Microsatellite DNA analysis reveals genetic change of P. vivax in Korea, 2002-2003

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Contact: Ryouhei Nishigaya
rnishiga@hosp.ncgm.go.jp
Public Library of Science

Continual reintroduction of P. vivax from North Korea could be the cause of change

Malaria is one of the major infectious diseases transmitted by mosquitos, with enormous impact on quality of life. According to World Health Organization figures, as of 2010 there were over 219 million reported cases of malaria with an estimated 660,000 deaths. Plasmodium vivax, which is the second most prevalent species of the human malaria parasite, is widely distributed around the world especially in Asia, Melanesia, the Middle East, South and Central America. 2.85 billion people worldwide live at risk of the infection in 2009.

Vivax malaria was once endemic in Japan including the mainland (Honshu) and the northern island (Hokkaido), but it has been eliminated from these areas as of 1959. In the same way as Japan, the Republic of Korea (South Korea) is another country where vivax malaria had been successfully eliminated by the late 1970s. However, re-emergence of vivax malaria in South Korea was reported in 1993. The first patient was a South Korean soldier who served in the demilitarized zone (a border region between South and North Korea) and had never been abroad. In spite of continuous malaria control measures implemented by the South Korean government, there was a steady increase in the number of reported vivax malaria cases until 2000 (4,183 cases), then a gradual decrease until 2004 (864 cases), when the number of infected civilians who lived in or near the area increased gradually. The number of reported cases fluctuated between 838 and 2,227 per year from 2005 to 2011.

Similarities in the ecology (i.e., climate, vegetation, species of mosquito vector) of Japan and South Korea mean that the Japanese environment is particularly suited to the establishment of Korean strains of vivax malaria. For example, the main vector species of vivax malaria in South Korea is Anopheles sinensis, which in the past has also been the main vector species of vivax malaria in the mainland of Japan, and which remains distributed throughout Japan. In addition, mosquitoes on the mainland of Japan are highly prevalent from June to September (the rainy season and the summer season), which is the same period in which vivax malaria is most prevalent in South Korea.

For these reasons, it is very important not only for South Korea, but also for Japan, to understand the characteristics of vivax malaria in South Korea and to provide a possible explanation as to why, in spite of a continuous malaria control program spanning two decades, efforts to eliminate vivax malaria have been unsuccessful. To answer this question, Dr. Moritoshi Iwagami, et al. conducted a 15-year-long longitudinal study on P. vivax population genetics in South Korea using highly polymorphic neutral markers of the parasites.

The team of researchers from the Japanese National Center for Global Health and Medicine, Inje University and the University of Tokyo analyzed 163 South Korean P. vivax isolates collected from South Korean soldiers who served in the demilitarized zone from 1994 to 2008, using 14 microsatellite DNA loci of the parasite genome. Based on this data, they performed population genetic analysis, with a focus on the differences of the parasite populations between successive years. Through this, they aimed to provide a detailed and precise estimate of the characteristics of the vivax malaria population structure and the temporal dynamics of its transmission.

Their population genetic analyses show that two genotypes coexisted from 1994 to 2001, while three different genotypes coexisted from 2002 to 2008. This result suggested that a drastic genetic change occurred in the South Korean population during 2002 and 2003.

This data suggests that vivax parasites were introduced from another population, most probably from North Korea, especially during 2002 and 2003, and explains why South Korea was not able to eliminate vivax malaria for 20 years. The finding is an example that malaria parasites were transmitted by Anopheles mosquitos between two countries where traveling is basically prohibited. This evidence demonstrates the difficulty of malaria elimination by one country and the need for collaboration between two (or more) adjacent countries for effective malaria elimination.

In the (near) future, a distribution of Anopheles mosquitoes might expand in Japan due to global warming or climate change. Should a certain numbers of vivax malaria patients (and/or carriers of vivax malaria hypnozoites) come to Japan from South Korea and stay in or near A. sinensis breeding sites during summer season, indigenous vivax malaria transmission might occur by locally infected mosquitoes in Japan. Therefore, careful monitoring of all travelers coming from endemic areas of South Korea is required, as is collaboration between both nations in order to prevent the introduction of the malaria parasite into Japan.

