Thursday, February 26, 2009

Sesame Seed Extract And Konjac Gum May Help Ward Off Salmonella And E. Coli

A new study in SCI’s Journal of the Science of Food and Agriculture shows that konjac gum and sesame seed extract may offer protection against different strains of E. coli and Salmonella bacteria.

sesame                                        Konjac gum

(Sesame Seed)                                                           (Konjac Gum)

The study by Dr Petra Becker et al from Wageningen University and Research Centre, the Netherlands, shows that these foodstuffs act as binders for E. coli and Salmonella bacteria. The bacteria attach themselves to the fibrous foods instead of the gut cells of the host.

Dr Becker says that eating a diet full of these foodstuffs may offer protection from gastro-intestinal infections or reduce the severity of symptoms caused by E. coli or Salmonella.

Other foods that were shown to have a beneficial effect included yeast, tomato, and pumpkin.

In the lab study which also included negative controls, the scientists looked at 18 food-related products including coffee beans, carrot, mango, fermented soya, and food stabilizers such as locust bean gum and konjac gum. All were subjected to in vitro exposure to various bacteria which were allowed to attach themselves to the test products. The levels of bound bacteria were determined in a microplate-based method specifically developed for this purpose.

The results showed that sesame seed extract and konjac gum had the greatest number of adhered bacteria, leading to the conclusion that they may have a part to play in preventing certain E. coli and Salmonella from latching onto the host.

Dr Becker said: ‘The importance of fibre, particularly from certain foodstuffs, in maintaining a healthy gut and digestion cannot be underestimated. The study shows that these foods bind certain bacteria and may be a means of stopping bacteria from entering host cells thereby preventing disease.’

Source: Sciencedaily

Tuesday, February 24, 2009

Wilson Disease

Copper is is a chemical element with the symbol Cu  and atomic number 29. It is a ductile metal with very high thermal and electrical conductivity. Copper is an essential trace nutrient to all high plant and animal life. In animals, including humans, it is found primarily in the bloodstream, as a co-factor in various enzymes and in copper-based pigments. However, in sufficient amounts, copper can be poisonous and even fatal to organisms which leads to Wilson Disease.

Wilson disease is a genetic disorder that prevents the body from getting rid of extra copper. A small amount of copper obtained from food is needed to stay healthy, but too much copper is poisonous. In Wilson disease, copper builds up in the liver, brain, eyes, and other organs. Over time, high copper levels can cause life-threatening organ damage.

People who get Wilson disease inherit two abnormal copies of the ATP7B gene, one from each parent. Wilson disease carriers, who have only one copy of the abnormal gene, do not have symptoms. Most people with Wilson disease have no known family history of the disease. A person’s chances of having Wilson disease increase if one or both parents have it.


Wilson disease is caused by a buildup of copper in the body. Normally, copper from the diet is filtered out by the liver and released into bile, which flows out of the body through the gastrointestinal tract. People who have Wilson disease cannot release copper from the liver at a normal rate, due to a mutation of the ATP7B gene. When the copper storage capacity of the liver is exceeded, copper is released into the bloodstream and travels to other organs—including the brain, kidneys, and eyes.


Wilson disease first attacks the liver, the central nervous system, or both.

A buildup of copper in the liver may cause ongoing liver disease. Rarely, acute liver failure occurs; most patients develop signs and symptoms that accompany chronic liver disease, including

  • swelling of the liver or spleen
  • jaundice, or yellowing of the skin and whites of the eyes
  • fluid buildup in the legs or abdomen
  • a tendency to bruise easily
  • fatigue

A buildup of copper in the central nervous system may result in neurologic symptoms, including

  • problems with speech, swallowing, or physical coordination
  • tremors or uncontrolled movements
  • muscle stiffness
  • behavioral changes

Other signs and symptoms of Wilson disease include

  • anemia
  • low platelet or white blood cell count
  • slower blood clotting, measured by a blood test
  • high levels of amino acids, protein, uric acid, and carbohydrates in urine
  • premature osteoporosis and arthritis

wilson dieases

Kayser-Fleischer rings result from a buildup of copper in the eyes and are the most unique sign of Wilson disease. They appear in each eye as a rusty-brown ring around the edge of the iris and in the rim of the cornea. The iris is the colored part of the eye surrounding the pupil. The cornea is the transparent outer membrane that covers the eye.


