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Human E. coli showed an increased resistance trend for ampicillin (0.59%/year, 95% CI 0.38%–0.81%; p<0.001), sulfonamide (0.49%/year, 95% CI 0.23%–0.73%; p<0.001), and tetracycline (0.45%/year, 95% CI 0.22%–0.70%; p<0.001), and this trend ranged during the study period from 0% to 66.7% for ampicillin, 0% to 50% for sulfonamide, and 0% to 58% for tetracycline. The resistance rate to ampicillin in animal E. coli isolates was similar to that in human isolates and ranged from 0% to 69.4%. In contrast, resistance rates for sulfonamide and tetracycline among animal E. coli isolates ranged from 0% to 73.7% and 0% to 85.5%, respectively, and were higher than those for human isolates. There was a linear increasing trend in resistance to ampicillin (0.97%/year, 95% CI 0.60%–1.33%; p<0.001), sulfonamide (1.11%/year, 95% CI 0.34%–1.85%; p<0.01), and tetracycline (0.7%/year, 95% CI 0.21%–1.21%; p<0.01)

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The bacterium Escherichia coli, commonly known as E. coli, has a duplicitous reputation. Scientists tell us that most strains of the microbe live peacefully in our guts or the guts of other mammals, munching on bits of food, causing no harm or even creating benefits for their hosts.

But the grotesque imagery of E. coli infections tells a different story: After eating food contaminated with pathogenic strains, people can experience vomiting, diarrhea, and dysentery. And in rare cases, the bacteria can lead to kidney failure and even death.

Ken Campellone, assistant professor of molecular and cell biology in the College of Liberal Arts and Sciences, wants to understand how these bacteria can play such different roles. By focusing on the interactions between one of the deadliest E. coli strains and the cells of the human gut, he's learning not only how the bacteria works, but how our own cells work, too.

Recently, Campellone discovered a particular protein in the cells of the human large intestine that is taken over by E. coli cells and helps to bind the bacterium to the intestinal wall.

"Pathogens have found really clever ways of taking over the normal processes of our cells," he says. "Often they know more about our own cells than we do, and it's really intriguing."

The strain of E. coli that Campellone studies belongs to a group of the bacteria called enterohemorrhagic E. coli, or EHEC, that often makes international news when people eat contaminated meat or vegetables. In 2011, an outbreak of a hemorrhagic strain in Germany infected more than 3,700 people, killing 45. The Centers for Disease Control and Prevention estimate that about 75,000 infections occur each year in the United States.

The reason for this high level of virulence, says Campellone, is a series of genetic acquisitions by the harmful bacteria. Scientists have sequenced several types of E. coli, and they've found more than 1,000 genes in the harmful group that are not present in the harmless, or commensal, group.

But, he adds, of the roughly 1,000 genes that have been identified as pathogenic, relatively few have been characterized.

"We know very little about the genes in EHEC that are different from the commensal version," he says. "My goal is to better understand how a group of genes that encode proteins called effectors take over their human cell targets."

In particular, the most dangerous types have acquired the genes to produce a poisonous substance called Shiga toxin, which Campellone says can produce an illness ranging from unpleasant to life-threatening.

"If the toxin is just released into your intestines, you would get diarrhea and dysentery," he says. "But if it enters your bloodstream, it can cause serious kidney damage and become fatal." Plus, he adds, there are currently no known medicines for the blood poisoning syndrome, and antibiotics only make the symptoms worse. Patients just have to wait and hope.

Campellone's research focuses on how the trafficking and organization of proteins control the shape of cells. When E. coli affix themselves to the intestinal wall, they disrupt its normal organization. They do this by delivering bacterial proteins into the cell, which in turn recruit specific intestinal cell proteins that normally shape the cell.

In 2004, Campellone was the first to identify a protein that the E. coli injects into the intestinal cells, causing the production of a fleshy bulge that lifts the attached bacteria away from the wall. Scientists call this lump a "pedestal" - because it really does look like one - but they still aren't sure what its purpose is.

Campellone also recently discovered a protein in human intestinal cells that interacts with the bacterial protein to help create the pedestal. He published these results in the June 2012 issue of The Journal of Biological Chemistry.

The discovery is significant because if a drug was developed that could block the pedestal from being produced, then the E. coli might not be able to stick to the intestinal wall, he explains. In that case, the bacteria might simply wash through a person's system, causing little harm.

In the classroom and in his laboratory, Campellone says these examples from his research give his students real-life examples of the information they learn about cell structure.

"When we teach cell biology, we show students that a lot of what we know about how human cells normally function is from studying infections," he says, pointing out that many cellular proteins have only been discovered in the context of pathogens trying to exploit them.

"Being able to ask scientific questions experimentally in the laboratory and then get an answer that could benefit people - that's the most exciting part for the students, and for me," he says. "You can be the first person in the world to know something."

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How E. coli Cells Work in the Human Gut - UConn Today

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The bacterium Escherichia coli, commonly known as E. coli, has a duplicitous reputation. Scientists tell us that most strains of the microbe live peacefully in our guts or the guts of other mammals, munching on bits of food, causing no harm or even creating benefits for their hosts.

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History of Adaptation of Escherichia coli

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What causes an E. coli intestinal infection?

You get an E. coli infection by coming into contact with the feces, or stool, of humans or animals. This can happen when you drink water or eat food that has been contaminated by feces.

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Researchers identify E. coli bacteria linking Crohn's disease to spondyloarthritis

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Patients with Crohn's disease, a type of inflammatory bowel disease (IBD) that causes abdominal pain and diarrhea, can also experience joint pain.