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Contact: Ryouhei Nishigaya
rnishiga@hosp.ncgm.go.jp
Public Library of Science

Continual reintroduction of P. vivax from North Korea could be the cause of change

Malaria is one of the major infectious diseases transmitted by mosquitos, with enormous impact on quality of life. According to World Health Organization figures, as of 2010 there were over 219 million reported cases of malaria with an estimated 660,000 deaths. Plasmodium vivax, which is the second most prevalent species of the human malaria parasite, is widely distributed around the world especially in Asia, Melanesia, the Middle East, South and Central America. 2.85 billion people worldwide live at risk of the infection in 2009.

Vivax malaria was once endemic in Japan including the mainland (Honshu) and the northern island (Hokkaido), but it has been eliminated from these areas as of 1959. In the same way as Japan, the Republic of Korea (South Korea) is another country where vivax malaria had been successfully eliminated by the late 1970s. However, re-emergence of vivax malaria in South Korea was reported in 1993. The first patient was a South Korean soldier who served in the demilitarized zone (a border region between South and North Korea) and had never been abroad. In spite of continuous malaria control measures implemented by the South Korean government, there was a steady increase in the number of reported vivax malaria cases until 2000 (4,183 cases), then a gradual decrease until 2004 (864 cases), when the number of infected civilians who lived in or near the area increased gradually. The number of reported cases fluctuated between 838 and 2,227 per year from 2005 to 2011.

Similarities in the ecology (i.e., climate, vegetation, species of mosquito vector) of Japan and South Korea mean that the Japanese environment is particularly suited to the establishment of Korean strains of vivax malaria. For example, the main vector species of vivax malaria in South Korea is Anopheles sinensis, which in the past has also been the main vector species of vivax malaria in the mainland of Japan, and which remains distributed throughout Japan. In addition, mosquitoes on the mainland of Japan are highly prevalent from June to September (the rainy season and the summer season), which is the same period in which vivax malaria is most prevalent in South Korea.

For these reasons, it is very important not only for South Korea, but also for Japan, to understand the characteristics of vivax malaria in South Korea and to provide a possible explanation as to why, in spite of a continuous malaria control program spanning two decades, efforts to eliminate vivax malaria have been unsuccessful. To answer this question, Dr. Moritoshi Iwagami, et al. conducted a 15-year-long longitudinal study on P. vivax population genetics in South Korea using highly polymorphic neutral markers of the parasites.

The team of researchers from the Japanese National Center for Global Health and Medicine, Inje University and the University of Tokyo analyzed 163 South Korean P. vivax isolates collected from South Korean soldiers who served in the demilitarized zone from 1994 to 2008, using 14 microsatellite DNA loci of the parasite genome. Based on this data, they performed population genetic analysis, with a focus on the differences of the parasite populations between successive years. Through this, they aimed to provide a detailed and precise estimate of the characteristics of the vivax malaria population structure and the temporal dynamics of its transmission.

Their population genetic analyses show that two genotypes coexisted from 1994 to 2001, while three different genotypes coexisted from 2002 to 2008. This result suggested that a drastic genetic change occurred in the South Korean population during 2002 and 2003.

This data suggests that vivax parasites were introduced from another population, most probably from North Korea, especially during 2002 and 2003, and explains why South Korea was not able to eliminate vivax malaria for 20 years. The finding is an example that malaria parasites were transmitted by Anopheles mosquitos between two countries where traveling is basically prohibited. This evidence demonstrates the difficulty of malaria elimination by one country and the need for collaboration between two (or more) adjacent countries for effective malaria elimination.

