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Researchers say they’ve found that people with atopic dermatitis i.e. eczema, are susceptible to bacterial infections in their skin because their bodies don’t produce enough of two antimicrobial peptides. The findings show that while an allergic reaction can cause a rash, true eczema is all about infection. And medicines containing or inducing the peptides could be used to fight the disorder, which affects millions worldwide.

Eczma patient Lack Natural Antibiotic in Skin
Researchers at National Jewish Medical and Research Center report in the October 10 issue of the New England Journal of Medicine that patients with atopic dermatitis, also known as eczema, are susceptible to bacterial infections of their skin because they fail to produce effective amounts of two antimicrobial peptides. The findings demonstrate for the first time the clinical significance of these peptides in humans, and suggest that a medication containing or inducing the peptides may one day be used to fight the infections that plague millions of atopic dermatitis patients. The accompanying editorial in the journal called it a “seminal study.”

“This study helps explain why 90 percent of atopic dermatitis patients are colonized by staphylococcus aureus and 30 percent develop active infections,” said the study’s senior author, Donald Leung, M.D., Ph.D., Head of Pediatric Allergy-Immunology at National Jewish Medical and Research Center, in Denver. “It is important to understand why people with this common skin disease are so susceptible to skin infections, especially in light of recent widespread concerns that they can develop severe infections after receiving a smallpox vaccination. Interestingly, these antimicrobial peptides are also needed to combat viral infections and therefore could account for the susceptibility of atopic dermatitis patients to eczema vaccinatum and herpes simplex infections.”

Atopic dermatitis is a common, chronic skin disease characterized by dry, itchy and easily irritated skin. It occurs most commonly in infants and young children, but can persist into adulthood. Severe cases can lead to sleep deprivation, chronic bacterial infections, and depression. Approximately one in nine people in the United States suffer from this disease at some point. Along with other allergic diseases, its prevalence has grown significantly in recent years.

Immunologists recently identified peptides in the skin that help fight incipient infections. They rarely appear in normal skin, but are produced in reaction to skin inflammation. Since atopic dermatitis patients are so frequently plagued by bacterial infections, Dr. Leung and his colleagues decided to investigate the potential role of the antimicrobial peptides in those patients.

They evaluated the levels of two antimicrobial peptides, known as LL-37 and HBD-2, in eight patients with moderate to severe atopic dermatitis, 11 psoriasis patients, and six healthy individuals. Psoriasis is an inflammatory skin disease, whose patients rarely suffer skin infections. Microscopic examination of skin samples showed significant amounts of the peptides in the skin of psoriasis patients, but none to minor amounts in skin from atopic dermatitis patients, and none in the skin of healthy controls. Additional analysis indicated that most psoriasis patients had at least 10 times as much of the peptides in their skin as did atopic dermatitis patients. Many atopic dermatitis patients had no detectable amounts of the antimicrobial peptides in their skin.

When the researchers treated staphylococcus aureus colonies with the antimicrobial peptides, levels found in skin of psoriasis patients killed the bacteria. The researchers also found that two hormone-like proteins associated with the immune response and commonly secreted by atopic dermatitis patients’ cells, IL-4 and IL-13, suppressed the production of HBD-2 in cell cultures.

“These findings indicate that atopic dermatitis patients have an impaired immune response that prevents them from producing adequate amounts of antimicrobial peptides in their skin,” said Dr. Leung.

The research suggests that the missing peptides might one day be used as a treatment to prevent skin infections in atopic dermatitis patients.

“Our body normally makes these peptides to fight infections, so there might be fewer side effects than with conventional antibiotics,” said co-author Richard Gallo, M.D., Ph.D., Chief of Dermatology at the Veterans Affairs San Diego Healthcare System and Associate Professor of Medicine at the University of California, San Diego. In 1994, Dr. Gallo was the first to discover the antimicrobial peptides in mammalian skin. The peptides might have another advantage over conventional antibiotics, said Dr. Gallo. While conventional antibiotics attack only bacteria, the antimicrobial peptides fight bacteria, viruses and fungi.

Researchers will also be working in the next several years to alter the immune response of atopic dermatitis patients to promote the production of the antimicrobial peptides, said Dr. Leung.

The findings could shed light on atopic dermatitis patients’ susceptibility to eczema vaccinatum, a widespread skin infection that can afflict those who receive the smallpox vaccination. They may have relevance for other diseases, as well. For instance, it is known that tuberculosis and leprosy patients, whose cells secrete the same immune system regulators as atopic dermatitis patients, are more likely to have disease that spreads widely in their bodies.

