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News Article | May 19, 2017
Site: www.eurekalert.org

A custom-engineered protein destroyed the deadly virus in the lab; could become a sweeping anti-viral in medicine and farming In June 2012, a 60 year-old man with flu-like symptoms walked into a private hospital in Jeddah, Saudi Arabia. Two weeks later, he died from multiple organ failure, becoming the first victim of a mysterious virus that came to be known as Middle East Respiratory Syndrome or MERS. The World Health Organization (WHO) has identified MERS as an urgent threat with no vaccine or treatment in sight. This could change thanks to a new anti-viral tool, developed by University of Toronto researchers. Writing in the journal PLoS Pathogens, the team led by Professor Sachdev Sidhu, of the Donnelly Centre for Cellular and Biomolecular Research and Department of Molecular Genetics, describe how they turned ubiquitin, a staple protein in every cell, into a drug capable of thwarting MERS in cultured human cells. Because the technology can be applied to a wide range of pathogens, it could become a game-changer in anti-viral therapeutics with implications for human health and the farming industry. "Vaccines are important for prevention, but there is a great need for anti-viral medicines to treat people who have become infected," says Dr. Wei Zhang, a postdoctoral research fellow in Sidhu's lab who did most of the work on the study. MERS is similar to SARS, the virus that killed almost 800 people in a 2002 global epidemic. Both kill upwards of a third of people infected and, like many viruses, emerged from animals--bats and camels in the case of MERS--after mutating into a form capable of infecting human cells. Although MERS has so far been detected in 27 countries since the first case emerged in 2012, the outbreak has largely been contained within Saudi Arabia, according to the WHO. Like many viruses, MERS works by hijacking the ubiquitin system in human cells composed of hundreds of proteins that rely on ubiquitin to keep the cells alive and well. Upon infection, viral enzymes alter ubiquitin pathways in a way that allows the virus to evade the immune defense while multiplying and destroying the host tissue as it spreads in the body. "Viruses have evolved proteins that allow them to hijack host proteins. We can now devise strategies to prevent this from happening," says Zhang. Zhang and colleagues engineered the human ubiquitin protein into a new form that paralyses a key MERS enzyme, stopping the virus from replicating. These synthetic ubiquitin variants act quickly, completely eliminating MERS from cells in a dish within 24 hours. The researchers also created UbVs that blocks the Crimean-Congo virus, the cause of a haemorrhagic fever that kills about 40 per cent of those infected. And they're designed to only target only the virus -- hopefully minimizing side effects in any future drug. But before these engineered proteins can be developed into medicine, researchers first must find a way to deliver them into the right part of the body. For this, Zhang and Sidhu are working with Dr. Roman Melnyk, a biochemist in The Hospital for Sick Children and a world expert in protein delivery. The team is also investigating the possibility of finding drugs that work in a similar manner but can already cross the cell membrane. It is likely that the proteins will be tested first in plants and animals where regulatory approvals are less strict than they are for human drugs. "We are also working on an engineered ubiquitin that targets a corn virus responsible for destroying large swaths of corn fields in North America, with colleagues in Manitoba," says Zhang. In the meantime, Zhang will continue to improve delivery of his designer proteins to human cells that target not only MERS but also other viruses. He hopes others will follow suit. "With our tool, we can quickly generate anti-viral medicine and we hope that our method will inspire other researchers to try it out against diverse pathogens," says Zhang. The study was done in collaboration with Professor Marjolein Kikkert, of Leiden University Medical Centre in The Netherlands and Professor Brian Mark at the University of Manitoba.