In the (near) future, a distribution of Anopheles mosquitoes might expand in Japan due to global warming or climate change. Should a certain numbers of vivax malaria patients (and/or carriers of vivax malaria hypnozoites) come to Japan from South Korea and stay in or near A. sinensis breeding sites during summer season, indigenous vivax malaria transmission might occur by locally infected mosquitoes in Japan. Therefore, careful monitoring of all travelers coming from endemic areas of South Korea is required, as is collaboration between both nations in order to prevent the introduction of the malaria parasite into Japan.

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Source: http://www.eurekalert.org/pub_releases/2013-10/plos-mda102913.php
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Scientists capture most detailed picture yet of key AIDS protein

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Contact: Sarah Smith
sas2072@med.cornell.edu
646-317-7401
Weill Cornell Medical College

Finding represents a scientific feat and progress towards an HIV vaccine

NEW YORK (October 31, 2013) -- Collaborating scientists at The Scripps Research Institute (TSRI) and Weill Cornell Medical College have determined the first atomic-level structure of the tripartite HIV envelope protein -- long considered one of the most difficult targets in structural biology and of great value for medical science.

The new data provide the most detailed picture yet of the AIDS-causing virus's complex envelope, including sites that future vaccines will try to mimic to elicit a protective immune response.

"Most of the prior structural studies of this envelope complex focused on individual subunits, but we've needed the structure of the full complex to properly define the sites of vulnerability that could be targeted, for example with a vaccine," said Dr. Ian A. Wilson, the Hansen Professor of Structural Biology at TSRI and a senior author of the new research with biologists Drs. Andrew Ward and Bridget Carragher of TSRI and virologist and immunologist Dr. John Moore of Weill Cornell.

The findings were published in two papers in Science Express, the early online edition of the journal Science, on October 31, 2013.

A Difficult Target

HIV, the human immunodeficiency virus, infects about 34 million people globally, 10 percent of whom are children, according to World Health Organization estimates. Although antiviral drugs are now used to manage many HIV infections, especially in developed countries, scientists have long sought a vaccine that can prevent new infections and would help perhaps to ultimately eradicate the virus from the human population.

However, none of the HIV vaccines tested so far has come close to providing adequate protection. This failure is due largely to the challenges posed by HIV's envelope protein, known to virologists as Env.

HIV's Env is not a single, simple protein but rather a "trimer" made of three identical, loosely connected structures with a stalk-like subunit, gp41, and a cap-like region, gp120. Each trimer resembles a mushroom and about 15 of these Env trimers sprout from the membrane of a typical virus particle, ready to latch onto susceptible human cells and facilitate viral entry.

Although Env in principle is exposed to the immune system, in practice it has evolved highly effective strategies for evading immune attack. It frequently mutates its outermost "variable loop" regions, for example, and also coats its surfaces with hard-to-grip sugar molecules called glycans.

Even so, HIV vaccine designers might have succeeded by now had they been able to study the structure of the entire Env protein at atomic-scale--in particular, to fully characterize the sites where the most effective virus-neutralizing antibodies bind. But Env's structure is so complex and delicate that scientists have had great difficulty obtaining the protein in a form that is suitable for atomic-resolution imaging.

"It tends to fall apart, for example, even when it's on the surface of the virus, so to study it we have to engineer it to be more stable," said Dr. Ward, who is an assistant professor in TSRI's Department of Integrative Structural and Computational Biology.
The key goal in this area has been to engineer a version of the Env trimer that has the stability and other properties needed for atomic-resolution imaging, yet retains virtually all of the complex structural characteristics of native Env.

Imaging Env

After many years in pursuit of this goal, Drs. Moore, Rogier W. Sanders and their colleagues at Weill Cornell, working with Drs. Wilson, Ward and others at TSRI, recently managed to produce a version of the Env trimer (called BG505 SOSIP.664 gp140) that is suitable for atomic-level imaging work--and includes all of the trimer structure that normally sits outside the viral membrane. The TSRI researchers then evaluated the new Env trimer using advanced versions of two imaging methods, X-ray crystallography and electron microscopy. The X-ray crystallography study was the first ever of an Env trimer, and both methods resolved the trimer structure to a finer level of detail than has been reported before.

