, which in the long run will help in the development of effective treatments for cancer and other diseases. The sensors can be used to assess the structure of antibody molecules and determining their content of sugar chains that prevent their functioning.
"Pharmacological method can help companies identify the reason for a certain technology of preparation of medicines work better than others, which will increase the efficiency of production", - says Michael Strano (Michael Strano), a professor of chemical engineering at MIT, one of the authors of the Nanoscale sensors, recently published in the journal ACS Nano.
According to Strano, the research team also demonstrated how nanosensor matrix can be used to determine the most productive and preferred cells in a population of genetically modified cells that synthesize drugs.
Evaluating the effectiveness of drugs
The results of previous studies conducted by countries and other scientists have shown that the use of the finest nanoscale sensors, such as carbon nanotubes, is an effective method to determine the chemical compounds present in the solution in small amounts. Carbon nanotubes are 50 thousand times thinner than a human hair. They are able to join the proteins recognize specific Targeted molecule. If the solution contains Targeted molecule fluorescent signal produced by the carbon nanotube varies and it can be detected.
For the simultaneous determination of a large number of different targets in solution, some scientists are trying to use a large array of nanosensors, in particular, carbon nanotubes or semiconductor nanowires, each of which focuses on a specific targeted molecule. In the new study, Strano and his colleagues studied the unique properties of large sensors that detect the same chemical.
The first property, scientists detected nanosensors - is that the matrix consisting of equally spaced sensors can measure the force distribution compounds arising in complex proteins such as antibodies.
Antibodies - the body naturally synthesized molecules that play a key role in the immune response. In recent years, scientists have developed antibodies to treat various diseases, including cancer. The addition of these antibodies to surface proteins of cancer cells stimulates an immune response to the tumor.
To drugs based on antibodies to be effective, they must be specifically attached to its target. However, the process of antibody production , which is dependent on engineering cells does not always lead to the production of consistently and uniformly acceding parties antibodies.
Currently, for testing batches of drugs in order to confirm their compliance with the performance standards used by pharmaceutical companies for long time and expensive analytical processes. The new sensor, developed by scientists from MIT, can greatly speed up the process, allowing scientists not only to more effectively monitor and control the process of production of drugs, but also to fine-tune their production. This will result in a more uniform product synthesized.
Measurements of weak interactions
Another nice feature of sensors is their ability to measure the weak binding interactions that can also help in the production of drugs based on antibodies.
Normally, this process of protein glycosylation antibodies surface is covered with long chains of carbohydrates which provide drug efficacy. But sugar chain is extremely difficult to detect, since they interact with weak bonds with other molecules. Organisms that produce antibodies are programmed in such a way as to connect the chain of sugars. However, this process is difficult to control, and it largely depends on the environment surrounding the cells, including the temperature and acidity.
If an antibody is introduced into the patient will not be glycosylated proteins, they can cause the development of an unwanted immune response or be destroyed by the patient's own cells, making them useless.
According to Strano, drug companies and scientists who have tried to identify glycosylated proteins by recognizing the hydrocarbon chains, experienced difficulties. "Nanosensor matrix can greatly increase the possibility of determining the rare events of joining molecules. You will be able to measure something that is not able to estimate with a large sensor with the same sensitivity, "- says the country.
The new method could help scientists determine the optimal conditions for adjusting the degree of glycosylation of proteins that facilitate the production of equally effective drugs.
The definition of the product obtained
The third property of nanoscale sensors, studied by scientists - is the ability to detect the synthesis of a molecule of interest. According to Strano, professionals want to be able to identify specific strains of microorganisms that synthesize the necessary medicines. "There are many ways to do this, but none of them is not easy," - says the country.
The research team from MIT found that culturing the cells on the surface coated with a matrix of nanoscale sensors that can help identify the location of the majority of synthesizing cells. In the new study, the researchers studied the antibodies are synthesized artificially synthesized human embryonic kidney cells. However, established engine also can be individually configured to proteins and other organisms.
