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    Thursday, 17 October 2013 17:07

    Staphylococcus aureus resistance unraveled

    Staphylococcus lugdunensis Z097New research findings on the mechanism and the ways in which methicillin-resistant golden staph (MRZS) becomes so difficult pathogen during the last 50 years.
     
    MRZS unaffected by atibiotitsite, including beta-lactam antibiotic drugs such as penicillin.
     
    Experts reveal allosteric center in the X-ray structure of penicillin binding protein 2a of MRZS. Allosteric center is a site of the protein, where its activity is regulated by its binding to another molecule.

    Scientists have documented that allosteric reaction is triggered by a fragment of the cell wall at a distance of 6 nanometers and activates a number of structural changes that culminate in the opening of the active side of the closed structure, allowing catalyzing enzyme.

    They also documented that the new beta- lactam antibiotic ceftaroline, which was recently approved by the Administration Food and Drug Administration in the U.S., you can contact center and allosteric trigger " allosteric opening " the active side.
     
    Thus allowing another molecule ceftaroline to enter and activate the center . This prevents the function of the enzyme and results in the destruction of MRZS . This mechanism of action of the antibiotic is unprecedented and provides many important ideas for future work on drugs to combat methicillin-resistant Staphylococcus aureus .

    Gentaur's Staphylococcus products:

    Staphylococcus simulans Z032, titered (1 mL)

    Staphylococcus lugdunensis Z097, titered (1 mL)

    Thursday, 17 October 2013 12:35

    Avian Influenza Virus Detection Using Smell

    influenza-virus-gentaur-antibodiesNew research from the Monell Chemical Senses Center and the U.S. Department of Agriculture (USDA) reveals how diseases can modify animal odors in subtle ways. In a recent study published in the public access journal PLOS ONE, scientists examined how infection with avian influenza (AIV) alters fecal odors in mallards.

    Using both behavioral and chemical methods, the findings reveal that AIV can be detected based on odor changes in infected birds.

    "The fact that a distinctive fecal odor is emitted from infected ducks suggests that avian influenza infection in mallards may be 'advertised' to other members of the population," notes Bruce Kimball, PhD, a research chemist with the USDA National Wildlife Research Center (NWRC) stationed at the Monell Center. "Whether this chemical communication benefits non-infected birds by warning them to stay away from sick ducks or if it benefits the pathogen by increasing the attractiveness of the infected individual to other birds, is unknown."

    In the study, laboratory mice were trained to discriminate between feces from AIV-infected and non-infected ducks, indicating a change in odor. Chemical analysis then identified the chemical compounds associated with the odor changes as acetoin and 1-octen-3-ol.

    The same compounds also have been identified as potential biomarkers for diagnosing gastrointestinal diseases in humans. Kimball and colleagues hypothesize that metabolites resulting from viral infection interact in concert with bacteria in the gastro-intestinal system of ducks to produce "odor signatures" indicating presence of the AI virus.

    "Avian influenzas are typically asymptomatic in ducks and waterfowl. Infection in these species can only be diagnosed by directly detecting the virus, requiring capture of birds and collection of swab samples. Our results suggest that rapid and simple detection of influenzas in waterfowl populations may be possible through exploiting this odor change phenomenon," said Monell behavioral biologist Gary Beauchamp, PhD, also an author on the paper.

    Future work will assess whether odor changes can be used for surveillance of AIV in waterfowl. In particular, researchers are interested in whether the odor change is specific to the AIV pathogen or if it is merely a general response to a variety of pathogens normally found in birds. Other studies will explore communicative functions of the AIV odor to gain greater understanding of how odors can shape social behavior in wildlife populations.

    Also contributing to the research, which was funded by the National Wildlife Research Center, were Kunio Yamazaki and Maryanne Opiekun of Monell and Richard Bowen and Jack Muth from Colorado State University. Dr. Yamazaki, who actively contributed to the design and realization of this work, died in April 2103.

    pandoravirus-cells-antibodies-gentaurWith the discovery of Mimivirus ten years ago and, more recently, Megavirus chilensis, researchers thought they had reached the farthest corners of the viral world in terms of size and genetic complexity. With a diameter in the region of a micrometer and a genome incorporating more than 1,100 genes, these giant viruses, which infect amoebas of the Acanthamoeba genus, had already largely encroached on areas previously thought to be the exclusive domain of bacteria. For the sake of comparison, common viruses such as the influenza or AIDS viruses only contain around ten genes each.