"The new data are consistent with the findings on Env subunits over the last 15 years, but also have enabled us to explain many prior observations about HIV in structural terms for the first time," said Dr. Jean-Philippe Julien, a senior research associate in the Wilson laboratory at TSRI, who was first author of the X-ray crystallography study.

The data illuminated the complex process by which the Env trimer assembles and later undergoes radical shape changes during infection and clarified how it compares to envelope proteins on other dangerous viruses, such as flu and Ebola.

Arguably the most important implications of the new findings are for HIV vaccine design. In both of the new studies, Env trimers were imaged while bound to broadly neutralizing antibodies against HIV. Such antibodies, isolated from naturally infected patients, are the very rare ones that somehow bind to Env in a way that blocks the infectivity of a high proportion of HIV strains.

Ideally an HIV vaccine would elicit large numbers of such antibodies from patients, and to achieve that, vaccine designers would like to know the precise structural details of the sites where these antibodies bind to the virus--so that they can mimic those viral "epitopes" with the vaccine.

"It's been a privilege for us to work with the Scripps' team on this project," said Dr. Moore, a professor of microbiology and immunology at Weill Cornell. "Now we all need to harness this new knowledge to design and test next-generation trimers and see if we can induce the broadly active neutralizing antibodies that an effective vaccine is going to need."

"One surprise from this study was the revelation of the complexity and the relative inaccessibility of these neutralizing epitopes," Dr. Julien added. "It helps to know this for future vaccine design, but it also makes it clear why previous structure-based HIV vaccines have had so little success."

"We found that these neutralizing epitopes encompass features such as the variable loop regions and glycans that were excluded from previous studies of individual Env subunits," said Dmitry Lyumkis, first author of the electron microscopy study, who is a graduate student at TSRI participating in the NIH-funded National Resource for Automated Molecular Microscopy. "We observed, too, that neutralizing antibody binding to gp120 can be influenced by the neighboring gp120 structure within the trimer--another complication that was not apparent when we were not studying the whole trimer."

Having provided these valuable structural insights, the new Env trimer is now being put to work in vaccine development. "We and others are already injecting the trimer into animals to elicit antibodies," Dr. Ward said. "We can look at the antibodies that are generated and if necessary modify the Env trimer structure and try again. In this iterative way, we aim to refine and increase the antibody response in the animals and eventually, humans."

###

Other contributors to the studies, "Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 Env trimer," and "Crystal structure of a soluble cleaved HIV-1 envelope trimer in complex with a glycan-dependent broadly neutralizing antibody," included TSRI's Natalia de Val, Devin Sok, Drs. Robyn L. Stanfield and Marc C. Deller; and Weill Cornell Medical College's Albert Cupo and Dr. Per-Johan Klasse. In addition to Drs. Wilson, Ward and Carragher, senior participants at TSRI included Drs. Clinton S. Potter and Dennis Burton.

The research was supported in part by the National Institutes of Health (HIVRAD P01 AI82362, R01 AI36082, R01 AI084817, R37 AI36082, R01 AI33292), the NIH's National Institute of General Medical Sciences (GM103310) and the International AIDS Vaccine Initiative Neutralizing Antibody Consortium. IAVI has filed a patent that includes WCMC and TSRI authors on the development of the BG505 SOSIP.664 trimers as vaccine antigens.

