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 Dr. Somchai Tancharakorn, Acting Beamline Manager of Beamline 5.1W, Synchrotron Light Research Institute (SLRI), Dr. Somboon Sahasithiwat, Vice President, National Science Technology and Quality Infrastructure, National Science and Technology Development Agency (NSTDA), and NSTDA colleagues were invited as representatives of Thailand’s infrastructure-related organizations to join the International Conference on Research Infrastructures (ICRI) 2022 held on 19-21 October 2022 at Brno, Czech Republic.  Representatives from Cambodia, Indonesia, and European Strategy Forum on Research Infrastructures (ESFRI) attended the conference as well.

                           ICRI2022 gained support from the Enhanced Regional EU-ASEAN Dialogue Instrument (E-READI) with aims to provide delegates both guidelines on building collaboration network and managing research infrastructures at international level.  The conference also aimed to update delegates on the current collaboration between networks in the European Union (EU) countries and other regions worldwide on both large-scale research infrastructures such as large telescope, synchrotron light research laboratory, High Performing Computing, etc. and middle or small infrastructures such as bioimaging laboratory, etc.  Experience exchange among infrastructure networks worldwide was done at the conference as well.

                        On this occasion, Dr. Tancharakorn, NSTDA colleagues, and representatives from ASEAN countries discussed with other delegates to seek opportunity of building collaboration between ASEAN and EU countries on research infrastructures.  On 21 October 2022, Dr. Piyawut Srichaikul from National Electronics and Computer Technology Center, NSTDA, as the co-chairman of ASEAN HPC network gave presentation on “ASEAN-EU Cooperation in High Performance Computing” which paves the way to ASEAN-EU collaboration on research infrastructures.

 The Synchrotron Light Research Institute (Public Organization) under the supervision of the Ministry of Higher Education, Science, Research and Innovation, in the name of Thailand and representative of Asia hosted the 13^th International Particle Accelerator Conference (IPAC22) in Thailand for the first time during 12-17 June 2022 at IMPACT Exhibition and Convention Center.  The conference was successfully held with over 800 Thai and foreign visitors from Germany, United States, France, Switzerland, Japan, Italy, United Kingdom, Korea and Spain, and over 1,000 topics of research abstracts as well as over 60 booths of the particle accelerator exhibition from international dealers.  The event provided insightful academic knowledge and performed as an experience exchange stage between researchers across the globe.  The meeting also boosted the local economy for hospitality and tourism and represented a good image of Thailand to all visitors.

 Dr. Prapong Klysubun, SPS-II Project Manager, SLRI, and Organising Committee Chair of IPAC’22, said, “The IPAC meeting has such global significance, and it is the largest conference of its kind.  The conference is held annually with the rotation of host within 3 continents which are Asia (including Australia), Europe and North-South America.  This year, it was being held in Asia and Thailand led by the Synchrotron Light Research Institute had signed up and was selected to be the host of the 13^th conference with the participation of academicians and people who are interested in the meeting from various industries such as scientists, researchers, engineers, and particle accelerator dealers.  The event was appreciated by visitors for its well-organized management and impressive atmosphere.

 In the IPAC’22, the latest research paper and insights of particle accelerators from worldwide were presented as well as the practical applications of research, technology and innovation used in a laboratory and the industrial sector.  International scientists from around the world had come to update researches of synchrotron technology, particle accelerator technology, magnet technology, vacuum technology and system technology to expand and enhance knowledge on science, technology and innovation for the future.  In addition, there were awards ceremonies for international particle accelerator physicists.  Each award is named after Asia particle accelerator physicists who have created benefactions and played an important role in the particle accelerator industry such as the Xie Jialin Prize which was named in the honor of Prof. Xie Jialin, a Chinese physicist who developed the particle accelerator to cure cancer, the Nishikawa Tetsuji prize was named in the honor of Nishikawa Tetsuji, a Japanese physicist who was expert on the light dynamics of linear particle accelerator, and the Hogil Kim Prize was named in the honor of Prof. Hogil Kim, a physicist and student who piloted the biggest particle accelerator project in South Korea and successfully graduated as particle accelerator physicist from an institute in the United States.  Moreover, there was also an exhibition to present Thailand’s second synchrotron light generator to be built in the Eastern Economic Corridor of Innovation in Rayong Province in order to support the industrial sector.  The second generator will take around 7 years to finish and will add at least 6,000 million Baht to the country economic value per year, bringing Thailand to be an innovative country and lifting Thai people’s quality of life.