    In the article published in Science, the researchers announced they had discovered two new giant viruses:

    • - Pandoravirus salinus, on the coast of Chile;
    • - Pandoravirus dulcis, in a freshwater pond in Melbourne, Australia.

     

    Detailed analysis has shown that these first two Pandoraviruses have virtually nothing in common with previously characterized giant viruses. What's more, only a very small percentage (6%) of proteins encoded byPandoravirus salinus are similar to those already identified in other viruses or cellular organisms. With a genome of this size,Pandoravirus salinus has just demonstrated that viruses can be more complex than some eukaryotic cells. Another unusual feature of Pandoraviruses is that they have no gene allowing them to build a protein like the capsid protein, which is the basic building block of traditional viruses.

    Despite all these novel properties, Pandoraviruses display the essential characteristics of other viruses in that they contain no ribosome, produce no energy and do not divide.

    This groundbreaking research included an analysis of thePandoravirus salinus proteome, which proved that the proteins making it up are consistent with those predicted by the virus' genome sequence. Pandoraviruses thus use the universal genetic code shared by all living organisms on the planet.

    This shows just how much more there is to learn regarding microscopic biodiversity as soon as new environments are considered. The simultaneous discovery of two specimens of this new virus family in sediments located 15,000 km apart indicates that Pandoraviruses, which were completely unknown until now, are very likely not rare.

    It definitively bridges the gap between viruses and cells -- a gap that was proclaimed as dogma at the very outset of modern virology back in the 1950s.

    It also suggests that cell life could have emerged with a far greater variety of pre-cellular forms than those conventionally considered, as the new giant virus has almost no equivalent among the three recognized domains of cellular life, namely eukaryota (or eukaryotes), eubacteria, and archaea.

    naked mole ratNaked mole rats have what any animal would want. They live long lives—about 30 years—and stay healthy until the very end. Now biologists at the University of Rochester have new insights into the animal's longevity—better-constructed proteins.

    Proteins are involved in nearly all functions of an animal cell, and consequently, are essential to all organisms. But before proteins can do their job, they must fold into the appropriate shapes that allow them to connect to and interact with other structures in the cell. In a paper published this week in the Proceedings of the National Academy of Sciences, Vera Gorbunova and Andrei Seluanov describe their discovery of the process in naked mole rats that leads to virtually perfect proteins.

    "While this is basic research," said Gorbunova, "we hope our findings encourage further studies on better protein synthesis."

    Their work focused on naked mole rat ribosomes—the site of protein creation in the animal's cells—and began by happenstance. Gorbunova and Seluanov were working with ribosome RNA (rRNA) when they made a discovery. After applying a dye to a sample, they studied it under ultraviolet light only to find three dark bands—representing concentrations of different rRNA molecules—not the two bands that are characteristic of all other animals, suggesting that there is a "hidden break" in the naked mole rat rRNA. Since rRNA is an essential part of the protein-creation mechanism, the two biologists decided to see if the broken rRNA affects the quality of naked mole rat proteins.

    Ribosome RNA strands act as scaffolds on the ribosome, a protein synthesis machine. Changing the shape of the scaffold can have a profound effect on the organization of the ribosome parts.

    Gorbunova and Seluanov discovered that the naked mole rat's rRNA scaffold is indeed unique. The rRNA strands split at two specific locations and discard the intervening segment. Instead of floating off on their own, the two remaining pieces from each strand stay close to each other and act as a scaffold on which ribosomal proteins are assembled to create a functional ribosome—a molecular machine that puts amino acids together to create proteins. And the results are impressive.

    When the ribosome connects amino acids together to create a protein a mistake is occasionally introduced when an incorrect amino acid is inserted. Gorbunova and Seluanov found that the proteins made by naked mole rat cells are up to 40 times less likely to contain such mistakes than the proteins made by mouse cells.

    "This is important because proteins with no aberrations help the body to function more efficiently," said Seluanov.

    The next step for the biologists is to split mouse rRNA in the same way to see if it would lead to improved protein creation.

    The two biologists hope their work will eventually result in pharmaceutical treatments that modulate protein synthesis in humans, though any medical solution is a long way off.

    smoking-formation-embryoid-body-formation-snl-feeder-pluripotency-marker-cf-1-geneThe world's first vaccine against smoking has been developed by the company "Selecta (RUS)." Expected in 2018 they arrived at pharmacies, said the site "newsru."