According to Strano, immediately after the detection of the most productive cells, scientists are studying the genes that distinguish these cells from other cells that have a lower efficiency in the production of medicines. As a result, they create a new strain having increased ability to synthesize the desired chemical compounds.
Scientists have created a prototype of a portable sensor, which they plan to test in the pharmaceutical company Novartis. The study will be funded by Novartis and the National Science Foundation (National Science Foundation, USA).
DNA Damage: The Dark Side of Respiration
Adventitious changes in cellular DNA can endanger the whole organism, as they may lead to life-threatening illnesses like cancer. Researchers at Ludwig-Maximilians-Universitaet (LMU) in Munich now report how byproducts of respiration cause mispairing of subunits in the double helix.
The DNA in our cells controls the form and function of every cell type in our bodies. The instructions for this are encoded in the linear sequence of the four subunits found in DNA, the bases adenine (A), cytosine (C), guanine (G) and thymine (T). Random changes in the sequence can lead to cell dysfunction, and may result in unrestricted cell proliferation and malignancies. Mutations can be induced by a variety of agents. For example, cellular respiration, i.e. the reduction of inspired oxygen to water, which powers cell function, also generates highly reactive oxygen species that can damage DNA, with the purine bases G and A being particularly susceptible to this kind of attack.
"Reactive oxygen species are responsible for two different sorts of DNA damage, as they induce formation of both 8-oxo-G and FaPy-G," says Professor Thomas Carell of the Department of Chemistry at LMU. In 2004, work done by Carell and his team defined how 8-oxo-G generates mutations. However, the basis for the mutagenic effect of FaPy-G has remained obscure -- until now. In their latest publication, Carell and his colleagues describe how FaPY-G leads to mispairing of bases in the double helix.
Pernicious partner swapping One G in one strand of the double helix normally matches up with a C on the other, forming a G:C pair. But as a consequence of damage by reactive oxygen species, the guanine base may be transformed into FaPy-G, so that we get a FaPy-G:C base pair. "We have now shown that, in the course of DNA replication prior to cell division, FaPy-G interacts with adenine, leading to the formation of FaPy-G:A base pairs. This partner swap is unusual, since unmodified guanine normally does not team up with adenine," Carell notes.
FaPy-G is subsequently recognized as abnormal and is removed by DNA repair enzymes. The missing base is replaced by a T -- which is the usual partner for A. The net result is that the original G:C base pair has been converted into an A:T pair, and the base sequence has undergone a potentially dangerous mutation.
This outcome is made possible by the fact that the cell's damage-control systems find it surprisingly difficult to distinguish the normal guanine base from its aberrant derivative FaPy-G during DNA replication. "That this defect then leads to mispairing with adenine is one of the main reasons for the spontaneous development of tumors," says Carell. "So with every breath we take, our risk of getting cancer goes up by a teeny-weeny bit." Further insights into the reasons why FaPy-G often eludes the cell's detection and correction systems could help to improve the treatment of cancer, as the inhibition of DNA repair processes in tumor cells increases their sensitivity to chemotherapeutic drugs.
The study was supported by DFG grants awarded to Collaborative Research Centers 646 and 749 and the Center for Integrated Protein Science Munich (CIPSM), an Excellence Cluster.
The human body strengthens protection against influenza throughout life
A natural reaction to the pandemic influenza virus - an ideal model, suitable for a universal flu vaccine. According to Live Science, researchers specifically examined the changes in the immune system caused by constant exposure to the virus of influenza. Analysis was applied to blood samples from 40 people 35-70 years of age.
People are faced with two strains of the pandemic virus (H2N2 - in 1957 and H1N1 - in 1977), had elevated levels of immune proteins - a broad spectrum neutralizing antibodies. These antibodies attack the part of the virus, called a "trunk". It differs only slightly depending on the strain. But the "head" of the virus changes frequently. If you find a way to increase the concentration of these antibodies, you get a new vaccine against influenza.
