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It's final. A decade after the Sars outbreak killed close to 800 people worldwide, scientists have fingered bats as the original carriers, or "reservoirs", of the disease that later jumped to humans.

They are also the likely culprits behind the deadly Mers (Middle East Respiratory Syndrome) virus sweeping the region.

Singapore scientist Wang Linfa, a key member of the research project, is convinced that bats will be the source of another infectious disease outbreak.

"I am almost certain that in the next 10 years, a new killer virus spread by bats will emerge," said Professor Wang, director of the Emerging Infectious Diseases programme at Duke-NUS Graduate Medical School Singapore.

You can bet on it

"I am almost certain that in the next 10 years, a new killer virus spread by bats will emerge."

PROFESSOR WANG LINFA, director of the Emerging Infectious Diseases programme at Duke-NUS Graduate Medical School Singapore

BATS: LONG-LIVING AND VIRUS-RESISTANT

They have existed alongside dinosaurs, and are among the most abundant and widespread mammals on Earth.

Bats are good hosts for diseases which skip the species barrier and infect people. They carry pathogens ranging from measles, mumps, pneumonias and colds, to the deadly Hendra, Nipah and Ebola viruses.

More here:
Bats are original carriers of Sars virus: Research

November 30, 2013

redOrbit Staff & Wire Reports Your Universe Online

A hepatitis C vaccine is one step closer thanks to the efforts of scientists at The Scripps Research Institute (TSRI), who have managed to discover unexpected structural features of a protein used by the virus to infect liver cells.

The study authors, whose work appears in Fridays edition of the journal Science, state any successful hepatitis C vaccine would most likely target this protein, which is known as E2 envelope glycoprotein. Rare antibodies capable of binding E2 in ways that can neutralize a vast array of different viral strains have already been isolated in patients by scientists, they added.

Were excited by this development, senior author Dr. Ian A. Wilson, the Hansen Professor of Structural Biology at TSRI, said in a statement. He added that it took him and his TSRI colleagues Dr. Mansun Law and Dr. Andrew B. Ward six years of painstaking work to complete a high resolution structure of the protein. They now intend to create vaccines that can mimic the structural details of those binding sites.

According to the Institute, the global spread of hepatitis C has resulted in a desperate need for an effective vaccine against the virus. The pathogen, which was once geographically isolated, has found its way throughout the world, primarily due to blood transfusions, the use of unsterilized medical equipment and the re-use of hypodermic needles. While hospitals have screened for the virus for approximately two decades, there are believed to be up to 200 million people worldwide infected with hepatitis C, including over three million in the US alone.

HCV was able to spread so widely because it typically causes few or no symptoms when it infects someone. In many cases it establishes a long-term infection of the liver, damaging it slowly for decades until liver cirrhosis and/or cancer develop, TSRI explained. The research was funded in part by the National Institutes of Health and the Skaggs Institute of Chemical Biology.

The disease, which according to Law is a silent killer, is typically fatal unless a patient undergoes a costly and high-risk liver transplantation procedure. Some antiviral medications can treat and even cure chronic hepatitis C infection, but the most effective ones are extremely expensive, and often those who are infected do not realize they have the virus and require medical attention. A vaccine could prevent new infections, ending the pandemic.

It could be given to people when theyre young and healthy, and theyd never have to worry about developing HCV-related liver diseases, Ward said. However, unlike HIV and other viruses, hepatitis C utilizes several different effective countermeasures to evade an immune system, including rapidly-mutating regions on the E2 protein that makes sure antibodies that are effective against one strain are not ineffective against others.

The TSRI researchers set out to analyze the high-resolution atomic structure of the virus in order to help overcome these countermeasures. However, according to the study authors, that has been a difficult task to attempt, let alone complete. It took dozens of experiments to find the right way to modify E2, making it so the protein aggregates less readily while making sure that its antibody-binding sites are maintained. Ward called it a Herculean effort because hepatitis C is one of the most difficult and unstable viral envelope proteins around.

Here is the original post:
Protein Analysis Could Lead To Hepatitis C Vaccine

Newswise LA JOLLA, CANovember 28, 2013Scientists at The Scripps Research Institute (TSRI) have determined the most detailed picture yet of a crucial part of the hepatitis C virus, which the virus uses to infect liver cells. The new data reveal unexpected structural features of this protein and should greatly speed efforts to make an effective hepatitis C vaccine.

The findings, which appear in the November 29, 2013 issue of the journal Science, focus on a protein known as E2 envelope glycoprotein.

Were excited by this development, said Ian A. Wilson, the Hansen Professor of Structural Biology at TSRI and a senior author of the new research with TSRI Assistant Professors Mansun Law and Andrew B. Ward. It has been very hard to get a high resolution structure of E2 and it took years of painstaking work to finally accomplish that.

Any successful hepatitis C vaccine is likely to target the E2 protein. Scientists already have isolated rare antibodies from patients that can bind E2 in ways that neutralize a broad range of viral strains.

It took our team six years to crack this very difficult scientific problem, but we didnt give up, said Law. Now that we can visualize the structural details of these binding sites, we can design vaccine molecules that mimic them.

A Silent Killer

There has long been an urgent need for an effective vaccine against hepatitis C virus. Once confined to isolated geographical regions, the virus spread globally during the 20th century, chiefly via blood transfusions, unsterilized medical instruments and re-used hypodermic needles. Although hospitals have screened blood products for hepatitis C virus (HCV) since the early 1990s, as many as 200 million people currently are thought to harbor the virus. These include more than 3 million people in the United States, where the virus is responsible for more deaths each year than HIV.