Wilson disease is diagnosed through a physical examination and laboratory tests.

During the physical examination, a doctor will look for visible signs of Wilson disease. A special light called a slit lamp is used to look for Kayser-Fleischer rings in the eyes. Kayser-Fleischer rings are present in almost all people with Wilson disease who show signs of neurologic damage but are present in only 50 percent of those with signs of liver damage alone.


Laboratory tests measure the amount of copper in the blood, urine, and liver tissue. Most people with Wilson disease will have a lower than normal level of copper in the blood and a lower level of corresponding ceruloplasmin, a protein that carries copper in the bloodstream. In cases of acute liver failure caused by Wilson disease, the level of blood copper is often higher than normal. A 24-hour urine collection will show increased copper in the urine in most patients who display symptoms. A liver biopsy—a procedure that removes a small piece of liver tissue—can show if the liver is retaining too much copper. The analysis of biopsied liver tissue with a microscope detects liver damage, which often shows a pattern unique to Wilson disease.

Genetic testing may help diagnose Wilson disease in some people, particularly those with a family history of the disease.

Wilson disease can be misdiagnosed because it is rare and its symptoms are similar to those of other conditions


Wilson disease requires lifelong treatment to reduce and control the amount of copper in the body.

Initial therapy includes the removal of excess copper, a reduction of copper intake, and the treatment of any liver or central nervous system damage.

The drugs d-penicillamine (Cuprimine) and trientine hydrochloride (Syprine) release copper from organs into the bloodstream. Most of the copper is then filtered out by the kidneys and excreted in urine. A potential major side effect of both drugs is that neurologic symptoms can become worse—a possible result of the newly released copper becoming reabsorbed by the central nervous system. About 20 to 30 percent of patients using d-penicillamine will also initially experience other reactions to the medication, including fever, rash, and other drug-related effects on the kidneys and bone marrow. The risk of drug reaction and neurologic worsening appears to be lower with trientine hydrochloride, which should be the first choice for the treatment of all symptomatic patients.

Pregnant women should take a lower dose of d-penicillamine or trientine hydrochloride during pregnancy to reduce the risk of birth defects. A lower dose will also help reduce the risk of slower wound healing if surgical procedures are performed during childbirth.

Zinc, administered as zinc salts such as zinc acetate (Galzin), blocks the digestive tract’s absorption of copper from food. Zinc removes copper too slowly to be used alone as an initial therapy for people who already have symptoms, but it is often used in combination with d-penicillamine or trientine hydrochloride. Zinc is safe to use at full dosage during pregnancy.

Maintenance therapy begins when symptoms improve and tests show that copper has been reduced to a safe level. Maintenance therapy typically includes taking zinc and low doses of either d-penicillamine or trientine hydrochloride. Blood and urine should be monitored by a health care provider to ensure treatment is keeping copper at a safe level.

People with Wilson disease should reduce their dietary copper intake. They should not eat shellfish or liver, as these foods may contain high levels of copper. Other foods high in copper—including mushrooms, nuts, and chocolate—should be avoided during initial therapy but, in most cases, may be eaten in moderation during maintenance therapy. People with Wilson disease should have their drinking water checked for copper content and should not take multivitamins that contain copper.

If the disorder is detected early and treated effectively, people with Wilson disease can enjoy good health.

Monday, February 23, 2009

Nose-spray Vaccine Against Botulism Effective In First Tests

A preclinical study found a new nasal spray vaccine to provide complete protection against a major botulism toxin, according to Nature journal Gene.

Botulism is caused by a bacterium, Clostridium botulinum, which produces toxins that cause paralysis and often death, as the muscles that control breathing fail.


Researchers are working to design a botulism vaccine that adds a second layer of immune protection against exposure to BoNTs. When complete, it would prime the disease-fighting cells in mucous membranes lining the nose, those most likely to be exposed first, along with those in the blood. Standard vaccines, given by injection, prepare only the blood-based immune system to fight a given disease. Secondly, the hope is that a new, well-defined subunit vaccine will enable authorities to provide an effective vaccine without having to mass-produce the actual toxin, the hazardous first step in the manufacture of the current, stockpiled vaccine.