    According to Russian scientists, a subsidiary of the large U.S. holding company, it is a means of stimulating the production of antibodies that block nicotine in the blood. To provoke an immune response against the tobacco.

    As a result, a person stops experiencing a pleasant sensation of smoking (nicotine can affect the brain).

    Thus no point in smoking and it is easy to grips with the psychological addiction.

    According to statistics from the World Health Organization (WHO) each year smoking kills about 4 million people.

    People do not quit smoking despite injury information on nicotine for smoking bans in public places in many countries and tax increases.

    Same group of Russian scientists now developing vaccines against diabetes, hepatitis B and skin cancer.

    Meanwhile, a new study of New Zealand scientists shows that smokers are switching to electronic cigarettes to quit the habit have the same chance of success as those using nicotine patches , reported the Associated Press and Reuters .

    The first-ever study comparing the efficacy of electronic cigarettes with nicotine patches as standard therapy for smoking.

    Scientists from the University of Auckland found that the achievement levels are similar, it is more likely that electronic cigarettes to help their users do to reduce the amount of tobacco you smoke. Moreover, people go to much greater willingness of electronic cigarettes than nicotine patches .

    A University of Colorado Cancer Center study published today in the journal Cancershows that the current criteria used to match lung cancers with the drug crizotinib may miss some patients who could benefit from the drug. The findings suggest that doctors should look closer at borderline or atypical ALK-negative cases, and could widen the population of lung cancer patients offered treatment with crizotinib or other ALK-inhibitor drugs.

    ALK stands for anaplastic lymphoma kinase, a gene that is turned off in most adult tissues in the body, but which can be re-activated to cause cancer when it is fused with another nearby gene. The original and still most widely-used test for ALK-positive lung cancer was co-developed by Leila Garcia, PhD, director of the Cytogenetics Core Resource at the University of Colorado Cancer Center. The test uses the technique known as fluorescence in situ hybridization (FISH) to test for the fusion of the ALK gene with another gene that turns ALK back on, allowing it to drive some lung cancers. When a cancer is ALK positive it can be very effectively treated with crizotinib, a targeted anti-ALK drug.

    "The test is fairly definitive -- either a cell is ALK positive or not using the criteria we initially implemented. However, what is less certain is the exact percentage of ALK-positive cells required to label an entire tumor as ALK-positive. Is there an exact threshold of ALK-positive cells that will make a patient respond to crizotinib or other ALK inhibitors?" Garcia says.

    "Since the beginning we have looked at the cells in a tumor and if 15 percent or more of these cells show the changes classically associated with an ALK rearrangement, we classify that tumor as ALK-positive and offer treatment with crizotinib," says Ross Camidge, MD, PhD, investigator at the CU Cancer Center and director of the thoracic oncology clinical program at University of Colorado Hospital.

    Previous studies indicated that this 15-percent point fell in a clear gap between tumors that were obviously ALK-positive and tumors that were obviously ALK-negative, making it an attractive threshold.

    "But what this study shows is that when you look not at tens, but hundreds of cases, tumors clearly exist that come right up to the 15-percent cutoff point," Camidge says.

    Another possible gray area is when a gene rearrangement occurs but is very complex -- like shuffling cards rather than just cutting the deck. In this situation the typical separated dot pattern indicative of ALK rearrangement may not be present, but instead doublets or triplets of single or un-separated dots may exist. This atypical cellular footprint can tell an expert that, while officially ALK-negative, the cancer has made some changes in the region of the ALK gene that could still make the cancer sensitive to ALK-inhibitor drugs.

    "We believe these data suggest that such borderline and atypical negative cases deserve a closer look, perhaps with new kinds of diagnostic tests," Says Camidge.

    The current study tested 1426 samples of non-small cell lung cancer, which included 174 officially positive for an ALK rearrangement and 1252 that were officially negative. Of the ALK-negative tumors, 121 had greater than 10 percent ALK-positivity, but were still below the 15 percent needed to classify the overall tumor as ALK-positive. This means that 8.5 percent of non-small cell lung cancers were "borderline" negative. In the study, 1-2 percent also showed atypical-negative patterns, a group that may also benefit from a closer re-evaluation of their ALK status.

    Early in 2013, serendipity provided a chance to test whether at least one of the Colorado team's hypotheses were correct. In a case described in an upcoming article in the Journal of Thoracic Oncology, Dr. Shengxiang Ren from the Shanghai Pulmonary Hospital describes a patient who traveled halfway across the world for a second opinion at the University of Colorado, where much of the research leading to ALK-targeted drugs has taken place.