News Article | May 22, 2017
Site: www.rdmag.com

In June 2012, a 60 year-old man with flu-like symptoms walked into a private hospital in Jeddah, Saudi Arabia. Two weeks later, he died from multiple organ failure, becoming the first victim of a mysterious virus that came to be known as Middle East Respiratory Syndrome or MERS. The World Health Organization (WHO) has identified MERS as an urgent threat with no vaccine or treatment in sight. This could change thanks to a new anti-viral tool, developed by University of Toronto researchers. Writing in the journal PLoS Pathogens, the team led by Professor Sachdev Sidhu, of the Donnelly Centre for Cellular and Biomolecular Research and Department of Molecular Genetics, describe how they turned ubiquitin, a staple protein in every cell, into a drug capable of thwarting MERS in cultured human cells. Because the technology can be applied to a wide range of pathogens, it could become a game-changer in anti-viral therapeutics with implications for human health and the farming industry. "Vaccines are important for prevention, but there is a great need for anti-viral medicines to treat people who have become infected," says Dr. Wei Zhang, a postdoctoral research fellow in Sidhu's lab who did most of the work on the study. MERS is similar to SARS, the virus that killed almost 800 people in a 2002 global epidemic. Both kill upwards of a third of people infected and, like many viruses, emerged from animals--bats and camels in the case of MERS--after mutating into a form capable of infecting human cells. Although MERS has so far been detected in 27 countries since the first case emerged in 2012, the outbreak has largely been contained within Saudi Arabia, according to the WHO. Like many viruses, MERS works by hijacking the ubiquitin system in human cells composed of hundreds of proteins that rely on ubiquitin to keep the cells alive and well. Upon infection, viral enzymes alter ubiquitin pathways in a way that allows the virus to evade the immune defense while multiplying and destroying the host tissue as it spreads in the body. "Viruses have evolved proteins that allow them to hijack host proteins. We can now devise strategies to prevent this from happening," says Zhang. Zhang and colleagues engineered the human ubiquitin protein into a new form that paralyses a key MERS enzyme, stopping the virus from replicating. These synthetic ubiquitin variants act quickly, completely eliminating MERS from cells in a dish within 24 hours. The researchers also created UbVs that blocks the Crimean-Congo virus, the cause of a haemorrhagic fever that kills about 40 per cent of those infected. And they're designed to only target only the virus -- hopefully minimizing side effects in any future drug. But before these engineered proteins can be developed into medicine, researchers first must find a way to deliver them into the right part of the body. For this, Zhang and Sidhu are working with Dr. Roman Melnyk, a biochemist in The Hospital for Sick Children and a world expert in protein delivery. The team is also investigating the possibility of finding drugs that work in a similar manner but can already cross the cell membrane. It is likely that the proteins will be tested first in plants and animals where regulatory approvals are less strict than they are for human drugs. "We are also working on an engineered ubiquitin that targets a corn virus responsible for destroying large swaths of corn fields in North America, with colleagues in Manitoba," says Zhang. In the meantime, Zhang will continue to improve delivery of his designer proteins to human cells that target not only MERS but also other viruses. He hopes others will follow suit. "With our tool, we can quickly generate anti-viral medicine and we hope that our method will inspire other researchers to try it out against diverse pathogens," says Zhang.


News Article | May 22, 2017
Site: www.biosciencetechnology.com

In June 2012, a 60 year-old man with flu-like symptoms walked into a private hospital in Jeddah, Saudi Arabia. Two weeks later, he died from multiple organ failure, becoming the first victim of a mysterious virus that came to be known as Middle East Respiratory Syndrome or MERS. The World Health Organization (WHO) has identified MERS as an urgent threat with no vaccine or treatment in sight. This could change thanks to a new anti-viral tool, developed by University of Toronto researchers. Writing in the journal PLoS Pathogens, the team led by Professor Sachdev Sidhu, of the Donnelly Centre for Cellular and Biomolecular Research and Department of Molecular Genetics, describe how they turned ubiquitin, a staple protein in every cell, into a drug capable of thwarting MERS in cultured human cells. Because the technology can be applied to a wide range of pathogens, it could become a game-changer in anti-viral therapeutics with implications for human health and the farming industry. "Vaccines are important for prevention, but there is a great need for anti-viral medicines to treat people who have become infected," says Dr. Wei Zhang, a postdoctoral research fellow in Sidhu's lab who did most of the work on the study. MERS is similar to SARS, the virus that killed almost 800 people in a 2002 global epidemic. Both kill upwards of a third of people infected and, like many viruses, emerged from animals--bats and camels in the case of MERS--after mutating into a form capable of infecting human cells. Although MERS has so far been detected in 27 countries since the first case emerged in 2012, the outbreak has largely been contained within Saudi Arabia, according to the WHO. Like many viruses, MERS works by hijacking the ubiquitin system in human cells composed of hundreds of proteins that rely on ubiquitin to keep the cells alive and well. Upon infection, viral enzymes alter ubiquitin pathways in a way that allows the virus to evade the immune defense while multiplying and destroying the host tissue as it spreads in the body. "Viruses have evolved proteins that allow them to hijack host proteins. We can now devise strategies to prevent this from happening," says Zhang. Zhang and colleagues engineered the human ubiquitin protein into a new form that paralyses a key MERS enzyme, stopping the virus from replicating. These synthetic ubiquitin variants act quickly, completely eliminating MERS from cells in a dish within 24 hours. The researchers also created UbVs that blocks the Crimean-Congo virus, the cause of a haemorrhagic fever that kills about 40 per cent of those infected. And they're designed to only target only the virus -- hopefully minimizing side effects in any future drug. But before these engineered proteins can be developed into medicine, researchers first must find a way to deliver them into the right part of the body. For this, Zhang and Sidhu are working with Dr. Roman Melnyk, a biochemist in The Hospital for Sick Children and a world expert in protein delivery. The team is also investigating the possibility of finding drugs that work in a similar manner but can already cross the cell membrane. It is likely that the proteins will be tested first in plants and animals where regulatory approvals are less strict than they are for human drugs. "We are also working on an engineered ubiquitin that targets a corn virus responsible for destroying large swaths of corn fields in North America, with colleagues in Manitoba," says Zhang. In the meantime, Zhang will continue to improve delivery of his designer proteins to human cells that target not only MERS but also other viruses. He hopes others will follow suit. "With our tool, we can quickly generate anti-viral medicine and we hope that our method will inspire other researchers to try it out against diverse pathogens," says Zhang.