Peptides previously isolated from hybrid striped bass may be able to control certain viral diseases in fish and humans, suggests new research published in the journal Virology. ”The peptides were highly inhibitory to channel catfish virus, as well as certain amphibian viruses,” said Ed Noga, a co-investigator and North Carolina Sea Grant researcher. The study was led by Greg Chinchar of the University of Mississippi Medical Center.

Peptides Antibiotics From Fish May Fight Viral Diseases, Sea Grant StudyFinds
Peptides previously isolated from hybrid striped bass may be able to control certain viral diseases in fish and humans, suggests new research published in the journal Virology. ”The peptides were highly inhibitory to channel catfish virus, as well as certain amphibian viruses,” said Ed Noga, a co-investigator and North Carolina Sea Grant researcher. The study was led by Greg Chinchar of the University of Mississippi Medical Center.

The peptide antibiotics or ”piscidins,” a name derived from pisces, the Latin word for fish, originally were isolated from mast cells — found in the immune systems of fish and other vertebrates, including humans. ”The results suggest that piscidins may be an important defense for fish against viral infections, which are among the most serious diseases in aquaculture,” added Noga. ”They also have the potential to fight viral infections in humans, particularly the herpes viruses.” Earlier work by other researchers found that viruses can be sensitive to other types of antimicrobial peptides besides piscidins, according to Noga. With the spread of emerging infectious diseases and the growing problem of antibiotic resistance, the search for effective treatments has taken on greater urgency.

In a previous North Carolina Sea Grant study, researchers found that piscidins possessed potent broad-spectrum antibacterial activity, including the ability to fight fish and human pathogens resistant to other antibiotics. This was the first time that researchers had isolated a peptide antibiotic from mast cells of any animals. ”The next step is to determine the specific role that piscidins play in defending fish against viral infections, as well as finding out if piscidins can effectively treat viral disease in an animal model,” Noga said. The study was funded by North Carolina Sea Grant, the National Science Foundation, and the U.S. Department of Agriculture.

Here is a load of crap, pajamas that is designed to protect against MRSA by incorporating silver into its fabric at a level of 2%.

They claim that by having 2% silver woven into its fabric, it can protect against the hospital super bug MRSA. It has already gone on sale UK with M&S the first British retailer to stock the £45 Sleep Safe pajamas and is trialing them at 100 stores.

Silver is known for its infection-fighting properties and silver-laced nightwear has already been tested in a handful of hospitals.

But campaigners called the pajamas a gimmick and said the only way to tackle MRSA was by making hospitals cleaner.

MRSA

MRSA (methicillin resistant Staphylococcus aureus) is a bacterium that can live completely harmlessly on the skin of healthy people but can lead to serious infection.

MRSA infections can cause a broad range of symptoms depending on the part of the body that is infected. These may include surgical wounds, burns, catheter sites, eye, skin and blood.

Dr Mark Enright, a microbiologist at Imperial College London, said that the pajamas would reduce the risk of a patient getting a skin infection that enters a wound.

The problem lies within the hospitals. They are dirty and it should not be up to the public to safeguard themselves

Tony Kitchen of MRSA Support

A spokesman for M&S said: “The fabric that the pajamas are made of has been clinically proven to reduce the risk of MRSA by killing bacteria that come into contact with the fabric.

“Clinical trials are currently ongoing and are three quarters of the way through. The interim results were positive.”

They are only available for men at present and are produced using a fabric which 2% silver has woven into it.

Katherine Murphy, from the Patients’ Association, said: “We welcome the fact these are going on sale, but it shows how desperate the public is.”

However, Tony Kitchen of MRSA Support said: “It sounds like a gimmick - it cannot be a super suit and probably doesn’t make a jot of difference.

“The problem lies within the hospitals. They are dirty and it should not be up to the public to safeguard themselves, it’s the ethos of the hospital that needs to change.”

A spokesman added that if the pajamas did prove effective then they ought to be provided by the health service. rather than paid for by the patient.

Streptococcus throat has become harder to fight using penicillin or amoxicillin, but that’s not because the Streptococci have developed a resistance to those drugs. Instead, more than 50 percent of children have bacteria in their throats that protect strep germs.

New versions of antibiotics called cephalosporins are targeting the other bacteria, improving the odds of successful treatment fivefold.

Strep throat is the second-most-common reason children get antibiotics. But the gold standard antibiotics they get don’t always clear up the infection.