    "We were thrilled this patient had sought out an opinion from one of the leading centers in lung cancer and could not have been happier with the collaboration that developed," Ren says.

    The patient was originally classified ALK-negative using the standard FISH assay. However, Dr. Garcia recognized that an atypical negative pattern was present. One way of looking closer at ALK uses the technique of immunohistochemistry (IHC), which looks directly for the protein the aberrant ALK gene creates. Using an IHC assay for ALK conducted within the laboratory of Fred R. Hirsch, MD, PhD, associate director for international programs at the CU Cancer Center, the team quickly confirmed that the patient's tumor was making the ALK protein and should really be considered ALK-positive. Another test called RT-PCR conducted in Shanghai on the same specimen looked at the ALK gene in a third way, confirming the presence of messages coming from the gene that were telling the cell to make the abnormal protein.

    "Amazingly, crizotinib was being licensed in China the following week and so we simply wrote the patient a prescription and sent him back to Dr. Ren in Shanghai, where his latest scans show he is responding beautifully to the drug," Camidge says. "All of the early work on ALK positive lung cancer has really helped to clarify what can be achieved by personalized medicine, but we have to keep pushing the envelope to maximize this approach in routine cancer care. For ALK-positive lung cancer, basically our goal now is to make sure that everyone who could benefit from an ALK inhibitor gets an ALK inhibitor."

    The CU Cancer Center's Thoracic Oncology Program is world renowned for its pioneering treatment of lung cancer. The program includes a multidisciplinary team of specialists and subspecialists working together to establish the best treatment plan for each patient. Advanced molecular profiling of a patient's tumor, combined with an extensive array of standard and experimental treatments available through clinical trials has led to major advances in patient outcomes in the last few years.

    The program's one-year survival rates for advanced lung cancer consistently run twice as high as the national average. The survival rates at five years run four times higher than the national average. Additionally, the Center's new Remote Second Opinion Program now offers access to program experts for patients who prefer not to travel.

    According to researchers, they prevent the growth of cancer cells

    images-targatt-culture-pcr-knockin-mouse-targatt-knockin-rat-pcr-premix-knockout-mouse-mice

    A new type of therapy can help to effectively treat breast cancer, reported biologists from the University of Aberdeen. It's about the application of the specific type of antibody IgNAR (immunoglobulin new antigen receptor), which are found in cartilage fish - such as sharks. According to researchers unique antibody can prevent the growth of cancer cells.

    Over the next three years is to provide a number of studies that confirm the theory and help to create a cure for the most common malignancy in women location. Scientists will focus on the two molecules - HER2 and HER3, which are arranged on the surface of cancer cells. When these molecules are combined, the cancer cells receive signals for growth and division. According to researchers IgNAR can stop the transmission of the signal and to prevent progression of the disease.

    cf-1-gene-knock-in-technology-ipscAt Tokuda Hospital in Sofia was presented the latest genetic testing in prenatal diagnosis.
     
    Latest biomedical innovation in prenatal care for expectant mothers called Prenatest. This is the first non-invasive prenatal test in Bulgaria. Unlike other Prenatal tests Prenatest analyze the DNA of the fetus without the manipulation of the body of the mother and fetus.

    The study gives as early safest information about the most common forms of chromosomal abnormalities in the fetus: trisomy 21, 18 and 13 - Down syndrome, Edwards syndrome and Patau syndrome. Subjecting Prenatest can be done by the 9th week of gestation and accuracy of the results is 99%.

    Europe territory test is licensed by the German company Layfkodeks. He carries CE mark, making it the only certified genetic testing of third generation - non-invasive prenatal test within the European Union.
     
    Breaking study was developed based on the discovery that the blood of a pregnant woman circulating DNA of the baby. This DNA is extracellular or free. Test its patented technology that isolated from maternal blood free fetal DNA and makes it possible for her research. Blood samples were transported to the laboratory Layfkodeks in Germany, where it is subjected to high-tech genetic analysis.