"In this study, we found that our vaccine could provide complete protection in one dose against one of the seven BoNTs, which strongly suggests that the same platform could be applied to build a multi-component vaccine against the remaining six," said Mingtao Zeng, Ph.D., assistant professor within Department of Microbiology and Immunology at the University of Rochester Medical Center, principal investigator and corresponding author of the study. "With these findings, we believe the design of a safe and inexpensive subunit vaccine can now proceed rapidly."

The study was in mice, but much of the evidence behind the current experimental vaccine was collected in animals as well. In a challenge common to many lines of vaccine research, it is "obviously unethical to test botulism vaccines in humans using the real pathogen."

Dangerous To Make

Without causing an actual infection, vaccines introduce weakened or detoxified versions of disease-related proteins to the immune system, which remembers to destroy them upon their next encounter.

Once researchers confirm the kind of immune response needed to achieve protection, they can choose for inclusion in a multi-component vaccine the key antigenic proteins that trigger the strongest immune response. The immune system reacts, not to the presence of a whole bacterium, but instead to specific proteins residing on its surface, or secreted by it, and which reveal its nature as an invader.

There is currently no licensed vaccine for protection against botulism. The U.S. Food and Drug Administration has authorized the manufacture of an experimental, injectable vaccine consisting of detoxified versions of five types of BoNTs (serotype A, B, C, D, and E). The first step in its manufacture is to produce massive amounts of active toxins that are extremely dangerous to handle, adding greatly to cost and slowing the process.

Subunit vaccines like the one in the current study include nontoxic proteins that resemble those created by the bacteria, making them much safer to work with. A specific end-piece protein called heavy chain 50-kDa fragment (Hc50) has been identified as part of the mechanism that enables BoNT/C to enter the bloodstream. Once there, the toxin locks onto nerve endings in the brain and extremities, inhibiting their ability to release of the neurotransmitter acetylcholine and causing paralysis. In an important 1995 discovery, John Middlebrook, Ph.D., of the U.S. Army Medical Research Institute of Infectious Diseases (USAMRIID), found that Hc50 fragment of BoNTs, unlike the whole toxin used in the current vaccine, are not toxic when detached from the rest of the toxin, but still bring about the desired immune response.

To insert Hc50 and prime the immune system against it, researchers took a page from gene therapy, which uses disabled viruses as delivery vehicles into cells. Viruses are precision-designed by nature to invade cells and deliver therapeutic genes, and can do so safely once the viruses' own reproductive genes have been removed. Past studies have shown that adenoviruses expressing protein antigens can be delivered by the mucosal route.

In addition, adenoviruses can be quickly and inexpensively mass produced, making them an attractive platform for researchers currently developing vaccines against HIV, bird flu, tuberculosis and anthrax, as well as against BoNTs. Zeng and colleagues are currently testing a nasal anthrax vaccine as well.

In the current study, the team used the virus to deliver BoNT/C Hc50 as a mucosal vaccine against botulism in a mouse model. A single dose of intranasal inoculation (nose spray) of the adenovirus vector brought about a high level of HC50-specific immune response as early as two weeks after vaccination. The response consisted of the activation of antibodies, immune cells in both mice and humans that attach to bacterial proteins like BoNTs to shut down their toxic effect. Antibodies classes start with the "Ig" prefix standing for immunoglobulin, another name for antibody, and the specific response to vaccine in the current study consisted of IgG, IgG1, and IgG2a activation in the blood and IgA activation in mucous membranes.

In mice injected with lethal doses of BoNT/C toxin, all mice (8/8, or 100 percent) that received larger dose (2 × 107 pfu) of the BoNT/C-HC50 vaccine had survived by seven weeks after toxin challenge with no botulism symptoms, whereas none of the mice that received vector control without Hc50 survived. The protective immunity in mice could last for seven months after vaccination, researchers said.

We have demonstrated for the first time that a single, intranasal vaccination of an adenovirus-based vector encoding a humanized HC 50 of BoNT/C can provide full protection in vaccinated mice against botulinum neurotoxin type C," Zeng said. "We look forward to finalizing a vaccine, the most likely candidates for which would be active military and emergency responding personnel in forward areas."