Pediatric infectious disease specialist Michael Pichichero, of the University of Rochester Medical Center in New York, says, says the standard strep drugs — amoxicillin and penicillin — fail in about 25 percent of kids.

“Strep is not actually resistant to penicillin or amoxicillin so, that cannot explain the failures that we’re seeing,” he says.

Instead, other bacteria are the problem. More than half of kids have bacteria in their throats that protect strep germs.

Dr. Pichichero says, “This is very much different from 20 or 30 years ago where almost all children treated with penicillin and amoxicillin would be cured.”

But his research shows newer drugs can kill strep. One in four kids fails treatment with penicillin. One in six fails newer drugs called cephalosporins. Only one in 20 fail the newer versions of those drugs. The newer antibiotics only need to be taken for four to five days, rather than the 10-day course of the older drugs.

BACKGROUND:
Researchers at the University of Rochester Medical Center have found that a short treatment of a newer class of antibiotics is more effective than the traditional 10-day dose of older antibiotics like penicillin and amoxicillin to treat strep throat. The Rochester scientists reviewed over 47 studies over the past 35 years involving more than 11,000 children and found that 25 percent of children treated for strep throat with penicillin ended up back in the doctor’s office within three weeks.

HOW ANTIBIOTICS WORK:
Infections are caused by single-celled organisms called bacteria, which can sometimes evade the body’s immune system and begin reproducing.

Antibiotics kill those harmful bacteria in various ways, such as preventing a bacterium from turning glucose into energy, or preventing it from construct a cell wall. The bacteria die instead of reproducing. Antibiotics are like selective poisons, because they target bacteria and not the body’s own cells.

They are not effective against viruses, however. Unlike bacteria, a virus isn’t a living, reproducing lifeform, just a piece of DBA or RNA. A virus injects its DNA into a living cell and the cell itself reproduces more of the viral DNA. There is nothing to “kill,” so antibiotics don’t work on viruses.

ABOUT STREP THROAT:
Most sore throats are caused by viruses and generally clear up without medical treatment.

Strep throat is an infection caused by a type of bacteria, and thus needs treatment with antibiotics. Symptoms include fever, stomach pain and red swollen tonsils. The bacteria can be transferred to others by sneezing, coughing or shaking hands.

A doctor will usually take a throat culture to test for strep throat. Lack of treatment can lead to other health problems, such as rheumatic fever (which can damage the heart), scarlet fever, blood infections or kidney disease.

DRUG RESISTANCE:
Bacteria are highly adaptive, and over time they naturally develop resistance, protecting them from incoming germs (and antibiotics) and making them harder to kill.

Repeated exposure to penicillin and amoxicillin can result in a throat full of bacteria that can shield strep germs from the older drugs.

The surviving bacteria then reproduce more and become more dominant. Sometimes parents discontinue antibiotic medication prematurely when their children begin to feel better, so the strep germ isn’t entirely killed off, leading to much more severe infections requiring the use of even stronger drugs later on.

North Carolina Sea Grant researchers have isolated a new peptide antibiotic from the American oyster that may have implications for managing many diseases in oysters.

The new antimicrobial peptide “American oyster defensin” (AOD) may protect against bacteria in Crassostrea virginica, a species that is native to North Carolina and important economically to Atlantic and Gulf Coast fisheries.

“This peptide may be helpful in selecting disease-resistant oysters for aquaculture and fisheries and may also allow for the development of a test to monitor oyster health,” says Ed Noga, professor at the North Carolina State University College of Veterinary Medicine.

“In recent years, a number of pathogens, especially bacteria and parasites, have devastated American oyster populations.”

The research findings appear in the new (Dec. 30) issue of Biochemical and Biophysical Research Communications.

Pathogens such as dermo (Perkinsus marinus) have caused major decreases in oyster productivity — bacterial pathogens — such as Vibrio vulnificus that can cause a food-borne illness are a human health concern, according to Noga.

This is the first time that researchers have isolated an antimicrobial peptide from any oyster species, he says.

NC State veterinary medicine postdoctoral research associate Jung-Kil Seo, as well as scientists J. Myron Crawford and Kathryn L. Stone of Yale University’s Keck Biotechnology Resource Laboratory, collaborated with Noga on the study.

“The results may be used to better understand the innate immune system of American oysters and to enhance research to protect it from important microbial infections,” according to Noga.

“Further studies are needed to identify sites of synthesis and storage of AOD and determine mechanisms affecting its regulation.”

The effort to find preserved samples of the 1918 influenza virus has been a pursuit of both historical and medical importance.