News Article | May 19, 2017
Site: www.sciencedaily.com

In June 2012, a 60 year-old man with flu-like symptoms walked into a private hospital in Jeddah, Saudi Arabia. Two weeks later, he died from multiple organ failure, becoming the first victim of a mysterious virus that came to be known as Middle East Respiratory Syndrome or MERS. The World Health Organization (WHO) has identified MERS as an urgent threat with no vaccine or treatment in sight. This could change thanks to a new anti-viral tool, developed by University of Toronto researchers. Writing in the journal PLoS Pathogens, the team led by Professor Sachdev Sidhu, of the Donnelly Centre for Cellular and Biomolecular Research and Department of Molecular Genetics, describe how they turned ubiquitin, a staple protein in every cell, into a drug capable of thwarting MERS in cultured human cells. Because the technology can be applied to a wide range of pathogens, it could become a game-changer in anti-viral therapeutics with implications for human health and the farming industry. "Vaccines are important for prevention, but there is a great need for anti-viral medicines to treat people who have become infected," says Dr. Wei Zhang, a postdoctoral research fellow in Sidhu's lab who did most of the work on the study. MERS is similar to SARS, the virus that killed almost 800 people in a 2002 global epidemic. Both kill upwards of a third of people infected and, like many viruses, emerged from animals -- bats and camels in the case of MERS -- after mutating into a form capable of infecting human cells. Although MERS has so far been detected in 27 countries since the first case emerged in 2012, the outbreak has largely been contained within Saudi Arabia, according to the WHO. Like many viruses, MERS works by hijacking the ubiquitin system in human cells composed of hundreds of proteins that rely on ubiquitin to keep the cells alive and well. Upon infection, viral enzymes alter ubiquitin pathways in a way that allows the virus to evade the immune defense while multiplying and destroying the host tissue as it spreads in the body. "Viruses have evolved proteins that allow them to hijack host proteins. We can now devise strategies to prevent this from happening," says Zhang. Zhang and colleagues engineered the human ubiquitin protein into a new form that paralyses a key MERS enzyme, stopping the virus from replicating. These synthetic ubiquitin variants act quickly, completely eliminating MERS from cells in a dish within 24 hours. The researchers also created UbVs that blocks the Crimean-Congo virus, the cause of a haemorrhagic fever that kills about 40 per cent of those infected. And they're designed to only target only the virus -- hopefully minimizing side effects in any future drug. But before these engineered proteins can be developed into medicine, researchers first must find a way to deliver them into the right part of the body. For this, Zhang and Sidhu are working with Dr. Roman Melnyk, a biochemist in The Hospital for Sick Children and a world expert in protein delivery. The team is also investigating the possibility of finding drugs that work in a similar manner but can already cross the cell membrane. It is likely that the proteins will be tested first in plants and animals where regulatory approvals are less strict than they are for human drugs. "We are also working on an engineered ubiquitin that targets a corn virus responsible for destroying large swaths of corn fields in North America, with colleagues in Manitoba," says Zhang. In the meantime, Zhang will continue to improve delivery of his designer proteins to human cells that target not only MERS but also other viruses. He hopes others will follow suit. "With our tool, we can quickly generate anti-viral medicine and we hope that our method will inspire other researchers to try it out against diverse pathogens," says Zhang.