Weill Cornell Medical College

Weill Cornell Medical College, Cornell University's medical school located in New York City, is committed to excellence in research, teaching, patient care and the advancement of the art and science of medicine, locally, nationally and globally. Physicians and scientists of Weill Cornell Medical College are engaged in cutting-edge research from bench to bedside, aimed at unlocking mysteries of the human body in health and sickness and toward developing new treatments and prevention strategies. In its commitment to global health and education, Weill Cornell has a strong presence in places such as Qatar, Tanzania, Haiti, Brazil, Austria and Turkey. Through the historic Weill Cornell Medical College in Qatar, the Medical College is the first in the U.S. to offer its M.D. degree overseas. Weill Cornell is the birthplace of many medical advances -- including the development of the Pap test for cervical cancer, the synthesis of penicillin, the first successful embryo-biopsy pregnancy and birth in the U.S., the first clinical trial of gene therapy for Parkinson's disease, and most recently, the world's first successful use of deep brain stimulation to treat a minimally conscious brain-injured patient. Weill Cornell Medical College is affiliated with NewYork-Presbyterian Hospital, where its faculty provides comprehensive patient care at NewYork-Presbyterian Hospital/Weill Cornell Medical Center. The Medical College is also affiliated with Houston Methodist. For more information, visit weill.cornell.edu.

Office of External Affairs

Weill Cornell Medical College

tel: 646.317.7401

email: pr@med.cornell.edu

Follow WCMC on Twitter and Facebook

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AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.

PUBLIC RELEASE DATE:

31-Oct-2013

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Contact: Sarah Smith
sas2072@med.cornell.edu
646-317-7401
Weill Cornell Medical College

Finding represents a scientific feat and progress towards an HIV vaccine

NEW YORK (October 31, 2013) -- Collaborating scientists at The Scripps Research Institute (TSRI) and Weill Cornell Medical College have determined the first atomic-level structure of the tripartite HIV envelope protein -- long considered one of the most difficult targets in structural biology and of great value for medical science.

The new data provide the most detailed picture yet of the AIDS-causing virus's complex envelope, including sites that future vaccines will try to mimic to elicit a protective immune response.

"Most of the prior structural studies of this envelope complex focused on individual subunits, but we've needed the structure of the full complex to properly define the sites of vulnerability that could be targeted, for example with a vaccine," said Dr. Ian A. Wilson, the Hansen Professor of Structural Biology at TSRI and a senior author of the new research with biologists Drs. Andrew Ward and Bridget Carragher of TSRI and virologist and immunologist Dr. John Moore of Weill Cornell.

The findings were published in two papers in Science Express, the early online edition of the journal Science, on October 31, 2013.

A Difficult Target

HIV, the human immunodeficiency virus, infects about 34 million people globally, 10 percent of whom are children, according to World Health Organization estimates. Although antiviral drugs are now used to manage many HIV infections, especially in developed countries, scientists have long sought a vaccine that can prevent new infections and would help perhaps to ultimately eradicate the virus from the human population.

However, none of the HIV vaccines tested so far has come close to providing adequate protection. This failure is due largely to the challenges posed by HIV's envelope protein, known to virologists as Env.

HIV's Env is not a single, simple protein but rather a "trimer" made of three identical, loosely connected structures with a stalk-like subunit, gp41, and a cap-like region, gp120. Each trimer resembles a mushroom and about 15 of these Env trimers sprout from the membrane of a typical virus particle, ready to latch onto susceptible human cells and facilitate viral entry.

Although Env in principle is exposed to the immune system, in practice it has evolved highly effective strategies for evading immune attack. It frequently mutates its outermost "variable loop" regions, for example, and also coats its surfaces with hard-to-grip sugar molecules called glycans.

Even so, HIV vaccine designers might have succeeded by now had they been able to study the structure of the entire Env protein at atomic-scale--in particular, to fully characterize the sites where the most effective virus-neutralizing antibodies bind. But Env's structure is so complex and delicate that scientists have had great difficulty obtaining the protein in a form that is suitable for atomic-resolution imaging.

"It tends to fall apart, for example, even when it's on the surface of the virus, so to study it we have to engineer it to be more stable," said Dr. Ward, who is an assistant professor in TSRI's Department of Integrative Structural and Computational Biology.
The key goal in this area has been to engineer a version of the Env trimer that has the stability and other properties needed for atomic-resolution imaging, yet retains virtually all of the complex structural characteristics of native Env.