The influenza pandemic in 1918 was the most devastating single disease outbreak in modern history, and examining the virus that caused it may help prepare for, and possibly prevent, future pandemics. When the complete sequence of the 1918 virus was published in 2005, it represented a watershed event for influenza researchers worldwide.

An article in the journal Antiviral Therapy, scientists at the National Institute of Allergy and Infectious Diseases (NIAID), part of the National Institutes of Health, narrate the story of how scientists discovered samples of the 1918 strain in fixed autopsy tissues and in the body of a woman buried in the Alaskan permafrost.

The article places this discovery in the context of decades of research into the cause of pandemic influenza, and the authors detail the strange convergence of events that allowed them to recover and sequence the virus in the first place. Its genetic material is so fragile that it should not have survived for days, let alone decades.

In a mass grave in a remote Inuit village near the town of Brevig Mission, a large Inuit woman lay buried under more than six feet of ice and dirt for more than 75 years. The permafrost plus the woman’s ample fat stores kept the virus in her lungs so well preserved that when a team of scientists exhumed her body in the late 1990s, they could recover enough viral RNA to sequence the 1918 strain in its whole entirety. This remarkable good fortune enabled these scientists to open a window onto a past pandemic. It could also help mankind gain a foothold for preventing a future one.

New Zealand with only a population of 6 million people is a nation of food worriers after a 750 people survey found some interesting data on their views of food and food borne pathogens.

Interestingly, scientists believe people may be anxiously worrying over small issues that pose little risk to their health.

In the phone survey conducted for the New Zealand Food Safety Authority (NZFSA), they found that salmonella was the worst food fear, with 77 per cent being “very concerned” about it.

In addition, an antibiotic in meat was next with 67 per cent and campylobacter with 63 per cent.

But scientist Dr Donald Campbell said people were missing the three biggest threats to life, the amount of salt, fat and sugar in their diet.

Interestingly, people were more concern about eating at local buffets, food halls and ethnic restaurants than food made at home in an unhygienic way.

Campbell, the NZFSA principal adviser of public health, was surprised salmonella was the most feared.

“I would have expected campylobacter to be higher than salmonella,” he said.

Campylobacter had a greater impact on the community than salmonella. There were generally 10 times as many cases of campylobacter in a year than salmonella, said Campbell.

New Zealand had a 15 per cent rise in notified campylobacter cases last year to 15,873, compared with 1335 cases of salmonella.

Both are food-borne illnesses that have been associated with chicken and raw meats, and can cause symptoms of diarrhea, abdominal pain, nausea and headache.

Canterbury medical officer of health Alistair Humphrey put campylobacter high on his list of concerns.

But he said many other bugs lurked in food, including norovirus which causes gastroenteritis’s of which there had been outbreaks in Christchurch.

Antibiotics used in animals for therapeutic purposes and to prevent disease may scare consumers towards vegetarianism, but “the evidence is of it being a very low risk,” Campbell said.

Listeria was a rarer food-borne illness (19 cases nationally last year) but could have devastating consequences, he said. At least half of cases occurred in pregnant women and one in four of their babies have died.

Listeria is linked to deli meats, poultry products, smoked seafood’s, soft cheeses and pre-cooked sausages. However stronger regulations have forced many food manufacturers to comply with strict hygiene.

Participants were more spooked about the use of pesticides in food production and additives.

More than 60 per cent of participants were “very concerned” about their potential effects.

Campbell said these were more “perceived risk” than actual risk, as pesticides and additives were covered by regulations.

The authority commissions the surveys every few years to gauge public feeling and tailor its food safety messages. “We eat at least three times a day, so it matters to us all,” Campbell said.

Genetically modified food greatly concerned 56 per cent of respondents, about the same as in two previous years, whereas a new category, food from cloned animals, worried 54 per cent.

“There is such a small use of genetically modified food. I would not put them as high on the list,” said Campbell.

Food allergies and irradiated food brought up the rear, with 47 per cent and 41 per cent respectively.

A team of scientist have developed a specially tailored viruses could eradicate chronic bacterial infections. When certain bacteria multiply, they produce exo-polysaccharides which lead to biofilms which are nearly impossible to eradicate using conventional antibiotics. Biofilms can be found on medical devices such as catheters.