HCV was able to spread so widely because it typically causes few or no symptoms when it infects someone. In many cases it establishes a long-term infection of the liver, damaging it slowly for decadesuntil liver cirrhosis and/or cancer develop. Its known as a silent killer, said Law. Expensive and risky liver transplantation is often the only way to save a patients life. Some antiviral drugs are useful in treating and even curing chronic HCV infection, but the more effective ones are extremely expensiveand most HCV-positive people dont even know that theyre infected and need treatment.

An HCV vaccine could put an end to the global pandemic by preventing new infections. It could be given to people when theyre young and healthy, and theyd never have to worry about developing HCV-related liver diseases, said Ward.

However, like HIV and some other viruses, HCV uses several effective countermeasures to evade the immune system. These include fast-mutating regions on the E2 protein, which ensure that antibodies to one HCV strain typically are ineffective against other strains. The E2 protein also coats itself with relatively antibody-proof sugar molecules.

Link:
Scripps Research Institute Scientists Achieve Most Detailed Picture Ever of Key Part of Hepatitis C Virus

Nov. 28, 2013 Scientists at The Scripps Research Institute (TSRI) have determined the most detailed picture yet of a crucial part of the hepatitis C virus, which the virus uses to infect liver cells. The new data reveal unexpected structural features of this protein and should greatly speed efforts to make an effective hepatitis C vaccine.

The findings, which appear in the November 29, 2013 issue of the journal Science, focus on a protein known as E2 envelope glycoprotein.

"We're excited by this development," said Ian A. Wilson, the Hansen Professor of Structural Biology at TSRI and a senior author of the new research with TSRI Assistant Professors Mansun Law and Andrew B. Ward. "It has been very hard to get a high resolution structure of E2 and it took years of painstaking work to finally accomplish that."

Any successful hepatitis C vaccine is likely to target the E2 protein. Scientists already have isolated rare antibodies from patients that can bind E2 in ways that neutralize a broad range of viral strains.

"It took our team six years to crack this very difficult scientific problem, but we didn't give up," said Law. "Now that we can visualize the structural details of these binding sites, we can design vaccine molecules that mimic them."

A Silent Killer

There has long been an urgent need for an effective vaccine against hepatitis C virus. Once confined to isolated geographical regions, the virus spread globally during the 20th century, chiefly via blood transfusions, unsterilized medical instruments and re-used hypodermic needles. Although hospitals have screened blood products for hepatitis C virus (HCV) since the early 1990s, as many as 200 million people currently are thought to harbor the virus. These include more than 3 million people in the United States, where the virus is responsible for more deaths each year than HIV.

HCV was able to spread so widely because it typically causes few or no symptoms when it infects someone. In many cases it establishes a long-term infection of the liver, damaging it slowly for decades -- until liver cirrhosis and/or cancer develop. "It's known as a 'silent killer'," said Law. Expensive and risky liver transplantation is often the only way to save a patient's life. Some antiviral drugs are useful in treating and even curing chronic HCV infection, but the more effective ones are extremely expensive -- and most HCV-positive people don't even know that they're infected and need treatment.

An HCV vaccine could put an end to the global pandemic by preventing new infections. "It could be given to people when they're young and healthy, and they'd never have to worry about developing HCV-related liver diseases," said Ward.

However, like HIV and some other viruses, HCV uses several effective countermeasures to evade the immune system. These include fast-mutating regions on the E2 protein, which ensure that antibodies to one HCV strain typically are ineffective against other strains. The E2 protein also coats itself with relatively antibody-proof sugar molecules.

Here is the original post:
Scientists achieve most detailed picture ever of key part of hepatitis C virus

Posted on: 4:42 pm, November 20, 2013, by Shain Bergan, updated on: 07:45pm, November 21, 2013

A link between the Facebook profiles of an accused child killer and a man suspected of unlawfully spreading HIV implies the two may be brothers.

Joseph Frank Blackmon, the Bentonville man arrested last month in an HIV crime case, lists on his Facebook page a Joe Blackmon of Bakersfield, Calif., as his father.

Meanwhile, on his own Facebook page, the Joe Blackmon in California lists Jersey Bridgemans accused killer, Zachary Holly, as his son.

Implications from the Facebook references that the two are brothers could not be immediately confirmed.

The 48-year-old Joe Blackmon is also listed as a sex offender in Bakersfield, Calif., the same city Joseph Blackmon and Holly list as their hometown on Facebook. Joe Blackmons name also appeared on the utility bill at the Bentonville house where Holly was arrested last year in the Bridgeman murder investigation, records show.

Holly and Joseph Blackmon remain in the Benton County Jail following their arrests. Holly faces charges of rape and capital murder of six-year-old Jersey Bridgeman, a Bentonville girl found dead in an abandoned house near her home last November. He is being held without bond and has a trial set for April.

Blackmon was arrested Oct. 9, but remains in jail on $40,000 bond, according to the Benton County Sheriffs Office. He faces charges of exposing another person to human immunodeficiency virus, public sexual indecency, possession of a controlled substance and possession of drug paraphernalia.

Police said Blackmon was caught having sex with another man in a Cave Springs cul-de-sac, after which it was allegedly revealed Blackmon has HIV and did not tell his sexual partner. An officer also found methamphetamine on Blackmon during the incident, police said.

Police said a Cave Springs officer caught Blackmon and another man likely engaging in sex acts in a parked car in a local cul-de-sac. After talking with the officer, Blackmon pulled methamphetamine out of his sock and gave it to the officer, while telling him his sexual partner did not know he was HIV-positive, according to a probable cause affidavit filed in Benton County Circuit Court.

Read more:
Facebook Links Suspected Child Killer To HIV-Crime Suspect