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One Dose of H1N1 Vaccine May Provide Sufficient Protection for Infants and Children

Posted on : 10:52 PM | By : Biochemistry Den | In : Diseases , swine Flu

One dose of vaccine may be effective to protect infants and children and reduce transmission of the H1N1 virus, according to a study in JAMA, just published online because of its public health implications. The study will appear in the January 6 print edition of the journal.

Initial reports of 2009 influenza A(H1N1) infection in many countries have largely involved children, especially those attending school. Reports have also indicated high hospitalization rates of children younger than 5 years of age in the current pandemic, according to background information provided by the authors. "The Advisory Committee on Immunization Practices also currently recommends that infants and children aged 9 years or younger receive two doses of H1N1 influenza vaccine at least 21 days apart, based on existing experience with seasonal trivalent influenza vaccines in this age group."

Terry Nolan, M.B.B.S., Ph.D., from the University of Melbourne, Australia and colleagues assessed the effectiveness and safety of two doses of a 2009 influenza A(H1N1) vaccine in 370 healthy infants and children ages six-months to less than 9 years living in Australia. The children were randomized into groups that received a two-injection regimen 21 days apart in doses of either 15-micrograms or 30-micrograms of the vaccine.

"Following the first dose of vaccine, antibody titers of 1:40 or greater were observed in 161 of 174 infants and children in the 15-microgram group (92.5 percent) and in 168 of 172 infants and children in the 30 microgram group (97.7 percent)," the authors report. "All participants demonstrated antibody titers of 1:40 or greater after the second vaccine dose," [which means that every child achieved an antibody level considered high enough to protect against the H1N1 virus]. The researchers note that the majority of adverse reactions to the vaccine were mild to moderate in severity. The immune responses to the vaccine were strong regardless of age, baseline antibody status, or whether the child had received a seasonal influenza vaccination prior to this study.

"Our findings suggest that a single dose 15-microgram dose vaccine regimen may be effective and well tolerated in children, and may have positive implications for disease protection and reduced transmission of pandemic H1N1 in the wider population," the authors conclude.

Editor's Note: This study was sponsored by CSL Limited with funding from the Australian government's Department of Health and Ageing.

Editorial: 2009 Influenza A(H1N1) Vaccines for Children

"Even though influenza activity has decreased in recent weeks in some states, there remains the possibility of continued activity through the traditional winter influenza season and the prospect of normal winter circulation of seasonal influenza viruses," and the authors of the editorial note that this pandemic has highlighted the fact the children have no measurable immunity against the H1N1 virus.

Anthony E. Fiore, M.D., M.P.H., from the National Center for Infectious Diseases, Centers for Disease Control and Prevention, Atlanta, and Kathleen M. Neuzil, M.D., M.P.H., of PATH, Seattle, write that children have been a primary source of illness in community outbreaks of pandemic influenza with more severe complications, hospitalizations and deaths from this virus than what is usually seen for seasonal influenza.

The editorial authors urge caution at interpretation of the results of the study. "The hemagglutinin antigen content administered to six-month-old infants and children younger than 3 years in this study was 15-micrograms, the equivalent of two doses of the 7.5-microgram vaccine currently licensed in the United States for this age group."

"The immunogenicity data presented by Nolan et al suggest that at least some children will be protected after a single 15-microgram dose of the H1N1 vaccine used in this study, but the findings cannot be generalized with confidence to all children, epidemiological circumstances in every country, or different vaccine formulations."

In conclusion, the authors write: "… it remains prudent to continue to follow current recommendations for administering two doses to infants and young children while awaiting definitive vaccine effectiveness data."

Swine flu - everything you need to know

The number of cases of swine flu in England continued to fall last week (week ending 9 August). The Health Protection Agency (HPA) estimates there were 25,000 new cases of swine flu in England last week, compared with 30,000 the week before and 100,000 the week before that. Cases of swine flu have fallen in all regions and among all age groups.

The disease is generally mild in most people so far, but is proving severe in a small minority of cases. So far 371 people have been hospitalised in England, while 44 people have died.

Swine flu vaccine

The government has announced that priority for the swine flu vaccine will be given to at-risk groups. These include pregnant women and people with serious underlying health conditions.

Vaccinations for these groups are expected to begin in the autumn. Steps are being taken to extend the vaccination programme to other people once this stage has been completed.