Thursday, February 19, 2009

Celiac Disease, Gluten

Pizza, Ice-Cream, Pasta, Cookies Wow !!!! But halt. foodThis may contain 'Gluten' which may be used during the process to taste and look better. Yes, Gluten is harmful and leads to a disease called 'Celiac', which results damage of small intestine.

Celiac disease is a digestive disease that damages the small intestine and interferes with absorption of nutrients from food. People who have celiac disease cannot tolerate gluten, a protein in wheat, rye, and barley. Gluten is found mainly in foods but may also be found in everyday products such as medicines, vitamins, and lip balms.

When people with celiac disease eat foods or use products containing gluten, their immune system responds by damaging or destroying villi—the tiny, fingerlike protrusions lining the small intestine. Villi normally allow nutrients from food to be absorbed through the walls of the small intestine into the bloodstream. Without healthy villi, a person becomes malnourished, no matter how much food one eats.

 Celiac disease is both a disease of malabsorption—meaning nutrients are not absorbed properly—and an abnormal immune reaction to gluten. Celiac disease is also known as celiac sprue, nontropical sprue, and gluten-sensitive enteropathy. Celiac disease is genetic, meaning it runs in families. Sometimes the disease is triggered—or small intesinebecomes active for the first time—after surgery, pregnancy, childbirth, viral infection, or severe emotional stress.


Classic symptoms of disease include diarrhea, weight loss (or stunted growth in children), and fatigue.

  • unexplained iron-deficiency anemia
  • fatigue
  • bone or joint pain
  • arthritis
  • bone loss or osteoporosis
  • depression or anxiety
  • tingling numbness in the hands and feet
  • seizures
  • missed menstrual periods
  • infertility or recurrent miscarriage
  • canker sores inside the mouth
  • an itchy skin rash called dermatitis herpetiformis

People with celiac disease may have no symptoms but can still develop complications of the disease over time. Long-term complications include malnutrition—which can lead to anemia, osteoporosis, and miscarriage, among other problems—liver diseases, and cancers of the intestine.


Celiac disease is caused by a reaction to gliadin, a gluten protein. Upon exposure to gliadin, the enzyme tissue transglutaminase modifies the protein, and the immune system cross-reacts with the bowel tissue, causing an inflammatory reaction. That leads to flattening of the lining of the small intestine (called villous atrophy). This interferes with the absorption of nutrients because the intestinal villi are responsible for absorption.


Blood Tests

People with celiac disease have higher than normal levels of certain autoantibodies—proteins that react against the body’s own cells or tissues—in their blood. To diagnose celiac disease, doctors will test blood for high levels of anti-tissue transglutaminase antibodies (tTGA) or anti-endomysium antibodies (EMA). If test results are negative but celiac disease is still suspected, additional blood tests may be needed.

Before being tested, one should continue to eat a diet that includes foods with gluten, such as breads and pastas. If a person stops eating foods with gluten before being tested, the results may be negative for celiac disease even if the disease is present.

Intestinal Biopsy

If blood tests and symptoms suggest celiac disease, a biopsy of the small intestine is performed to confirm the diagnosis. During the biopsy, the doctor removes tiny pieces of tissue from the small intestine to check for damage to the villi. To obtain the tissue sample, the doctor eases a long, thin tube called an endoscope through the patient’s mouth and stomach into the small intestine. The doctor then takes the samples using instruments passed through the endoscope.


The only treatment for celiac disease is a gluten-free diet. A gluten-free diet means not eating foods that contain wheat, rye, and barley. People with celiac disease can eat a well-balanced diet with a variety of foods. They can use potato, rice, soy, amaranth, quinoa, buckwheat, or bean flour instead of wheat flour. They can buy gluten-free bread, pasta, and other products from stores that carry organic foods. Plain” meat, fish, rice, fruits, and vegetables do not contain gluten.

The gluten-free diet requires a completely new approach to eating. Newly diagnosed people and their families may find support groups helpful as they learn to adjust to a new way of life. People with celiac disease must be cautious about what they buy for lunch at school or work, what they purchase at the grocery store, what they eat at restaurants or parties, and what they grab for a snack. Eating out can be a challenge. When in doubt about a menu item, a person with celiac disease should ask the waiter or chef about ingredients and preparation or if a gluten-free menu is available.