Boston University biomedical engineers have designed a new, highly effective means of dispersing and killing the bacteria living in biofilms. Led by synthetic biologist James Collins, the team has engineered viruses that attack biofilms on two fronts: by killing the bacteria that live in them, and by dissolving the carbohydrates that hold them together. If such bacteria attacking viruses are proved safe for industrial and clinical use, says Collins, researchers could develop stocks of different kinds of viruses, each tailored to attack a different kind of biofilm.

Collins has designed a virus that can disperse more than 99 percent of the E. coli in a model biofilm. Helen Blackwell a chemist at the University of Wisconsin-Madison, believes that this is an “enormous” achievement: “I haven’t seen anything as effective as this approach.” Collins’s engineered virus is described online in the journal Proceedings of the National Academy of Sciences.

Bacteria living communally in biofilms are one thousand times more resistant to antibiotics than free-swimming bacteria are, says Collins. They are protected by a sticky carbohydrate scaffold called a matrix. The matrix blocks antibiotics and cells from the human immune system, and even provides something like a primitive circulatory system for the bacteria.

In a few cases, including some chronic ear infections in children and chronic lung infections in cystic-fibrosis patients, the tissue harboring a biofilm must simply be cut out. Large doses of antibiotics can usually eradicate these infections, says Blackwell.

But she notes that there is some worry that drug-resistant biofilm infections are becoming more common, and that the use of antibiotics seems to induce biofilm formation.

“One thing I like about Collins’s approach is that it is two-pronged, says Philip Stewart, director of the Center for Biofilm Engineering at Montana State University. “The viruses kill the bacteria, but they also target the biofilm matrix.” Collins’s approach is to select a virus that already targets the bacteria of interest, such as E. coli or Staphylococcus. Then he introduces into the virus a gene for an enzyme that dissolves the main carbohydrate component of the biofilm matrix protecting the bacteria.

There are viruses specialized to infect every bacterial species. These viruses replicate inside bacterial cells, then burst them open, killing the bacteria, and spread to other bacterial cells. But they do not harm animal cells or bacteria other than the kind to which they are targeted.

Naturally occurring viruses can attack biofilms. But Collins showed that giving a virus a gene for dissolving the matrix increased the virus’s effectiveness by 4.5 orders of magnitude.

Collins’s proof-of-concept virus is tailored to a particular type of E. coli biofilm. “There are many species and strains of bacteria out there,” he says, and a single biofilm might support multiple bacterial species and strains. To a lesser degree, there is also some diversity in the components of the biofilm matrix. However, Collins says that because of the increasing speed and falling price of DNA-sequencing and synthesis technologies, it would not be difficult to develop a virus tailored to each kind of biofilm.

Collins’s viral technique appears to overcome some of the problems with chemical techniques. Blackwell, who is designing small molecules to disrupt the bacterial signaling pathways that maintain biofilms, says that delivery of biofilm-disrupting chemicals such as enzymes has been a major hurdle.

The risks of such viruses are unclear, but there is some concern that they might provoke a dangerous immune response. One reason they might not have been widely studied for their potential to treat infection, says Collins, is that antibiotics have been sufficient so far. But with the emergence of multi-drug resistant bacterial strains in hospitals, “a number of companies are looking to viruses,” he says.

For industrial applications where you’re not putting them in someone’s body, these viruses could have a huge impact”. Finding and farming bacteria could change the way we live.

The first detailed images of an elusive drug that targets the outer wall of bacteria may provide scientists with enough new information to aid design of novel antibiotics. The drugs are much needed to treat deadly infections initiated by Staphylococcus aureus and other bacterial pathogens.

The research team, led by Natalie Strynadka, a Howard Hughes Medical Institute (HHMI) international research scholar at the University of British Columbia in Vancouver, Canada, published its findings in the March 9, 2007, issue of the journal Science.

“This enzyme is an awesome target for antibiotics. We have a totally new understanding of how the enzyme works and how a very good animal antibiotic inhibits the enzyme”, Dr Strynadka said.

Penicillin and many newer antibiotics work by blocking a piece of the machinery bacteria use to construct their durable outer walls. Without these tough, protective coatings, bacteria die. The enzymatic machinery (known as PBP2) studied by Strynadka’s group has two main parts: One end assembles long sugar fibers; the other end stitches them together with bits of protein to form a sturdy inter-locking mesh shell.

Strynadka’s team has provided a long-awaited look at the portion of the enzyme used in the first step of the biochemical pathway that initiates assembly of the sugar coating. The second step is targeted by penicillin and has been well studied.