Swine flu - treatment and prevention

If you are in England, you can get antivirals to treat swine flu from a local collection point without seeing your GP. If you are in Scotland, Wales or Northern Ireland, contact your GP or specific helpline. Reduce your risk of catching swine flu by following good hand hygiene – CATCH IT, BIN IT, KILL IT. Antiviral drugs - Tamiflu and Relenza

Swine flu is being treated with antiviral drugs such as Tamiflu and Relenza. Antiviral drugs work by preventing the flu virus from reproducing - to be effective you need to take them within 48 hours of the symptoms beginning. This can reduce the risk of complications and possibly shorten the illness by a day.

If the National Pandemic Flu Service or your GP confirm you have swine flu, you will be told where your nearest antiviral collection point is so your 'flu friend' - a friend or relative who does not have swine flu - can pick up antiviral drugs for you

What Is Swine Flu? How Is Swine Flu Treated?

Posted on : 2:10 AM | By : Biochemistry Den | In : biochemistry , Clinical Studeis , CSIR-UGC-NET , Diseases , Examination gallary , GATE , Immunology

Swine flu (swine influenza) is a disease of pigs. It is a highly contagious respiratory disease caused by one of many Influenza A viruses. Approximately 1% to 4% of pigs that get swine flu die from it. It is spread among pigs by direct and indirect contact, aerosols, and from pigs that are infected but do not have symptoms. In many parts of the world pigs are vaccinated against swine flu.
Most commonly, swine flu is of the H1N1 influenza subtype. However, they can sometimes come from the other types, such as H1N2, H3N1, and H3N2.
The current outbreak of swine flu that has infected humans is of the H1N1 type - this type is not as dangerous as some others.

Avian Influenza (Bird Flu) can also infect pigs

Avian flu and human seasonal flu viruses can infect pigs, as well as swine influenza. The H3N2 influenza virus subtype, a virulent one, is thought to have come from pigs - it went on to infect humans.
It is possible for pigs to be infected with more than one flu virus subtype simultaneously. When this happens the genes of the viruses have the opportunity to mingle. When different flu subtypes mix they can create a new virus which contains the genes from several sources - a reassortant virus.

Although swine influenza tends to just infect pigs, they can, and sometimes do, jump the species barrier and infect humans.

What is the risk for human health?

Outbreaks of human infection from a virus which came from pigs (swine influenza) do happen and are sometimes reported. Symptoms will generally be similar to seasonal human influenzas - this can range from mild or no symptoms at all, to severe and possibly fatal pneumonia.
As swine flu symptoms are similar to typical human seasonal flu symptoms, and other upper respiratory tract infections, detection of swine flu in humans often does not happen, and when it does it is usually purely by chance through seasonal influenza surveillance. If symptoms are mild it is extremely unlikely that any connection to swine influenza is found - even if it is there. In other words, unless the doctors and experts are specifically looking for swine flu, it is rarely detected. Because of this, we really do not know what the true human infection rate is.

Examples of known swine flu infecting humans

Since the World Health Organization's (WHO's) implementation of IHR (2005) in 2007, they have been notified of swine influenza cases from the USA and Spain.
In March/April 2009 human cases of influenza A swine fever (H1N1) were first reported in California and Texas. Later other states also reported cases. A significant number of human cases during the same period have also been reported in Mexico - starting just in Mexico City, but now throughout various parts of the country. More cases are being reported in Canada, Europe, and New Zealand - mainly from people who have been in Mexico.

How does a human catch swine influenza?

From contact with infected pigs (most common way)
From contact with infected humans (much less common way)

In cases when humans have infected other humans close contact was necessary with the infected person, and they nearly always occurred in closed groups of people.

Can I eat pork meat and pork products?

If the pork meat and pork food products have been handled properly transmission of swine influenza to humans is not possible. Cooking pork meats to a temperature of 70C (160F) kills the virus. So the answer is YES, pork meat and pork food products are safe to eat.

Where have pigs been infected?

As swine influenza infection among pigs is not an internationally notifiable disease we cannot be completely sure. Swine influenza infection among pigs is known to be endemic in the USA. Outbreaks have also occurred in other parts of North America, South American, Europe, Africa, China, Japan, and other parts of Asia.

Is there a pandemic risk?