BASEL, Switzerland, CAMBRIDGE, Mass. and GAINESVILLE, Fla., May 16, 2017 (GLOBE NEWSWIRE) -- CRISPR Therapeutics (NASDAQ:CRSP), a biopharmaceutical company focused on creating transformative gene-based medicines for serious diseases, today announced that Target ALS Foundation, a non-profit organization dedicated to accelerating new treatments for amyotrophic lateral sclerosis (ALS), has awarded a two-year grant to CRISPR Therapeutics and its collaborators to support preclinical discovery and validation of CRISPR/Cas9-based therapeutic approaches directed to amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). CRISPR Therapeutics will collaborate with Dr. Laura Ranum and Dr. Eric Wang, researchers at the University of Florida in the Center for NeuroGenetics and the Department of Molecular Genetics & Microbiology, to test CRISPR/Cas9 gene-editing strategies in disease models developed by Dr. Ranum and Dr. Wang. The CRISPR Therapeutics and University of Florida consortium was one of four awardees selected by the independent scientific review committee out of a large field of highly competitive applications. “We are pleased to support this collaborative consortium between CRISPR Therapeutics and the University of Florida. Dr. Laura Ranum and Dr. Eric Wang are two of the leading researchers globally in ALS and similar disorders, and it brings them together with the leading gene-editing company to accelerate the path to clinic for CRISPR-based therapies in ALS,” said Manish Raisinghani, President of the Target ALS Foundation. “We are delighted to partner with Dr. Ranum and Dr. Wang to translate our in vivo gene-editing platform into potential therapies that address the underlying cause of ALS and FTD. The advances we make on ALS could pave the way for CRISPR/Cas9-based therapies in other CNS indications as well,” said Chad Cowan, Head of Research, CRISPR Therapeutics. “Building on our expertise in repeat expansion diseases and our development of a robust mouse model of C9orf72 ALS/FTD we are uniquely poised to test the efficacy of CRISPR/Cas9-based therapeutic strategies and their potential to prevent or reverse disease. My colleague Eric Wang and I are excited to embark on this collaboration to advance the development of CRISPR-based therapeutics,” said Laura Ranum, Kitzman Family Professor of Genetics and Microbiology and Director of the Center for NeuroGenetics, University of Florida. ALS and FTD are incurable diseases, certain forms of which are caused by pathologic expansion of a naturally occurring short DNA sequence repeat in specific genes. The CRISPR/Cas9-based approaches that will be the focus of this collaboration have the potential to correct these mutations at the molecular level to address the underlying cause of disease. CRISPR Therapeutics is a leading gene-editing company focused on developing transformative gene-based medicines for serious diseases using its proprietary CRISPR / Cas9 gene-editing platform. CRISPR/Cas9 is a revolutionary technology that allows for precise, directed changes to genomic DNA. The company's multi-disciplinary team of world-class researchers and drug developers is working to translate this technology into breakthrough human therapeutics in a number of serious diseases. Additionally, CRISPR Therapeutics has established strategic collaborations with Bayer AG and Vertex Pharmaceuticals to develop CRISPR-based therapeutics in diseases with high unmet need. The foundational CRISPR / Cas9 patent estate for human therapeutic use was licensed from the company's scientific founder Emmanuelle Charpentier, Ph.D. CRISPR Therapeutics AG is headquartered in Basel, Switzerland, with its wholly-owned U.S. subsidiary, CRISPR Therapeutics, Inc., and R&D operations based in Cambridge, Massachusetts. For more information, please visit www.crisprtx.com. About the University of Florida Center for NeuroGenetics The Center for NeuroGenetics (CNG), in the College of Medicine at the University of Florida, uses molecular, genetic and clinical research to define the causes of neurodegenerative disease, including ALS, and to develop effective treatment strategies. The goal of our Center is to advance our understanding of these genetic disorders so that we can develop rational therapeutic strategies for patients. Key aspects of the Center’s approach are to partner with affected families, non-profit organizations like Target ALS, and industry to understand these diseases using both clinical and basic science approaches. The Center for NeuroGenetics was founded in 2010 by Dr. Laura Ranum, PhD (Director) and Dr. Maurice Swanson, PhD (Associate Director). For more information, please visit www.neurogenetics.med.ufl.edu. Target ALS Foundation, Inc. (www.targetals.org) is a non-profit organization with the overall goal of accelerating development of new treatments for ALS. We drive emergence of novel ALS drug discovery programs in industry by funding collaborative consortia focused on development of novel therapeutic targets. To ensure that all new ideas get tested, we make essential tools and resources openly available to all—especially young investigators—with no embargo or strings attached.