Imaging Env

After many years in pursuit of this goal, Drs. Moore, Rogier W. Sanders and their colleagues at Weill Cornell, working with Drs. Wilson, Ward and others at TSRI, recently managed to produce a version of the Env trimer (called BG505 SOSIP.664 gp140) that is suitable for atomic-level imaging work--and includes all of the trimer structure that normally sits outside the viral membrane. The TSRI researchers then evaluated the new Env trimer using advanced versions of two imaging methods, X-ray crystallography and electron microscopy. The X-ray crystallography study was the first ever of an Env trimer, and both methods resolved the trimer structure to a finer level of detail than has been reported before.

"The new data are consistent with the findings on Env subunits over the last 15 years, but also have enabled us to explain many prior observations about HIV in structural terms for the first time," said Dr. Jean-Philippe Julien, a senior research associate in the Wilson laboratory at TSRI, who was first author of the X-ray crystallography study.

The data illuminated the complex process by which the Env trimer assembles and later undergoes radical shape changes during infection and clarified how it compares to envelope proteins on other dangerous viruses, such as flu and Ebola.

Arguably the most important implications of the new findings are for HIV vaccine design. In both of the new studies, Env trimers were imaged while bound to broadly neutralizing antibodies against HIV. Such antibodies, isolated from naturally infected patients, are the very rare ones that somehow bind to Env in a way that blocks the infectivity of a high proportion of HIV strains.

Ideally an HIV vaccine would elicit large numbers of such antibodies from patients, and to achieve that, vaccine designers would like to know the precise structural details of the sites where these antibodies bind to the virus--so that they can mimic those viral "epitopes" with the vaccine.

"It's been a privilege for us to work with the Scripps' team on this project," said Dr. Moore, a professor of microbiology and immunology at Weill Cornell. "Now we all need to harness this new knowledge to design and test next-generation trimers and see if we can induce the broadly active neutralizing antibodies that an effective vaccine is going to need."

"One surprise from this study was the revelation of the complexity and the relative inaccessibility of these neutralizing epitopes," Dr. Julien added. "It helps to know this for future vaccine design, but it also makes it clear why previous structure-based HIV vaccines have had so little success."

"We found that these neutralizing epitopes encompass features such as the variable loop regions and glycans that were excluded from previous studies of individual Env subunits," said Dmitry Lyumkis, first author of the electron microscopy study, who is a graduate student at TSRI participating in the NIH-funded National Resource for Automated Molecular Microscopy. "We observed, too, that neutralizing antibody binding to gp120 can be influenced by the neighboring gp120 structure within the trimer--another complication that was not apparent when we were not studying the whole trimer."

Having provided these valuable structural insights, the new Env trimer is now being put to work in vaccine development. "We and others are already injecting the trimer into animals to elicit antibodies," Dr. Ward said. "We can look at the antibodies that are generated and if necessary modify the Env trimer structure and try again. In this iterative way, we aim to refine and increase the antibody response in the animals and eventually, humans."

###

Other contributors to the studies, "Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 Env trimer," and "Crystal structure of a soluble cleaved HIV-1 envelope trimer in complex with a glycan-dependent broadly neutralizing antibody," included TSRI's Natalia de Val, Devin Sok, Drs. Robyn L. Stanfield and Marc C. Deller; and Weill Cornell Medical College's Albert Cupo and Dr. Per-Johan Klasse. In addition to Drs. Wilson, Ward and Carragher, senior participants at TSRI included Drs. Clinton S. Potter and Dennis Burton.

The research was supported in part by the National Institutes of Health (HIVRAD P01 AI82362, R01 AI36082, R01 AI084817, R37 AI36082, R01 AI33292), the NIH's National Institute of General Medical Sciences (GM103310) and the International AIDS Vaccine Initiative Neutralizing Antibody Consortium. IAVI has filed a patent that includes WCMC and TSRI authors on the development of the BG505 SOSIP.664 trimers as vaccine antigens.