People who are not in close contact with pigs generally have no immunity to the swine influenza viruses - they are less likely to be able to prevent a virus infection. If the virus infects enough people in a given area, the risk of an influenza pandemic is significantly greater. Experts say it is very hard to predict what impact a flu pandemic caused by a swine influenza virus would have on the global human population. This would depend on how virulent the virus is, what existing immunity among humans there already is, plus several other factors.

Do we have a specific swine flu vaccine?

No - not for humans.

Will current human flu vaccines help protect people from swine influenza infection?

We really don't know. Influenza viruses are adapting and changing all the time. If a vaccine was made, it would have to be specifically for a current strain that is circulating for it to be effective. The WHO says it needs access to as many viruses as possible so that it can isolate the most appropriate candidate vaccine.

What are the signs and symptoms of swine influenza in humans?

They are similar to those of regular flu, and include:

Body aches
Chills
Cough
Diarrhea (less common)
Headache
Sore throat
Temperature (fever)
Tiredness (fatigue)
Vomiting (less common)

What medications are there?

There are some drugs around that can effectively treat swine flu infection in humans - and many types of flu infections in humans. There are two main types:

adamantanes (amantadine and remantadine)
inhibitors of influenza neuraminidase (oseltamivir and zanamivir)

Most previous swine influenza human cases recovered completely without the need for medical attention.

What can I do to protect myself?

Wash your hands regularly with soap
Try to stay healthy
Get plenty of sleep
Do plenty of exercise
Try to manage your stress
Drink plenty of liquids
Eat a well balanced diet
Refrain from touching surfaces which may have the virus
Do not get close to people who are sick
Stay away from crowded areas if there is a swine flu outbreak in your area

If I am infected, how can I stop others from becoming infected?

Limit your contact with other people
Do not go to work or school
When you cough or sneeze cover your mouth with a tissue. If you do not have a tissue, cover your mouth and nose.
Put your used tissues in a waste basket
Wash your hands and face regularly
Keep all surfaces you have touched clean
Follow your doctor's instructions

Mexico City - Some good news

In Mexico City, where a sizeable number of people have become infected with H1N1 swine flu, authorities are urging people with flu symptoms to go straight to their doctors or a local hospital. They insist that the flu is completely treatable if the patient comes in straight away.

What is Swine Flu - Video

The Centers for Disease Control and Prevention (CDC) Influenza Division has produced a video all about swine flu.
This video includes information on the signs and symptoms of swine flu, how swine flu is transmitted, what medicines are available to treat it and steps that people can take to help protect themselves from it. There are also some tips on what to do if you become ill with swine flu.

Map of Swine Flu Outbreaks

If you would like to keep up-to-date with the locations of the latest outbreaks of H1N1, see the map of swine flu outbreaks.

Virus Linked To Some Cases Of Common Skin Cancer

Posted on : 2:37 AM | By : Biochemistry Den | In : biochemistry , Cancer , Clinical Studeis , CSIR-UGC-NET , Diseases , GATE

A virus discovered last year in a rare form of skin cancer has also been found in people with the second most common form of skin cancer among Americans, according to researchers at the Ohio State University Comprehensive Cancer Center - James Cancer Hospital and Solove Research Institute.

The researchers examined tissue samples from 58 people with squamous cell carcinoma (SCC), a highly curable form of skin cancer that is expected to affect more than 200,000 Americans this year.

They identified the virus in more than a third of the patients and in 15 percent of the tumors tested. In addition, all of the virus found in tumor cells had a mutation that could enable the viral DNA to integrate into the DNA of the host cell.

“This is indirect evidence that the virus might play a role in causing some cases of squamous cell carcinoma,” says principal investigator Amanda E. Toland, assistant professor of molecular virology, immunology and medical genetics and a researcher with the Ohio State University Comprehensive Cancer Center - James Cancer Hospital and Solove Research Institute.

The findings are published in a recent issue of the Journal of Investigative Dermatology.

The virus was first discovered in patients with Merkel cell carcinoma, a rare, aggressive skin cancer that occurs mainly in the elderly and people with a suppressed immune system. The people in the new study all had a healthy immune system.

“Originally it was thought that this virus caused only this rare skin cancer, but our findings indicate that it is a lot more prevalent than we initially thought.”