The International Association of HealthCare Professionals is pleased to welcome Dr. Jerrod Hendry, BS, MS, MD, CCFP(EM) to their prestigious organization with his upcoming publication in The Leading Physicians of the World. Dr. Jerrod Hendry is a highly trained and qualified physician with a vast expertise in all facets of his work, especially family medicine and emergency medicine. Dr. Jerrod Hendry has been in practice for more than 15 years, and is currently serving patients as an Emergency Room Physician at Peace Arch Hospital in White Rock, British Columbia. Dr. Jerrod Hendry’s career in medicine began in 2001 when he graduated with his Medical Degree from the University of British Columbia, where he earlier gained a Master of Science Degree in Molecular Genetics. He then went on to serve his Emergency Medicine residency at McGill University. Dr. Hendry is double board certified by the American Board of Emergency Medicine and the American Board of Family Medicine. To keep up to date with the latest advances and developments in his field, he remains a distinguished member of the Canadian Association of Emergency Physicians, and the College of Family Physicians of Canada. Dr. Hendry attributes his success to his love for emergency medicine, as well as his drive to make a difference. When he is not assisting his patients, Dr. Hendry enjoys traveling, swimming, and hockey. Learn more about Dr. Hendry by reading his upcoming publication in The Leading Physicians of the World. FindaTopDoc.com is a hub for all things medicine, featuring detailed descriptions of medical professionals across all areas of expertise, and information on thousands of healthcare topics.  Each month, millions of patients use FindaTopDoc to find a doctor nearby and instantly book an appointment online or create a review.  FindaTopDoc.com features each doctor’s full professional biography highlighting their achievements, experience, patient reviews and areas of expertise.  A leading provider of valuable health information that helps empower patient and doctor alike, FindaTopDoc enables readers to live a happier and healthier life.  For more information about FindaTopDoc, visit http://www.findatopdoc.com


News Article | February 23, 2017
Site: phys.org

The discovery, published on February 23, 2017 in the journal Cell, reveals new details about the evolution of sex. The protein acts as a nearly universal, biochemical "key" that enables two cell membranes to become one, resulting in the combination of genetic material—a necessary step for sexual reproduction. New details about the protein's function could help fight parasitic diseases, such as malaria, and boost efforts to control insect pests. "Our findings show that nature has a limited number of ways it can cause cells to fuse together into a single cell," said William Snell, a senior author of the study and a research professor in the University of Maryland Department of Cell Biology and Molecular Genetics. Snell joined UMD in June 2016, but performed the majority of the work at his previous institution, the University of Texas Southwestern Medical Center. "A protein that first made sex possible—and is still used for sexual reproduction in many of Earth's organisms—is identical to the protein used by dengue and Zika viruses to enter human cells," Snell said. "This protein must have really put the spice in the primordial soup." Snell and his colleagues studied the protein, called HAP2, in the single-celled green alga Chlamydomonas reinhardtii. HAP2 is common among single-celled protozoans, plants and arthropods—although it is not found in fungi or vertebrates such as humans. Prior results from Snell and his collaborators, as well as other research groups, indicated that HAP2 is necessary for sex cell fusion in the organisms that possess the protein. But the precise mechanism remained unclear. For the current study, Snell and his colleagues at UT Southwestern used sophisticated computer analysis tools to compare the amino acid sequence of Chlamydomonas HAP2 with that of known viral fusion proteins. The results suggested a striking degree of similarity, especially in a region called the "fusion loop" that enables the viral proteins to successfully invade a cell. If HAP2 functioned like a viral fusion protein, Snell reasoned, then disrupting HAP2's fusion loop should block its ability to fuse sex cells. Sure enough, when Snell's team changed just a single amino acid in the fusion loop of Chlamydomonas HAP2, the protein entirely lost its function. The sex cells were able to stick together—a process that depends on other proteins—but they were not able to complete the final fusion of their cell membranes. Similarly, the cells could not fuse when the researchers introduced an antibody that covered up the HAP2 fusion loop. "We were thrilled with these results, because they supported our new model of HAP2 function," Snell said. "But we needed to visualize the three-dimensional structure of the HAP2 protein to be sure it was similar to viral fusion proteins." Snell reached out to Felix Rey, a structural biologist at the Pasteur Institute in Paris who specializes in viruses. Coincidentally, Rey and his colleagues had just determined the structure of Chlamydomonas HAP2 using X-ray crystallography. Rey's results demonstrated that, indeed, HAP2 was functionally identical to dengue and Zika viral fusion proteins. "The HAP2 protein from Chlamydomonas is folded in an identical fashion to the viral proteins," Rey said, referring to the molecular folding that creates the three-dimensional structure of all proteins from a simple chain of amino acids. "The resemblance is unmistakable." HAP2 appears to be necessary for cell fusion in a wide variety of organisms, including disease-causing protozoans, invasive plants and destructive insect pests. So far, every known version of HAP2 shares the one critical amino acid in the fusion loop region. As such, HAP2 could provide a promising target for vaccines, therapies and other control methods. Snell is particularly encouraged by the possibility of controlling malaria, which is caused by the single-celled protozoan Plasmodium falciparum. "Developing a vaccine that blocks the fusion of Plasmodium sex cells would be a huge step forward," Snell said, noting that Plasmodium has a complex life cycle that depends on both mosquito and human hosts. "Our findings strongly suggest new strategies to target Plasmodium HAP2 that could disrupt the mosquito-borne stage of the Plasmodium life cycle." Explore further: Sperm-egg fusion proteins have same structure as those used by Zika and other viruses More information: The research paper, "The ancient gamete fusogen HAP2 is a eukaryotic class II fusion protein," Juliette Fedry, Yanjie Liu, Gerard Péhau-Arnaudet, Jimin Pei, Wenhao Li, M. Alejandra Tortorici, Francois Traincard, Annalisa Meola, Gerard Bricogne, Nick Grishin, William J. Snell, Félix A. Rey and Thomas Krey, was published February 23, 2017 in the journal Cell.