    madetoorderaProtein synthesis in the extensions of nerve cells, called dendrites, underlies long-term memory formation in the brain, among other functions. "Thousands of messenger RNAs reside in dendrites, yet the dynamics of how multiple dendrite messenger RNAs translate into their final proteins remain elusive," says James Eberwine, PhD, professor of Pharmacology, Perelman School of Medicine at the University of Pennsylvania, and co-director of the Penn Genome Frontiers Institute.
    Dendrites, which branch from the cell body of the neuron, play a key role in the communication between cells of the nervous system, allowing for many neurons to connect with each other. Dendrites detect the electrical and chemical signals transmitted to the neuron by the axons of other neurons. The synapse is the neuronal structure where this chemical connection is formed, and investigators surmise that it is here where learning and memory occur.
    Previous studies in the Eberwine lab have shown that translation of messenger RNAs (mRNAs) into proteins occurs in dendrites at focal points called translational hotspots. Local protein synthesis in dendrites, not in the cell body of nerves, provides the ability to respond rapidly and selectively to external stimuli. This ability is especially important in neurons that have highly polarized cell morphology, meaning one end of the cell has a very different shape from the other end.
    In dendrites and axons these rapid structural and functional changes occur concurrently – their length, size, shape, and number change to suit the needs of neuronal cell body communication.
    These structural and chemical changes – called synaptic plasticity—require rapid, new synthesis of proteins. Cells may use different rates of translation in different types of mRNA to produce the right amounts and ratios of required proteins.
    Knowing how proteins are made to order – as it were - at the synapse can help researchers better understand how memories are made. Nevertheless, the role of this "local" environment in regulating which messenger RNAs are translated into proteins in a neuron's periphery is still a mystery.
    Eberwine, first author Tae Kyung Kim, PhD, a postdoc in the Eberwine lab, and colleagues including Jai Yoon Sul, PhD, assistant professor in Pharmacology, showed that protein translation of two dendrite mRNAs is complex in space and time, as reported online in Cell Reports this week.
    "We needed to look at more than one RNA at the same time to get a better handle on real- world processes, and this is the first study to do that in a live neuron," Eberwine explains.
    At Home in the Hippocampus
    The team looked at two RNAs that make proteins that bind to glutamate, the dominant neurotransmitter in the brain. Using rat hippocampus neurons the researchers found a heterogeneous distribution of translational hotspots along dendrites for the two mRNAs.
    This finding indicates that RNA translation is dictated by translational hotspots, not solely when RNA is present. A translational hot spot is characterized by where translation is occurring in a ribosome at any one time in a discrete spot. Since hotspots are not uniform, understanding individual hotspot dynamics is important to understanding learning and memory.
    "It's not always one particular RNA that dominates at a translation hotspot versus another type of RNA," says Eberwine. "Since there are 1,000 to 3,000 different mRNA types present in the dendrite overall, but not 1,000 to 3,000 different translational hot spots, do the mRNAs 'take turns' being translated in space and time at the ribosomes at the hotspots?"
    The researchers engineered the glutamate receptor RNAs to contain different fluorescent proteins that are independently detectable, as well as a photo-switchable protein to determine when new proteins were being made. In the case of the photo-switchable protein studies, when an mRNA for the glutamate receptor protein is marked green, it means it has already been translated.
    When a laser is passed over the green protein, it changes to red as a way of tagging when it has been been translated, and new proteins synthesized at that hotspot would be green, which is visible by the appearance of yellow fluorescence (green + red, as measured by light on the visible spectrum). These tricks of the light allow the team to keep track of newly made proteins over time and space.
    "This is the first time this method of protein labeling has been used to measure the act of translation of multiple proteins over space and time in a quantitative way," says Eberwine. "We call it quantitative functional genomics of live cell translation."
    "Our results suggest that the location of the translational hotspot is a regulator of the simultaneous translation of multiple messenger RNAs in nerve cell dendrites and therefore synaptic plasticity," says Sul.
    Laying the Groundwork
    Almost 10 years ago, the Eberwine lab discovered that nerve-cell dendrites have the capacity to splice messenger RNA, a process once believed to take place only in the nucleus of cells. Here, a gene is copied into mRNA, which possesses both exons (mature mRNA regions that code for proteins) and introns (non-coding regions). mRNA splicing works by cutting out introns and merging the remaining exon pieces, resulting in an mRNA capable of being translated into a specific protein.
    The vast array of proteins within the human body arises in part from the many ways that mRNAs can be spliced and reconnected. Specifically, splicing removes pieces of intron and exon regions from the RNA. The resulting spliced RNA is made into protein.
    If the RNA has different exons spliced in and out of it, then different proteins can be made from this RNA. The Eberwine lab was successful in showing that splicing can occur in dendrites because they used sensitive technologies developed in their lab, which permits them to detect and quantify RNA splicing, as well as the translated protein in single isolated dendrites.
    Understanding the dynamics of RNA biology and protein translation in dendrites promises to provide insight into regulatory mechanisms that may be modulated for therapeutic purposes in neurological and psychiatric illnesses. The directed development of therapeutics requires this detailed knowledge, says Eberwine.