Although scientists have spent many years identifying bacterial components whose structural features might have weaknesses that can be exploited by antibiotics, progress in turning up bona fide drug targets has been slow. The cell wall enzymes in particular have tantalized scientists, Strynadka said. “The cell wall has all the hallmarks of a great drug target,” she explained. “It is essential to the survival of all bacteria. The enzymes that create the cell wall are unique to bacteria. And it is accessible; you don’t have to get the
antibiotics into the cell.”

In their structural studies, the researchers focused on Staphylococcus aureus, a notorious human pathogen. An epidemic strain of the bacteria known as methicillin-resistant Staphylococcus aureus is resistant to several common antibiotics, including penicillin and amoxicillin, and is a great cause for concern among hospital infectious disease staff.

Postdoctoral fellow Andrew Lovering, who is first author on the paper, hopes the group’s three-dimensional pictures of the sugar-building enzyme from S. aureus will accelerate the search for an effective weapon against the infamous super bug.

The images produced by Strynadka’s team show the enzyme frozen in place by a powerful antibiotic called moenomycin. Moenomycin has been used for decades in animal feed to promote livestock growth. Bacteria have shown very little evidence of resistance to this antibiotic so far, and scientists think related compounds may be promising candidates for use in humans.

“This enzyme is an awesome target for antibiotics,” said Strynadka. “We have a totally new understanding of how the enzyme works and how a very good animal antibiotic inhibits the enzyme.” Although moenomycin is poorly absorbed by the human body, the new understanding of exactly how it
interferes with bacterial enzyme function should help scientists design modified versions that are more suitable for use in people.

Understanding the structure of this enzyme should also speed up screening and design of new antibiotics, which are in constant demand as microbes continually evolve new ways to evade the drugs that researchers design to thwart them.

The time it takes for bacteria to develop resistance to new antibiotics has been as short as one year for penicillin V and as long as 30 years for vancomycin.

Researchers attempting to solve the structure of this enzyme have struggled to recreate its cellular environment in the laboratory. But after much tinkering with different combinations of detergent, ions, and chemical additives, Strynadka’s team was able to crystallize the enzyme so that it would diffract x-rays into a pattern that would ultimately reveal its natural structure. They then were able to repeat the feat to reveal the crystal structure of the enzyme combined with the animal antibiotic.

Their findings help reveal how the enzyme prepares to assemble the bacteria’s sugar-coating by plucking sugars from a fat-sugar package known as lipid II. The antibiotic, which is another kind of sugar-lipid, probably mimics the lipid II molecule by tucking into a fold in the enzyme and taking up the space needed to bind to lipid II, the researchers believe. “We would like to see the enzyme in a complex with its natural substrates as well as with inhibitors,” Lovering said.

In the meantime, scientists now have the details of its shape and key contact points between enzyme and
antibiotic. The enzyme structure is the first ever solved of a member of a family of enzymes that remove sugars from lipids and attach them to other sugars. This process is used in a wide range of biochemical reactions, including allergic responses and cell signaling in cancer.

Researchers from the University of Sheffield have received joint funding from the Engineering and Physical Science Research Council (EPSRC) and the Ministry of Defence (MoD) to develop an innovative sensor to detect bacteria. The new method will use a polymer which will give a fluorescent signal when it encounters bacteria, allowing scientists to easily identify infected wounds much earlier than using conventional methodologies.

The new technology will be of immediate benefit to healthcare industries in general, as well as those involved in detecting infection in battlefield conditions and bacterial contamination, whether accidental or deliberate.

Currently identifying bacterial infection takes several days and requires swabbing and culturing of bacterial swabs as well as the use of specialist bacteriology laboratory facilities.

By combining polymers, which change shape when they encounter bacteria, and developing a light signal through fluorescence non radiative energy transfer (NRET), the researchers will be able to detect early stages of bacterial contamination.

Being developed by a multi-disciplinary team of researchers from the University’s Departments of Chemistry, Engineering Materials and the Dental School, the sensor will have widespread applications beyond the initial project.

Dr Steve Rimmer from the University’s Department of Chemistry, said: “The project is a great example of progress that can be achieved at the life sciences/physical sciences interface and we hope the project will deliver technology of real importance.”

The multi-disciplinary team will be led by Dr Steve Rimmer of the Department of Chemistry and consists of Dr Linda Swanson (Chemistry) Professor Sheila MacNeil (Engineering Materials) and Dr Ian Douglas (Clinical Dentistry).

The project received £670,000 funding jointly from the Engineering and Physical Science Research Council and the Defence Science and Technology Laboratory - an agency of the Ministry of Defence over three years and started in December 2006.