News Article | February 23, 2017
Site: www.eurekalert.org

Researchers determine that a protein required for sperm-egg fusion is identical to a protein viruses use to invade host cells; discovery could help fight parasitic diseases like malaria Sexual reproduction and viral infections actually have a lot in common. According to new research, both processes rely on a single protein that enables the seamless fusion of two cells, such as a sperm cell and egg cell, or the fusion of a virus with a cell membrane. The protein is widespread among viruses, single-celled protozoans, and many plants and arthropods, suggesting that the protein evolved very early in the history of life on Earth. The discovery, published on February 23, 2017 in the journal Cell, reveals new details about the evolution of sex. The protein acts as a nearly universal, biochemical "key" that enables two cell membranes to become one, resulting in the combination of genetic material--a necessary step for sexual reproduction. New details about the protein's function could help fight parasitic diseases, such as malaria, and boost efforts to control insect pests. "Our findings show that nature has a limited number of ways it can cause cells to fuse together into a single cell," said William Snell, a senior author of the study and a research professor in the University of Maryland Department of Cell Biology and Molecular Genetics. Snell joined UMD in June 2016, but performed the majority of the work at his previous institution, the University of Texas Southwestern Medical Center. "A protein that first made sex possible -- and is still used for sexual reproduction in many of Earth's organisms -- is identical to the protein used by dengue and Zika viruses to enter human cells," Snell said. "This protein must have really put the spice in the primordial soup." Snell and his colleagues studied the protein, called HAP2, in the single-celled green alga Chlamydomonas reinhardtii. HAP2 is common among single-celled protozoans, plants and arthropods -- although it is not found in fungi or vertebrates such as humans. Prior results from Snell and his collaborators, as well as other research groups, indicated that HAP2 is necessary for sex cell fusion in the organisms that possess the protein. But the precise mechanism remained unclear. For the current study, Snell and his colleagues at UT Southwestern used sophisticated computer analysis tools to compare the amino acid sequence of Chlamydomonas HAP2 with that of known viral fusion proteins. The results suggested a striking degree of similarity, especially in a region called the "fusion loop" that enables the viral proteins to successfully invade a cell. If HAP2 functioned like a viral fusion protein, Snell reasoned, then disrupting HAP2's fusion loop should block its ability to fuse sex cells. Sure enough, when Snell's team changed just a single amino acid in the fusion loop of Chlamydomonas HAP2, the protein entirely lost its function. The sex cells were able to stick together -- a process that depends on other proteins--but they were not able to complete the final fusion of their cell membranes. Similarly, the cells could not fuse when the researchers introduced an antibody that covered up the HAP2 fusion loop. "We were thrilled with these results, because they supported our new model of HAP2 function," Snell said. "But we needed to visualize the three-dimensional structure of the HAP2 protein to be sure it was similar to viral fusion proteins." Snell reached out to Felix Rey, a structural biologist at the Pasteur Institute in Paris who specializes in viruses. Coincidentally, Rey and his colleagues had just determined the structure of Chlamydomonas HAP2 using X-ray crystallography. Rey's results demonstrated that, indeed, HAP2 was functionally identical to dengue and Zika viral fusion proteins. "The HAP2 protein from Chlamydomonas is folded in an identical fashion to the viral proteins," Rey said, referring to the molecular folding that creates the three-dimensional structure of all proteins from a simple chain of amino acids. "The resemblance is unmistakable." HAP2 appears to be necessary for cell fusion in a wide variety of organisms, including disease-causing protozoans, invasive plants and destructive insect