To learn if people with SCC harbored the virus, Toland, working closely with first author and graduate research associate Amy Dworkin and Ohio State pathologists O. Hans Iwenofu and Sara B. Peters, examined DNA samples from SCC tumors, from normal-appearing skin adjacent to the tumor, when available; from white blood cells, and from cells washed from the mouth.

The investigators detected the virus in 26 of 177 SCC samples, 11 of 63 adjacent-skin samples, and one sample from a mouthwash. They found no viral DNA in any of the blood samples from 57 patients. In all, 21 of 58 SCC patients, or 36 percent, tested positive for the virus.

By sequencing the viral DNA from 31 normal and tumor samples, the researchers showed that the same mutation was present in all the viruses tested from tumors, and in 60 percent of the viruses tested from adjacent healthy-looking tissue.

“That suggests that the virus may develop a mutation that causes it to integrate into host-cell DNA, and, therefore, may play a role in causing the cancer,” Toland says.

Next, Toland wants to test normal skin in healthy individuals to learn how common this virus is in people generally and to learn whether the virus actually integrates with the host DNA.

“If it proves to be a cancer-causing virus, and if it proves to be common in the general population, it might be something we should begin screening people for,” she says.

Funding from the American Cancer Society supported this research. Ohio State researchers Stephanie Y. Tseng and Dawn C. Allain were also involved in this study.

New Drug Target For Kaposi's Sarcoma

Posted on : 2:34 AM | By : Biochemistry Den | In : biochemistry , Clinical Studeis , CSIR-UGC-NET , Diseases , GATE

UCSF researchers have identified a new potential drug target for the herpes virus that causes Kaposi’s sarcoma, re-opening the possibility of using the class of drugs called protease inhibitors against the full herpes family of viruses, which for 20 years has been deemed too difficult to attain.

The new drug target, which is known as a protease dimer, could serve as a model for developing new therapeutics for diseases ranging from cancer to Alzheimer’s, the researchers say. Findings are reported in the Advance Online Publication section of the Nature Chemical Biology web site.

Most current antiviral drugs target the active sites of viral proteins, where enzymes and receptors work in a lock-and-key approach to either activate or deactivate that particular protein, the researchers explained. Traditionally, drug development has focused on inhibiting that lock-and-key action to prevent the enzyme, or receptor from being effective.

Some viral enzymes known as proteases, however, including those for HIV and the herpes virus family, take the form of a dimer, or two identical halves – much like a fully opened clamshell – in their most stable state. Those proteases play an essential role in making the virus infectious, but require the two clamshell halves to bind together to be activated, according to the paper.

The HIV protease was successfully targeted for drug development in the 1980s, by blocking the active site on the surface of the dimer, but the herpes virus protease dimer has consistently eluded efforts to disrupt it at its active site, the researchers said.

The UCSF team set out to find ways to instead prevent the two halves of the dimer from connecting at that clamshell joint, to prevent it from activating. What they found was a new target on the unstable, monomer form of the protease, which responded well to a chemical inhibitor.

“If you disrupt the protein-protein interactions, you don’t need the key to a specific lock,” said Charles S. Craik, PhD, senior author on the paper and a professor of pharmaceutical chemistry in the UCSF School of Pharmacy. “Instead, we’re essentially preventing the lock from being made in the first place.”

Craik, who also led a team that identified HIV protease inhibitors in the late 1980s, said the “Nature Chemical Biology” paper validates this new site as a viable option for small-molecule drugs to treat Kaposi’s, as well as other members of this viral family.

“All known herpes virus proteases are structurally similar,” Craik explained. “The inhibitor we found knocks out not only KS, but also the cytomegalovirus protease, so the site we’ve identified here could be a target for a broad-acting inhibitor against the entire viral family.”

To their knowledge, the researchers said, this is the first small-molecule inhibitor of a herpes virus protease to not only act outside the active site, but also to select for the partially unfolded protein to keep it from forming the dimer interface.

Herpes viruses make up one of the most prevalent viral families, including eight human viruses that cause a variety of devastating illnesses, the researchers said. Those include mononucleosis (Epstein-Barr virus), shingles (Varicella zoster virus), genital herpes (herpes simplex), retinitis (cytomegalovirus) and cancer (Kaposi’s sarcoma). While therapies exist for these viruses, they often have negative side effects and are facing rising viral resistance.