    ahiddengenetScientists routinely seek to reprogram bacteria to produce proteins for drugs, biofuels and more, but they have struggled to get those bugs to follow orders. But a hidden feature of the genetic code, it turns out, could get bugs with the program. The feature controls how much of the desired protein bacteria produce, a team from the Wyss Institute for Biologically Inspired Engineering at Harvard University reported in the September 26 online issue of Science.
    The findings could be a boon for biotechnologists, and they could help synthetic biologists reprogram bacteria to make new drugs and biological devices.
    By combining high-speed "next-generation" DNA sequencing and DNA synthesis technologies, Sri Kosuri, Ph.D., a Wyss Institute staff scientist, George Church, Ph.D., a core faculty member at the Wyss Institute and professor of genetics at Harvard Medical School, and Daniel Goodman, a Wyss Institute graduate research fellow, found that using more rare words, or codons, near the start of a gene removes roadblocks to protein production.
    "Now that we understand how rare codons control gene expression, we can better predict how to synthesize genes that make enzymes, drugs, or whatever you want to make in a cell," Kosuri said.
    To produce a protein, a cell must first make working copies of the gene encoding it. These copies, called messenger RNA (mRNA), consist of a specific string of words, or codons. Each codon represents one of the 20 different amino acids that cells use to assemble proteins. But since the cell uses 61 codons to represent 20 amino acids, many codons have synonyms that represent the same amino acid.
    In bacteria, as in books, some words are used more often than others, and molecular biologists have noticed over the last few years that rare codons appear more frequently near the start of a gene. What's more, genes whose opening sequences have more rare codons produce more protein than genes whose opening sequences do not.
    No one knew for sure why rare codons had these effects, but many biologists suspected that they function as a highway on-ramp for ribosomes, the molecular machines that build proteins. According to this idea, called the codon ramp hypothesis, ribosomes wait on the on-ramp, then accelerate slowly along the mRNA highway, allowing the cell to make proteins with all deliberate speed. But without the on-ramp, the ribosomes gun it down the mRNA highway, then collide like bumper cars, causing traffic accidents that slow protein production. Other biologists suspected rare codons acted via different mechanisms. These include mRNA folding, which could create roadblocks for ribosomes that block the highway and slow protein production.
    To see which ideas were correct, the three researchers used a high-speed, multiplexed method that they'd reported in August in The Proceedings of the National Academy of Sciences.
    First, they tested how well rare codons activated genes by mass-producing 14,000 snippets of DNA with either common or rare codons; splicing them near the start of a gene that makes cells glow green, and inserting each of those hybrid genes into different bacteria. Then they grew those bugs, sorted them into bins based on how intensely they glowed, and sequenced the snippets to look for rare codons.
    They found that genes that opened with rare codons consistently made more protein, and a single codon change could spur cells to make 60 times more protein.
    "That's a big deal for the cell, especially if you want to pump out a lot of the protein you're making," Goodman said.
    The results were also consistent with the codon-ramp hypothesis, which predicts that rare codons themselves, rather than folded mRNA, slow protein production. But the researchers also found that the more mRNA folded, the less of the corresponding protein it produced—a result that undermined the hypothesis.
    To put the hypothesis to a definitive test, the Wyss team made and tested more than 14,000 mRNAs – including some with rare codons that didn't fold well, and others that folded well but had no rare codons. By quickly measuring protein production from each mRNA and analyzing the results statistically, they could separate the two effects.
    The results showed clearly that RNA folding, not rare codons, controlled protein production, and that scientists can increase protein production by altering folding, Goodman said.
    The new method could help resolve other thorny debates in molecular biology. "The combination of high-throughput synthesis and next-gen sequencing allows us to answer big, complicated questions that were previously impossible to tease apart," Church said.
    "These findings on codon use could help scientists engineer bacteria more precisely than ever before, which is tremendous in itself, and they provide a way to greatly increase the efficiency of microbial manufacturing, which could have huge commercial value as well," said Wyss Institute Founding Director Don Ingber, M.D., Ph.D. "They also underscore the incredible value of the new automated technologies that have emerged from the Synthetic Biology Platform that George leads, which enable us to synthesize and analyze genes more rapidly than ever before."