pests. So far, every known version of HAP2 shares the one critical amino acid in the fusion loop region. As such, HAP2 could provide a promising target for vaccines, therapies and other control methods. Snell is particularly encouraged by the possibility of controlling malaria, which is caused by the single-celled protozoan Plasmodium falciparum. "Developing a vaccine that blocks the fusion of Plasmodium sex cells would be a huge step forward," Snell said, noting that Plasmodium has a complex life cycle that depends on both mosquito and human hosts. "Our findings strongly suggest new strategies to target Plasmodium HAP2 that could disrupt the mosquito-borne stage of the Plasmodium life cycle." In addition to Snell and Rey, co-authors of the study include: Juliette Fedry, Gerard Péhau-Arnaudet, M. Alejandra Tortorici, Francois Traincard and Annalisa Meola (Pasteur Institute); Yanjie Liu, Jimin Pei, Wenhao Li and Nick Grishin (UT Southwestern); Gerard Bricogne (Global Phasing, Ltd.); and Thomas Krey (Pasteur Institute, Hannover Medical School and German Center for Infection Research). The research paper, "The ancient gamete fusogen HAP2 is a eukaryotic class II fusion protein," Juliette Fedry, Yanjie Liu, Gerard Péhau-Arnaudet, Jimin Pei, Wenhao Li, M. Alejandra Tortorici, Francois Traincard, Annalisa Meola, Gerard Bricogne, Nick Grishin, William J. Snell, Félix A. Rey and Thomas Krey, was published February 23, 2017 in the journal Cell. This work was supported by the United States National Institutes of Health (Award Nos. GM56778 and GM094575), the Welch Foundation (Award No. I-1505), the European Research Council, the Pasteur Institute and the French National Center for Scientific Research. The content of this article does not necessarily reflect the views of these organizations. University of Maryland College of Computer, Mathematical, and Natural Sciences 2300 Symons Hall College Park, MD 20742 http://www. @UMDscience About the College of Computer, Mathematical, and Natural Sciences The College of Computer, Mathematical, and Natural Sciences at the University of Maryland educates more than 7,000 future scientific leaders in its undergraduate and graduate programs each year. The college's 10 departments and more than a dozen interdisciplinary research centers foster scientific discovery with annual sponsored research funding exceeding $150 million.


TORONTO, ON--(Marketwired - February 08, 2017) - Next generation sequencing (NGS) based clinical genomics assays are increasingly being offered by laboratories worldwide across a wide range of disease areas, including cancer, reproductive health, inherited disease and infectious disease. Developing, optimizing, and monitoring such assays however can be a time consuming and challenging task. Scientists and clinicians can build and implement robust and accurate clinical genomics assays with the help of highly multiplexed and patient-like reference materials. Join industry expert Sandi Deans, Consultant Clinical Scientist and Director of UK National External Quality Assessment Service (UK NEQAS) for Molecular Genetics as she discusses a case study of how a global external quality assessment (EQA) organization is using these reference materials to ensure the accuracy and consistency of one such clinical genomics application in non-invasive prenatal testing (NIPT). The live broadcast takes place on Wednesday, March 1, 2017 at 1pm EST. For more information or to register for this complimentary event, visit: Enabling Precision Medicine with Highly Multiplexed and Patient-like Reference Materials Xtalks, powered by Honeycomb Worldwide Inc., is a leading provider of educational webinars to the global Life Sciences community. Every year thousands of industry practitioners (from pharmaceutical & biotech companies, private & academic research institutions, healthcare centers, etc.) turn to Xtalks for access to quality content. Xtalks helps Life Science professionals stay current with industry developments, trends and regulations. Xtalks webinars also provide perspectives on key issues from top industry thought leaders and service providers. To learn more about Xtalks visit http://xtalks.com For information about hosting a webinar visit http://xtalks.com/sponsorship.ashx


