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One-Third of Human Food Depends on Bees! The National Synchrotron Radiation Research Center Cracks the Structure of Honeybee-Infecting Viruses to Protect Bee Colonies4
漢璽科技股份有限公司 新竹縣湖口鄉成功路421巷5弄18號
NSRRC to Send Virus-Like Particles to SpaceUnder the prolonged period of support from the Ministry of Science and Technology (MOST), the National Synchrotron Radiation Research Center (NSRRC) is now joining hands with Japan-based Space BD and its Taiwanese general agency HelioX Cosmos Co., Ltd. on participating in the impending space experiment program at the end of 2021, which delivers “virus-like particles” of the NSRRC to the international space station for crystallization experiment through the supply vessel of the space station, and the particles will be sent back to Taiwan after almost a month of space travel in order to probe into the impact of the gravity-free environment of outer space on the crystal growth and structure of viruses.The diversified ways of virus infection results in rapid spreading speed, which leads to discomfort, sickness, and a significant level of deaths for the hosts upon a short period of infection, such as the COVID-19 pandemic that has been ravaging the world in the last two years, as well as swine virus, fish and shrimp viruses, and avian influenza that bring terror to the breeding industry. A further understanding in the properties of viruses will be able to develop more effective pandemic-prevention technology that will reduce the threats of viruses on humans and the breeding industry.The virus-like particles that will be traveling in the outer space this time are produced by Deputy Director Chun-Jung Chen and his research team, where molecular biology technology is adopted in mass producing high purity capsid protein that are then assembled into non-infectious virus-like particles. The virus-like particles will be sent to Japan under the escort of Space BD and HelioX Cosmos Co., Ltd., before boarding the supply vessel of the space station and heading towards the international space station.The virus-like particles will transform into “virus-like particle crystals” and be delivered back to earth after about a month of time, and then rapidly frozen to -196°C, before sent back to Taiwan. The high-intensity X-ray and the “protein crystallography technology” of the Taiwan Photon Source (TPS) of the NSRRC will be utilized in observing the crystalline state of virus-like particles under a gravity-free environment, and comparing the differences in virus assembly and structure against the gravity environment of earth.Chen commented, “We expect the quality of the crystal to elevate significantly under a gravity-free environment in comparison to that of general laboratories on earth, and the better the quality the structure of the virus-like particle crystal is, the higher degree of precision in the comprehensive virus particle structure is under an atomic level, where the formation of each atom in the virus can be analyzed and interpreted. The high-resolution structural information of the virus allows us to probe into the assembly and structure of viruses, as well as the key mechanism in invading the main cells of the hosts.”Viruses are incredible ultra-microorganisms, where hundreds of capsid protein molecules are spontaneously arranged into highly symmetrical spherical virus particles that are approximately tens of nanometers in diameters, while the hollow spheres contain RNA of viral genetic inheritance.The surface of viruses is filled with dense and apparent protrusion subunits that resemble the flamboyant outer of flowers, such as the spike protein of the coronavirus. Protrusion subunits usually portray the essential role in identifying and infecting the cells of various hosts, and act similar to a bunch of keys that open the door to viral infections in cells. An understanding to the structure of the keys will grasp on the passcode of the lives of viruses, which can be utilized to develop high-efficiency subunit vaccines.Chen commented that using protrusion subunits as the main antigenic epitope will significantly increase the specificity of the antibody in virus identification, where specific targeted and valuable vaccines can be developed so as to enhance the effectiveness of vaccines that is useful for the research and development of new anti-virus strategies, as well as introduce new breakthroughs in precision health and pandemic-prevention technology. https://www.hannxi.com/zh/hot_452028.html Precision Medicine Sets Sail 2023-02-17 2024-02-17
漢璽科技股份有限公司 新竹縣湖口鄉成功路421巷5弄18號 https://www.hannxi.com/zh/hot_452028.html
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With the long-term support of the National Science and Technology Council, the research team led by Dr. Chun-Jung Chen and Dr. Nai-Chi Chen of the National Synchrotron Radiation Research Center (NSRRC) has after nearly five years achieved a world first in identifying the capsid protein structure and function of the Lake Sinai Honeybee-Affecting Virus, as well as the dynamic assembly process for virion formation. This research is of great significance for developing natural antiviral medicines for bees, and the results were published in the prestigious journal Nature Communications on February 1.

According to the Food and Agriculture Organization (FAO) of the United Nations, nearly one-third of the world's agricultural crops rely on bee pollination. In the past few decades, bee populations around the world have plummeted because their habitats have been greatly reduced, which affects not only crop pollination but also food supply for human beings. In 2006, the United States named the mysterious disappearance of bee populations "Colony Collapse Disorder." Previous studies have revealed that in addition to human factors and environmental changes, one of the major causes of Colony Collapse Disorders is viral infection, which could cause severe damage to a bee's brain, central nervous system, and wings, affecting its ability to harvest and return to the nest, or even resulting in death.

The Lake Sinai virus is a recently discovered and highly contagious honeybee-infecting virus that could cause a large number of bee deaths in a short period of time, and for which there is currently no cure. The current method to control transmission involves large-scale incineration of infected hives, which hugely impacts beekeeping. Another method is the use of pesticide; however, this approach is likely to cause environmental pollution; the chemical residues in honey may exacerbate the food safety problem. In order to improve the survival rate of honeybees, scientists are eager to gain a full understanding of the virus and the mechanism of infection so that antiviral drugs can be developed to block the spread of the virus and minimize damage.

The research team used the protein crystallography and small-angle scattering techniques of the high-intensity X-ray endstations at NSRRC in Taiwan and SPring-8 in Japan, in partnership with the SLAC National Accelerator Laboratory of Stanford University in the United States, as well as Drs. Meng-Chiao Ho and Chun-Hsiung Wang of Academia Sinica who assisted with cryo-electron microscopy. A detailed analysis of the capsid protein structure of the virus was conducted with a resolution of up to 0.25 nanometers, affording the first glimpse of the virus.

The research team found that the Lake Sinai virus has a hollow spherical shell consisting of 240 identical capsid proteins. The inside of the sphere with a diameter of approximately 50 nanometers is for the accommodation of genome RNA. The spheroid is composed of surface spikes, the outer capsid region, and the inner capsid structure. Each surface spike is like a key used to connect and open the door of the honeybee host cell, allowing the viral RNA to invade the host. The outer capsid region is responsible for the assembly and consolidation of the spherical shell, while the inner capsid structure completes the replication and reproduction of the virus by binding to RNA.

The research team also for the first time observed the transition of the virus particle assembly process. In the initial stage of the virus capsid formation, three outer capsid proteins combine to form a stable trimer as the main unit (point), which is then connected to others to form domino-like scaffold structures (lines) of various lengths. The structures are then assembled into a complete shell (surface) like a spherical puzzle. In addition, the research team found that in response to physiological environments of different acidity, the size and structure of the spherical shell changes dynamically, which plays an essential role in the invasion, infection, and replication of the virus in host cells.

The results of this study allow scientists to better understand the transmission route and pathogenic mechanism of the Lake Sinai virus and facilitate the development of new antiviral drugs, such as seeking appropriate natural extracts expected to have antiviral properties based on the virus structures. Antiviral drugs can be mixed with bee feed to prevent infection and improve colony immunity against the virus, thereby effectively preventing pests and diseases. The findings of this study could help to reduce the use of pesticide and to maintain the natural ecological balance, as well as bringing possible solutions to beekeeping’s existing challenges and developing new opportunities to agriculture.

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