However, such antibodies do not normally produced in large quantities when in contact with the seasonal influenza. The body realizes that it is now important to produce antibodies that attack the "head" of the virus.
And only if the virus is very different from the previous ones by the structure of the "head" (it comes with a pandemic strain), the body begins to increase the concentration of neutralizing a broad spectrum of antibodies that work against the "trunk". The aim - to create a vaccine conditions similar to those that are added when pandemic influenza.
The highest concentration of neutralizing antibodies in humans was facing more than one pandemic. If a person is in contact with H2N2, and H1N1, the figures are higher by 3.8 times compared to a person, only bolevshim H1N1.
The level of antibodies targeted at the "head" of the virus, eventually grew - despite the fact that the contact with the pandemic virus was only once. From this, scientists have concluded that immunity to this strain of flu remains active for a long time. And in fact, the body is constantly enhances protection against strains with which the person met.
Buy Influenza products form Gentaur:
Flu antibodies can make disease worse
Some antibodies to flu viruses may actually make patients sicker, a new study of pigs suggests.
The finding, published August 28 in Science Translational Medicine, may point to problems with catchall influenza vaccines.
Pigs vaccinated against a seasonal strain of influenza made antibodies to that strain. Some of the antibodies could also latch on to a different flu virus that caused a pandemic among humans in 2009, report scientists led by Hana Golding of the Food and Drug Administration’s Center for Biologics Evaluation and Research in Bethesda, Md., and Amy Vincent of the Department of Agriculture’s National Animal Disease Center in Ames, Iowa.
Instead of protecting the pigs against the 2009 pandemic flu, the broad-range antibodies actually helped the virus invade lung cells, causing pneumonia and lung damage.
Scientists hoping to create a universal flu vaccine need to learn how the pigs’ antibodies and viruses interacted to make the disease worse, James Crowe Jr. of Vanderbilt University writes in a commentary in the same issue of the journal.
And vaccines aren't the only problem, Crowe says. Natural infections may provoke similar disease-worsening problems.
Watching the production of new proteins in live cells
Researchers at Columbia University, in collaboration with biologists in Baylor College of Medicine, have made a significant step in understanding and imaging protein synthesis, pinpointing exactly where and when cells produce new proteins. Assistant Professor Wei Min's team developed a new technique to produce high-resolution imaging of newly synthesized proteins inside living cells. The findings were published in the July 9th issue of The Proceedings of the National Academy of Sciences (Volume 110; Issue 28).
Proteins carry out almost every crucial biological function. Synthesis of new proteins is a key step in gene expression and is a major process by which cells respond rapidly to environmental cues in physiological and pathological conditions, such as cancer, autism and oxidative stress. A cell's proteome (i.e., the sum of all the cell's proteins) is highly dynamic and tightly regulated by both protein synthesis and disposal to maintain homeostasis and ensure normal functioning of the body. Many intricate biological processes, such as cell growth, differentiation and diseases, involve new protein synthesis at a specific location and time. In particular, long-lasting neuronal plasticity (changes in neural pathways and synapses that come from alterations in behavior, environment and bodily injury), such as those underlying learning and long-term memory, require new protein synthesis in a site- and time- dependent manner inside neurons.
Min and colleagues' new technique harnesses deuterium (a heavier cousin of the normal hydrogen atom), which was first discovered by Harold Urey in 1932, also at Columbia University. When hydrogen is replaced by deuterium, the biochemical activities of amino acids change very little. When added to growth media for culturing cells, these deuterium-labeled amino acids are incorporated by the natural cell machineries as the necessary building blocks for new protein production. Hence, only newly synthesized proteins by living cells will carry the special deuterium atoms connected to carbon atoms. The carbon-deuterium bonds vibrate at a distinct frequency, different from almost all natural chemical bonds existing inside cells.