In addition to validating herpes virus proteases as suitable targets, Craik said this research was also among the first to use computational design to identify and create a potential drug to target that protease interface.

Using high-throughput screening, the team screened a library of 182 compounds that it had specifically and rationally designed to mimic the protease interface. The work identified six molecules that inhibited the Kaposi’s sarcoma virus protease activity by at least 50 percent, including one that was highly potent.

That discovery potentially opens myriad opportunities for drug discovery, Craik said, by making target receptors that were biologically validated, but then deemed undruggable, more attractive. Protein-protein interactions have been researched as drug targets against a range of diseases, from certain cancers to neurodegenerative diseases. This advance could enable researchers to reconsider those targets, he said.

The lead investigator on the paper was Tina Shahian, with the Graduate Group in Biochemistry and Molecular Biology at UCSF. Co-authors were Gregory M. Lee and Ana Lazic, both in the UCSF Department of Pharmaceutical Chemistry; and Leggy A. Arnold, Priya Velusamy, Christina M. Roels and R. Kiplin Guy, all with the Department of Chemical Biology and Therapeutics at St. Jude Children’s Research Hospital, Memphis, TN.

The CMV protease expression plasmid for this work was provided by Wade Gibson, a professor in the Department of Pharmacology and Molecular Sciences at Johns Hopkins School of Medicine. The work was funded by grants from the National Institutes of Health, the American Lebanese and Syrian Associated Charities and St. Jude Children’s Research Hospital.

Wood Glue Inspired by Mussels Chemist's Glue Borrows Unique Amino Acid from Mollusk

Posted on : 2:31 AM | By : Biochemistry Den | In : biochemistry , Clinical Studeis , CSIR-UGC-NET , Diseases , Examination gallary , GATE , Osmania University

Chemists combined an exotic form of an amino acid -- used by mussels to stick to rocks -- with soy flour to make a new, high-strength adhesive. The new glue helps in manufacturing natural-looking plywood without cancer-causing chemicals such as formaldehyde.

CORVALLIS, Ore.--Many people look for natural or green products for their homes. But even something as natural-looking as wood furniture or cabinets can contain cancer-causing chemicals like formaldehyde. Now, a scientist has created a non-toxic wood adhesive. And his inspiration didn't come from the forest. It came from the Oregon coast.

Pounding waves are no match for the mighty mussel, that produces strong, flexible threads that cling to rocks. This small shellfish inspired a big idea for wood chemist Kaichang Li.

"This thing is really amazing," Li, of Oregon State University in Corvallis, tells DBIS. He noticed mussels secrete a unique amino acid called dihydroxyphenylalanine. He found a way to add that amino acid to soy flour -- a product that's rich in protein, plentiful and non-toxic.

"Now the soy protein becomes a really good, very strong adhesive," Li says, wood glue so strong that plywood made with it stays stuck even after hours of boiling.

Oregon State University licensed the new glue to a plywood manufacturer who then sells the wood to furniture and cabinet makers.

Rick Fields, President of Neil Kelly Cabinets in Portland, Ore., says: "We're very excited about it. It's going to add a whole new dimension to our green and healthy approach to cabinet making." He is confident the new glue is safer for customers and says it shouldn't add to the cost of the cabinets.

BACKGROUND: Researchers have developed a new group of adhesives for wood products inspired by the ability of mussels to cling to rocks using thread-like tentacles. These threads are proteins that retain powerful adhesive properties even in water. By adding these amino acids to more common proteins, like soy flour, the scientists have produced new wood adhesives. The researchers are also exploring ways to create new adhesives from tree bark or decayed wood.

ADVANTAGES: The new wood adhesives are natural and environmentally friendly, unlike the formaldehyde-based adhesives currently used to make some wood products, especially plywood, particleboard, and laminated veneers. They are also stronger and more water resistant.

USES: The new glue is being used to make environmentally friendly particle board-the main wood used to make kitchen cabinets and other wood products. They may replace the formaldehyde-based wood adhesives currently used to make some wood composite products such as plywood, particleboard, and laminated veneer lumber products.