Researchers from University of Southern California, Interventional Pain Institute, and Proove Biosciences Publish Clinical Utility Study Supporting Precision Medicine in Pain Perception IRVINE, CA--(Marketwired - Feb 13, 2017) -  Proove Biosciences, Inc., the Healthcare Decision Company™, is pleased to announce the publication of a clinical study supporting the clinical utility of Proove Pain Perception® Profile in the latest edition of the peer-reviewed Journal of Psychiatric Research. In the study entitled, An observational study of the impact of genetic testing for pain perception in the clinical management of chronic non-cancer pain, researchers from the University of Southern California Keck School of Medicine in Los Angeles, Interventional Pain Institute in Baltimore, and Proove Biosciences published findings which demonstrate how clinicians use Proove Pain Perception to improve clinical outcomes for patients. Adding to the voluminous clinical validity evidence supporting Proove Pain Perception that is published in marquee peer-reviewed journals such as Human Molecular Genetics, Science, and Pain, this clinical utility study demonstrates the impact of physician decision-making and patient outcomes using this technology. "It is gratifying to see Proove's collaborative efforts gain acceptance among our vast community of discerning peers," says Dr. Maneesh Sharma, lead author of the study, Medical Director of the Interventional Pain Institute and member of Proove's Medical Advisory Board. "Proove is committed to uncovering the best treatment options for pain patients, and through this study, we hope to advance the adoption of precision medicine solutions in clinical settings to reduce the burden of chronic pain and prescription opioid abuse. We are grateful to our colleagues and to the Journal of Psychiatric Research for their recognition of our findings." Proove Pain Perception® Profile provides an objective measure of pain perception based, in part, on genetic markers in the catechol-O-methyltransferase (COMT) gene. The proprietary haplotype algorithm characterizing this gene was invented by NIH-funded scientists at the University of North Carolina at Chapel Hill, and the exclusive rights to this intellectual property was licensed to Proove Biosciences. In this study, authors found that using Proove Pain Perception substantially affected physician clinical decision-making and that the availability and utilization of this information was a contributing factor in clinical improvement. These findings demonstrate the clinical utility and actionability of the already clinically-validated algorithm behind the Proove Pain Perception Profile. "With opioid abuse and deaths from overdose at an all-time high as a result of mismanaged or misunderstood chronic pain, we have no doubt that these innovative treatment solutions may soon be the go-to option for thousands of doctors, surgeons and hospitals," adds Sharma. Since launching in 2009, Proove Biosciences has become the commercial and educational leader in the research, investigation and development of patent-protected tests that combine genetic and clinical data into reports to help physicians individualize -- and optimize -- medicine selection and dosing. Proove is backed by science, driven by data and supported by an advisory board of the world's leading medical experts. Its patented bioinformatics platform for collecting, storing, analyzing and integrating biological and genetic information, is changing the future of healthcare. "Over the past 5 years, Proove has been conducting a number of multi-center studies involving prospective outcomes of thousands of patients," explained Dr. Svetlana Kantorovich, Director of Research & Development at Proove. "Through these large studies, we look forward to many more publications in peer-reviewed journals providing continued evidence of the accuracy and positive impact of Proove's precision medicine technology." To learn more about Proove Biosciences, visit www.proove.com. With media inquiries, please contact Leslie Licano at leslie@beyondfifteen.com or (949)-733-8679. About Proove Biosciences: Proove Biosciences -- the Healthcare Decision Company™ -- is the commercial and educational leader in the research, investigation and development of patent-protected tests that combine genetic and clinical data into reports to help physicians to individualize -- and optimize -- medicine selection and dosing. Supported by leading medical experts and institutions across the globe, the reports facilitate objective decision-making to improve outcomes for patients, providers and insurers. Backed by science and driven by data, Proove is revolutionizing individualized medicine. With a patented bioinformatics platform that delivers therapy-defining information that allows prescribers to evaluate pain tolerance, assess patient drug metabolism, predict response and immunity to opioid and non-opioid pain medication, and identify risk for dependence and addiction, Proove provides the most technologically advanced solutions to enable accurate and evidence-based medical decision-making rather than "trial-and-error" approaches. Proove helps reduce the risk of treatment failure, decrease costs to insurers and relieve society of the emotional and financial burdens associated with addiction and other avoidable consequences. For more information, please visit www.proove.com or call toll free 855-PROOVE-BIO (855-776-6832).

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