The Columbia team utilized an emerging technique called stimulated Raman scattering (SRS) microscopy to target the unique vibrational motion of carbon-deuterium bonds carried by the newly synthesized proteins. They found that by quickly scanning a focused laser spot across the sample, point-by-point, SRS microscopy is capable of delivering location-dependent concentration maps of carbon-deuterium bonds inside living cells.
"Incorporation of deuterium-labeled amino acids to new proteins is minimally disruptive, and their biochemical properties are almost identical to their natural counterparts," says Lu Wei, the lead author of the paper. "Our technique is highly sensitive, specific, and compatible with living systems under physiological conditions that don't require killing cells or staining."
Prior to this discovery, the ability to observe protein synthesis in living cells had eluded scientists, who devoted extensive efforts to achieving this goal. A classic strategy that involves labeling amino acids with radioisotopes to trace and quantify proteome dynamics requires the samples be killed and exposed to films. Fluorescence microscopy, another popular method, takes advantage of the inherent glowing of green fluorescent protein (GFP) to follow a protein. While this process does work on individual proteins, scientists can't observe the cell's entire proteome. A third technique, bioorthogonal noncanonical amino acid tagging (BONCAT) metabolically incorporates unnatural (biosynthetic) amino acids containing reactive chemical groups. However, the method generally requires killing cells and subsequent dye staining, a process that presents an issue for live tissues and animals. Therefore, it is extremely challenging and desirable to quantitatively image proteome synthesis in living cells, tissues and animals with high resolution. Min's research opens the door for a new method to study living cells, presenting opportunities to understand previously unanswered questions about the behavior of cells as they perform their functions.
The next step for Min's team is to capture where and when a new protein is produced inside brain tissues when an animal is subject to various lab exercises to form long-term memory. "Our new technique will greatly facilitate understanding the molecular mechanisms of many complex behaviors such as learning and diseases," he says.
Bat brought deadly new infection MERS
Bats in Saudi Arabia are the source of a mysterious virus that sick nearly 100 people and half of them died, said, "New York Times". For the Middle respiratory syndrome coronavirus (MERS) to speak a little more than 15 months after the infection started to kill people in the Middle East and traveled far Europeans. The virus causes severe pneumonia with respiratory failure. With the increase in not only the region but also in Europe, the World Health Organization warned that could lead to an epidemic. The first fear is for the upcoming Hajj, when millions of pilgrims gather in Mecca. Forbid a blast, but the disease has not abated with time.
Initially the virus was associated with the cause of TORS, which has spread to 30 countries and killed 800 people in 2003, but later it turned out that the two strains are genetically different.
In a study published on Wednesday, an international team of doctors attributed the spread of new species of small mammals. But cautioned that many questions remain.
The virus was detected in faecal sample of bat species Taphozous perforatus, who inhabit abandoned buildings and even tombs. But it is not clear how dangerous infection has come to humans because these animals usually do not bite people, and there is no way to contaminate food. According to veterinarian Dr. Jonathan Epstein, who helped in the study, it is possible that infection occurred through inhalation of dust from the droppings of "flying mice". Most likely when cleaning. Similarly hantaviruses is now transmitted by the mice of people.
But it is also possible coronavirus bat first passed in pets and they do it "moved" to the people. Days ago scientists announced they had found a similar virus antibodies in camels in Oman. And even appear hypothesis that they are the source of infection.
Bat with MERS was found in an abandoned house in the date palms in a small town in Saudi Arabia. Near this place had the first store ill man - a wealthy businessman, who died two weeks after entering the hospital. He was the owner and 4 camels. Provide separate houses for his three wives and planned to take a fourth wife, suggesting that he was in good health. But most were infected with weakened immune systems or have chronic problems such as diabetes or cardiovascular disease. The virus does not spread easily from person to person, but there are already cases of illness of a family or people were in close contact.
According to participate in the study, Dr. Ziad Memish needed more tests on animals, and not just bats and camels, but also sheep, goats and cows.