Gluten is also used in some medications. People with celiac disease should ask a pharmacist if prescribed medications contain wheat. Because gluten is sometimes used as an additive in unexpected products—such as lipstick and play dough reading product labels is important. If the ingredients are not listed on the label, the manufacturer should provide a list upon request. With practice, screening for gluten becomes second nature.

Wednesday, February 18, 2009

Micro-motor runs on bacteria power

System could power tiny robots or electronic systems

Scientists have yoked bacteria to power rotary motors, the first microscopic mechanical devices to successfully incorporate living microbes together with inorganic parts.

"In far future plans, we would like to make micro-robots driven by biological motors," researcher Yuichi Hiratsuka, a nanobiotechnologist now at the University of Tokyo, told LiveScience.

While at Japan's National Institute of Advanced Industrial Science and Technology near Tokyo, Hiratsuka and his colleagues experimented with one of the most rapid crawling bacteria, Mycoplasma mobile.

micro motor

This pear-shaped microbe, a millionth of a meter long, can glide over surfaces at up to seven-tenths of an inch an hour. Translated to a 6-foot-tall (180-centimeter-tall) runner, this roughly equates to 20 mph (32 kilometers per hour).

The researchers built circular pathways coated with sugary proteins, which the microbe needs to stick to in order to glide over surfaces. They then docked a rotor onto the track and coated the bacteria with vitamin B7, which acted like glue to yoke the germs to the cog. They also genetically modified the microbes so they stuck to their tracks more stably.

The scientists created roughly 20,000 rotors on a silicon chip. Each cog is etched from silica, which sand is made of, and is 20 microns wide, or roughly a fifth the diameter of a human hair.

The rotors spun at roughly 1.5 to 2.6 revolutions per minute. Each individual cell in these motors generates roughly 10,000 times less torque than conventional microscopic electronic motors can.

However, Hiratsuka noted they could improve the torque their systems generate by increasing the number of bacteria circling the tracks, which can hold up to 100 microbes. Moreover, he added that their systems could repair themselves, require only the sugar glucose as fuel, do not need wires and can work in wet environments, unlike the electronic motors.

In the future, instead of live bacteria, the researchers suggest using dead ones to avoid the potential biohazards living microbes pose. These dead "ghosts," as the scientists dub them, can still glide if their motors are given the right organic compounds.

In addition to helping drive micro-robots, Hiratsuka suggested that bacteria-powered motors could help propel micropumps in lab-on-a-chip devices. "Alternatively, we may be able to construct electronic generator systems, which generate electric energy from an abundant chemical source — glucose in the body," he said.


Wednesday, February 4, 2009

Cheese — it's grosser than you thought

Behind the taste lie bacteria, stomach lining, pesticides and pure fat

Cheese makes some foodies jump up and down like little kids, but behind that heavenly taste and texture lies bacteria, mammal stomach lining and pure fat.

To ripen cheese and add flavor, bacterial strains are freely injected and smeared into the substance. But not all have been accounted for, a new study finds.

Researchers at Newcastle University in England have now identified eight previously undiscovered microbes on the French, brie-like cheese called Reblochon. The potential benefits of these new microbes are still unknown.


Flourishing microbes are consumed with every bite of cheese (though the cooling temperatures in refrigerators do slow down bacterial growth, they do not kill them in cheese or in any other food). Bacteria (either naturally swimming around the milk or manually injected) and enzymes derived from the inner stomach linings of any slaughtered milk-producing mammal (called rennet) are added to coagulate the milk into curds.

Two proteins arise from curdled milk and manufacturers capitalize on them: The first is whey, which is essentially leftover liquid from curdled milk (and is increasingly being used as an ingredient in producing other foods). The second is casein, which makes up the bulk of the solid part of cheese, along with fat.

Fat is what gives cheese its taste, and 70 to 80 percent of the calories in cheese come from pure fat.

Factories are adding more bacterial groups into cheese to achieve enhanced flavors.

Cheese might be a hot commodity, but like other dairy products, it can have some unhealthy aspects. Other ways to get your calcium fix include eating the following foods: fortified grains, kale, collard greens, mustard greens, cabbage, kelp, seaweed, watercress, chickpeas, broccoli, red beans, soybeans, tofu, seeds and raw nuts. With all that variety, there's hope for any cheese addict. Only it won't taste, or smell, the same.