WHAT IS BIOMIMICRY? Biomimicry is a field in which scientists, engineers, and even architects study models and concepts found in nature, and try to use them to design new technologies. Here are some well-known examples of biomimicry:

Velcro was inspired by cockleburs, which cling tenaciously to clothing and animal fur.
The design for the Eastgate Building in Harare, Zimbabwe -- the country's largest commercial and shopping complex -- is based on the region's termite mounds.
Both Leonardo da Vinci and the Wright brothers studied the flight of birds when designing their flying machines.
Alexander Graham Bell designed his telephone receiver around the principles of the human ear.
Sonar was inspired by how whales, dolphins and bats emit high-pitched sounds and analyze the returning echoes to help them navigate.

WHERE IT'S BEING SOLD: Columbia Forest Products of Portland, the nation's largest producer of decorative plywood, has exclusive rights to use the glue in plywood.

Little-known Protein Found To Be Key Player in Building and Maintaining Healthy Cells

Posted on : 2:28 AM | By : Biochemistry Den | In : biochemistry , Clinical Studeis , clinical studies , CSIR-UGC-NET , Diseases , Examination gallary , Food Science , GATE

Italian and U.S. biologists have report that a little-understood protein previously implicated in a rare genetic disorder plays an unexpected and critical role in building and maintaining healthy cells. Even more surprising, their report in the journal Nature shows that the protein, called "atlastin," does its work by fusing intracellular membranes in a previously undocumented way.

"If you'd asked me a year ago whether this was possible, I would have said, 'No,'" said study co-author James McNew, associate professor of biochemistry and cell biology at Rice University. "In fact, that's exactly what I told (co-author) Andrea Daga when we first spoke about the idea a year ago."

McNew has spent the past 15 years studying SNARE proteins, a specialized family of proteins that carries out membrane fusion. It's a vital process that happens thousands of times a second in every cell of our bodies.

"It is fitting that the discovery of a new protein capable of fusing membranes comes 10 years after the demonstration that SNAREs can fuse lipid bilayers," said Daga, a researcher at the Eugenio Medea Scientific Institute in Conegliano, Italy.

In the new study, Daga's and McNew's research teams used fruit flies to study how atlastin functions. The atlastin in fruit flies is very similar to the human version of the protein and serves the same function.

"Prior to this, there were only two defined ways in which you could take biological membranes and put them together in a specific way," said McNew, a faculty investigator at Rice's BioScience Resesarch Collaborative. "Atlastin is the third, and it's the only one that requires enzymatic activity, so it's distinctly different."

Using a range of tests on purified proteins, live fruit flies and cell cultures, the Italian and U.S. teams examined the effect of both an overabundance and a scarcity of atlastin on cell function and on fruit fly development. They also created mutant versions of the protein to see how it functioned -- or failed to function -- when some parts were disabled.

The tests showed that cells with extra atlastin had an overdeveloped endoplasmic reticulum (ER), a system of interconnected membrane tubes and chambers that's critical for normal cell function. The tests also showed too little atlastin led to a fragmented ER. Flies with defective atlastin were sterile and short-lived.

"The endoplasmic reticulum is an ever-changing environment," McNew said. "It grows. It retracts. It expands. It collapses. It's highly dynamic, and for that to be the case, there has to be a mechanism by which it can grow new pieces and connect those pieces together. That's where the fusion comes in."

Daga said the discovery will lay the foundation for a deeper understanding of both basic biological processes and disease.

"We hope the findings lead to a better understanding of hereditary spastic paraplegia (HSP), the genetic disorder that atlastin has been linked with," Daga said.

HSP is a rare genetic condition that affects fewer than one million people worldwide. It's marked by a partial paralysis of the lower extremities due to defects in the body's longest cells, the neurons that run from the spine through the legs.

Daga said atlastin's role in building and maintaining a healthy ER may help HSP researchers better understand why neurons are affected first.

"This is the first clue," Daga said. "We have the definition of what the protein does. Now we need to explore how it does that, and what it means."

Co-authors include Genny Orso, Diana Pendin, Jessica Tosetto and Andrea Martinuzzi, all of Eugenio Medea Scientific Institute; Song Liu, Tyler Moss and Joseph Faust, all of Rice; Anastasia Egorova of Consorzio Mario Negri Sud in Santa Maria Imbaro, Italy; and Massimo Micaroni, now of the University of Queensland in Brisbane, Australia.

The research was supported by the National Institutes of Health, the G. Harold and Leila Mathers Charitable Foundation, Telethon Italy, the Italian Ministry of Health and the Foundation Compagnia di San Paolo