Weill Cornell Medical College

Weill Cornell Medical College, Cornell University's medical school located in New York City, is committed to excellence in research, teaching, patient care and the advancement of the art and science of medicine, locally, nationally and globally. Physicians and scientists of Weill Cornell Medical College are engaged in cutting-edge research from bench to bedside, aimed at unlocking mysteries of the human body in health and sickness and toward developing new treatments and prevention strategies. In its commitment to global health and education, Weill Cornell has a strong presence in places such as Qatar, Tanzania, Haiti, Brazil, Austria and Turkey. Through the historic Weill Cornell Medical College in Qatar, the Medical College is the first in the U.S. to offer its M.D. degree overseas. Weill Cornell is the birthplace of many medical advances -- including the development of the Pap test for cervical cancer, the synthesis of penicillin, the first successful embryo-biopsy pregnancy and birth in the U.S., the first clinical trial of gene therapy for Parkinson's disease, and most recently, the world's first successful use of deep brain stimulation to treat a minimally conscious brain-injured patient. Weill Cornell Medical College is affiliated with NewYork-Presbyterian Hospital, where its faculty provides comprehensive patient care at NewYork-Presbyterian Hospital/Weill Cornell Medical Center. The Medical College is also affiliated with Houston Methodist. For more information, visit weill.cornell.edu.

Office of External Affairs

Weill Cornell Medical College

tel: 646.317.7401

email: pr@med.cornell.edu

Follow WCMC on Twitter and Facebook

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Source: http://www.eurekalert.org/pub_releases/2013-10/wcmc-scm103113.php
Category: tlc   liam hemsworth   Kelly LeBrock   powerball winning numbers   Demi Lovato  

iMore show LIVE! 8am PT, 11am ET - Join us!

Join Peter, Richard, and me for the live version of our iPad Air and iPad mini buyers guide! We'll be talking through upgrading, which models to get, how they compare, choosing the right capacity, color, and carrier, and more!

Source: http://feedproxy.google.com/~r/TheIphoneBlog/~3/Na8Jp2YOKeQ/story01.htm
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Oracle, Red Hat, And Google Employees Pitch In To Fix Beleaguered Healthcare.gov, Reports Indicate

Workers from tech giants Google, Red Hat, and Oracle and other companies have reportedly joined with the government to help fix the notoriously broken Healthcare.gov website that is a key portion of the Affordable Care Act.

According to a tweet from CNBC, “experts” from the firms have been dispatched. It is not clear yet in what quantity or what their role will be. The government needs the help, and it is good to see the technology community step up. After all, this is our domain.

In a piece by Alex Wayne on BusinessWeek, Google is parting with Michael Dickerson, a “site reliability engineer.” Also according to Wayne, Greg Gershman of mobile company Mobomo is said to be taking part as well.

When the Affordable Care Act went live recently, its website, which was supposed to provide a central exchange, failed: It lagged, dropped users, and fed wrong information to insurance companies. It was a tectonically embarrassing moment for the government and the president. Later, a “tech surge” was called for. It appears that this is part of that effort.

The government has promised that the website will be functional by the end of November. That gives the Silicon Valley cavalry just a single month to get the beast back in the pen. Also unclear at the moment is why these three firms have stepped up and not others. Microsoft, Apple, Yahoo, and Twitter are other firms that could spare an engineer or two.

Private tech employees helping the public government untangle a website built in part by Canadian contractors? The leaks from this saga are going to be amazing.

This is a developing story, and this post will be updated as new information becomes available.

Top Image Credit: Flickr

Source: http://feedproxy.google.com/~r/Techcrunch/~3/V35cpL0HhrE/
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Samsung updates mobile, TV, and gaming SDKs to attract more developers

Like most other device builders, Samsung relies on Google's Android OS to power its smartphones and tablets. But not content to simply ride the Android wave, Samsung is trying to set itself apart with vendor-specific capabilities ranging from pen functionality to enterprise security, prompting the company to release its own software development kits over the last couple years.