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For the general information here :

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Skip directly to search Skip directly to A to Z list Skip directly to navigation Skip directly to page options Skip directly to site content

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SCIENCE, CHRIS BICKEL The genetic code normally contains 64 codons, but researchers from Harvard University and their colleagues have designed an Escherichia coli genome with only 57 codons, replacing the others wholesale. In a paper published today (August 18) in Science, the team describes the computer-generated genome and reports on the first phases of its synthesis in the lab.

"We create something that really pushes the limit of genomes," study coauthor Nili Ostrov, a postdoc in George Church's lab at Harvard, told The Scientist. "The idea is that this is completely new, and we're trying to see if it's viable."

In the planned 57-codon E. coli genome, each of the seven deleted codons is exchanged for a synonymous one. The team has a number of goals for the project. Once the E. coli genome is pared down to 57 codons, the seven blank codons can be reintegrated and used to introduce nonstandard amino acids, the researchers have proposed; this would open the door to creating a wider range of proteins for industrial applications.

A recoded genome also imparts resistance to viral infection and can be used for biocontainment: the DNA incorporated from wild-type E. coli or viruses can't be used to build proteins successfully when transfer RNAs (tRNAs) insert a nonstandard amino acid in response to a given codon. One or more of the free codons could also be recoded to an amino acid only available in the lab, making the engineered E. coli metabolically dependent on scientist-supplied media.

"We put great care and thought into how to develop methods," said Ostrov, noting the safety and biocontainment concerns of the project. "What we're trying to do is chart uncharted waters."

To design the genome, the research team created a software tool that replaced every instance of the seven codons with a synonymous codon in a stretch of DNA that could be synthesized in a lab. In total, the recoded genome design had 62,214 codon replacements across 3,548 genes. "It's arguably the largest and most radical genome engineering project," Church told The Scientist.

With the theoretical genome in hand, Ostrov and colleagues began testing their design in living cells. They divided the recoded genome into 87 segments, each about 50 kb long-containing an average of 40 genes-and handed the design off to biotech companies to synthesize the DNA. The researchers then began integrating each segment into a separate strain of E. coli and deleting the corresponding wild-type DNA to check for viability.

"In principle you could do this whole-genome synthesis in vitro and then transplant the genome," said Church. Instead, his team developed a pipeline to obtain real-time feedback from living cells: "Assembly occurs with the motor running," he explained.

In their paper, the researchers review the results of this validation for 55 of the 87 genome segments, covering 63 percent of the recoded genome.The initial computational design for the recoded genome wasn't quite perfect: 13 essential genes had fatal errors that killed the E. coli when the wild-type DNA segment was deleted.

"We anticipated that there would be so-called synonymous or silent positions that aren't really synonymous or silent, where we'd overlap with regulatory elements or secondary structures," said Church. To resolve these errors, the researchers pinpointed each individual problematic codon and tested replacement-but still synonymous-sequences.

"It is a bit surprising to see how plastic the genome could be," Patrick Cai, a synthetic biologist at the University of Edinburgh who was not involved with the work, wrote in an email to The Scientist. "It is also very exciting to see [that] technologies such as computational design, de novo synthesis and assembly, as well as a range of phenotyping assays, are now mature to support genome refactoring at this scale."

The team must still finish validating the rest of the synthesized DNA segments and then combine them in vivo. "This is, of course, an exciting paper with clear advances," said Patrick O'Donoghue, a biochemist at Western University in Canada who was not involved with the work. O'Donoghue pointed out two key issues that represent future hurdles for the field: first, preventing the replacement codons from mutating back to the original genome state; second, if the codons are someday reintroduced with matching tRNAs to insert noncanonical amino acids, preventing the normal near-cognate tRNAs from translating them as well. "The strain that they're working towards will be useful, but there will clearly be some technological challenges," he added.

"The next paper, which hopefully will be soon, will be to polish off the genome and start testing for things like multivirus resistance, seeing how many amino acids we can load up, and confirming the biocontainment," said Church.

N. Ostrov et al., "Design, synthesis, and testing toward a 57-codon genome," Science, doi:10.1126/science.aaf3639, 2016.

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Streamlining the E. coli Genetic Code | The Scientist Magazine®

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SCIENCE, CHRIS BICKEL The genetic code normally contains 64 codons, but researchers from Harvard University and their colleagues have designed an Escherichia coli genome with only 57 codons, replacing the others wholesale. In a paper published today (August 18) in Science, the team describes the computer-generated genome and reports on the first phases of its synthesis in the lab.

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First discussion among our group members

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http://popplet.com/app/#/3911423

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https://www.youtube.com/watch?v=Q1LxcMA7tEI&t=23s

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Hope ur guys can look inside it

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Identification of E-coli from other microorganisms

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Identification of E-coli from other microorganisms

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Okay guys,first and foremost, lets decide on the scrapbook that we want to do about the E.coli.this is the list of the scrapbook avalable..please do choose and suggest  one.

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https://medlineplus.gov/ecoliinfections.html
. coli is the name of a type of bacteria that lives in your intestines. Most types of E. coli are harmless. However, some types can make you sick and cause diarrhea. One type causes travelers' diarrhea. The worst type of E. coli causes bloody diarrhea, and can sometimes cause kidney failure and even death. These problems are most likely to occur in children and in adults with weak immune systems.

You can get E. coli infections by eating foods containing the bacteria. Symptoms of infection include

Nausea or vomiting

Severe abdominal cramps

Watery or very bloody diarrhea

Fatigue

Fever

To help avoid food poisoning and prevent infection, handle food safely. Cook meat well, wash fruits and vegetables before eating or cooking them, and avoid unpasteurized milk and juices. You can also get the infection by swallowing water in a swimming pool contaminated with human waste.
Most cases of E. coli infection get better without treatment in 5 to 10 days.