At its first ever Samsung Developer Conference in San Francisco this week, the company unveiled several SDK updates for those proprietary capabilities currently offered on top of Android on Samsung devices and, in some cases, available for iOS applications such as its ChatOn instant messaging service or Smart TV remote-control app.

Samsung's SDKs include the updated Samsung Mobile SDK for using the S Pen input device standard on several Samsung devices, the new Knox SDK for mobile security and management, the updated ChatOn SDK for its instant messaging service, and the updated Chord SDK for one-touch discovery and pairing of devices.

Banking on the company's strength in home entertainment gear, Samsung also updated its Smart TV SDK for build applications for its Smart TV line of Internet-connected TVs and its Multiscreen gaming SDK for building games to be played on a big-screen TV via a Samsung tablet or smartphone. All but the Smart TV SDK use Android; the Smart TV SDK relies on Linux.

"They want to capture the developer, so if you use those APIs, you're on Samsung, you're not on other things," said Keithen Hayenga, a developer relations engineer at Marmalade, which enables cross-platform game development.

If successful, Samsung's efforts would yield a set of committed developers for its devices. Samsung is the largest Android smartphone manufacturer and the top smartphone maker overall. "By introducing their own SDKs and APIs, they're trying to [provide] the whole experience much like Apple tries to do with its ecosystem," said Andrew Cook, a senior software engineer for Vision Service Plan, which provides vision care benefits.

Samsung is "flexing its developer muscles," while working on both consumer and enterprise systems, said IDC analyst Al Hilwa. "On the enterprise side, the Knox platform caught my attention because it involves Samsung integrating security deeply in the OS. This is definitely evidence of the depth of R&D that they now have on Android," Hilwa said. "The other impressive set of functionality that caught my attention in the consumer world is the Smart TV SDK and the multiscreen capabilities added such as overlay of mobile device screen objects on the TV."

While emphasizing Android at the moment, Samsung also used its conference to air the latest developments for its open source Tizen OS, which Samsung is working on with Intel. Tizen features an Internet interface and supports HTML5. But the company has yet to announce a roadmap for Tizen rollouts.

This story, "Samsung updates mobile, TV, and gaming SDKs to attract more developers," was originally published at InfoWorld.com. Get the first word on what the important tech news really means with the InfoWorld Tech Watch blog. For the latest developments in business technology news, follow InfoWorld.com on Twitter.

Source: http://www.infoworld.com/t/development-tools/samsung-updates-mobile-tv-and-gaming-sdks-attract-more-developers-229946?source=rss_infoworld_blogs
Category: elizabeth olsen   Brian Hoyer   emmy awards   Pope Francis   Jason Heyward  

There's No Escaping These Pack-Hunting Soviet Assault Choppers

Sure the MI-24 Hind packs a wallop, but it's big, heavy, and cumbersome to fly. So, to penetrate enemy territory, Russia designed and built the agile and deadly Black Shark assault chopper. All it's missing is a frickin' laser.

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Source: http://feeds.gawker.com/~r/gizmodo/full/~3/mATEDLPxb08/theres-no-escaping-these-pack-hunting-soviet-assault-c-1455000802
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Time Warner Cable promises faster internet to woo back fleeing customers

One of the downsides of taking a risk is that the consequences are liable to come back and hurt you further down the line. Take Time Warner Cable, for instance, which took CBS' channels offline for the better part of two months in protest of "outrageous" carriage fees. Now that it's come to ...

Source: http://feeds.engadget.com/~r/weblogsinc/engadget/~3/x9v-IATA06Q/
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Chrome Canary now blocks recognized malware downloads

Google's stable Chrome release already has a reset tool in case malware hijacks the browser, but we're sure many would rather avoid that rogue code in the first place. Thankfully, a new build of Chrome Canary automatically blocks hostile apps. Try to download malware that Google recognizes and ...

Source: http://feeds.engadget.com/~r/weblogsinc/engadget/~3/BkCYJQn6JHo/
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