 Dr. Prapong Klysubun added “Thailand has the Synchrotron Light Research Institute (Public Organization) or SLRI to provide synchrotron light for public, private and industrial sectors with an aim of research purposes and product development in various fields, including food, cosmetics, pharmaceuticals, and polymers.  The institute is located in the campus of Suranaree University of Technology (SUT), Nakhon Ratchasima.  It is the only synchrotron light research institute in Thailand and is the biggest one in ASEAN.  It provides service and support to farmland, medical, pharmacy and industry such as the service of providing synchrotron light to the industry to develop cosmetics with skin absorption analysis.  More example is a project using synchrotron light to develop medicine; COVID-19 medicines by using synchrotron light to identify molecule model of COVID-19 virus which the Synchrotron Light Research Institute in China was the first to discover, followed by England.  This helped scientists to develop medicine which blocks virus molecules attached to human body cells.  Another example is the usage of synchrotron light to develop medicine for Avian Influenza which the Synchrotron Light Research Institute in Australia was able to develop medicine to cure the H5N1 virus.  As above mentioned, the synchrotron light generator is considered as a scientific tool with a complication of engineering technology and is recognized as a key infrastructure to develop the country in terms of science and technology for business expansion and competitive increase to support industrial research leading to human resources development as well as creating jobs and building careers in various fields.           

The next 14^th International Particle Accelerator Conference will be held in Italy. 

  In the 21st century, many principles, theories, and various bodies of knowledge have been formulated leading to advanced technological development for more human convenient living. One technology apparently taking as a part in human life is nanotechnology. The nanotechnology is a technology occurred from applying multidisciplinary knowledge from many fields such as physics, chemistry, engineering, or applied science to make and synthesize atomic and molecular materials, also nanoscale parts and structures. Nanotechnology is utilized to develop materials or tools with specific physical, chemical, and biological properties or functions in response to human’s need in term of more life safety and convenience.

Microsystems Electronics and Control Systems (MEMs) laboratory at Beamline 6: Deep X-ray Lithography, Synchrotron Light Research Institute, the laboratory equipped with tools and instruments for production of nanoscale parts and structures, is upgraded in efficacy to support the era of nanotechnology.  The FE-SEM (MIRA3 model) was installed to fabricate nanoscale-structure using Electron Beam Lithography (EBL) process.  In this process, the focused electron beam is applied to create nanostructures on photoresist. The photoresist reacts to electrons and is rinsed off by Developer liquid to acquire nanoscale structure for adding metal on substrate and building metallic nanostructure later on. 

              The MEMs lab is currently developed and can make the small metallic structure at     100-nanometer scale with the Electron Beam Lithography to support frontier research and advanced technology.    

Article by: Mr. Kiattisuk Srisoam, Laboratory Scientist

                 Dr. Pattanaphong Janphuang, Beamline Manager

 Figure 1 Three dimensional models of the SARS-CoV-2 virion and a schematic diagram of its four structural proteins. Figures were modified from    coronavirusexplained       

 A novel zoonotic coronavirus SARS-CoV-2 was originally explored in Wuhan, China in December 2019 and further regarded to the serious pandemic known as COVID-19. In early March 2022, the global COVID-19 pandemic has caused over 453 million confirmed cases and over 6 million deaths (John Hopkins Coronavirus Resource Center, https://coronavirus.jhu.edu).

 The COVID-19 virus and the emergence of new virus variants seriously threat to global public health. It is a strong requirement to develop the effective diagnostic tools which are able to quickly and reliably detect active SARS-CoV-2 infections.

 Structural proteins of the COVID-19 virus are very important to understand its pathogenic mechanism, thus leading to the development of antibodies, vaccines and drugs for targeting these proteins and viruses.

 SARS-CoV-2 comprised the four structural proteins; the spike (S), nucleocapsid (N), envelope (E) proteins and membrane glycoprotein (M). A complete virus particle (virion) is represented in Figure 1. Cryo-electron microscopy is one of the powerful tools to determine the overall structure of the S protein, thus presenting a unique crown or ‘corona’-like shape.

 Three viral proteins; the spike (S), envelope (E) and membrane (M) are embedded in the outer layer of the corona viral particle. The corona viruses protect themselves from the surrounding environment, then the ribonucleic acid (RNA) forms a stable packed in the lipid membrane. The nucleocapsid protein (nucleoprotein) is responsible for tightly wrap the RNA of viruses. However, the fatty membrane of SARS-CoV-2 is sensible to be destroyed by soap, detergent or surfactant.

 The nucleocapsid protein significantly involves in viral genomic RNA binding, thus protecting the coiled RNA as its genetic material inside the virus particle. Moreover, the N protein also plays an important role in the early stages of viral infection when the RNA genome is first released into the target host cell.

 X-ray crystal structures of the N-terminal (PDB entry 7CDZ) and C-terminal domains have been illustrated here (PDB entry 6WZO). Holo structure of N-terminal domain in complex with double strand RNA (PDB entry 7ACS) has been determined by Nuclear Magnetic Resonance Spectroscopy technique.

 The SARS-CoV-2 nucleocapsid protein comprises a total of 419 amino-acid residues as shown in Figure 2a. The N-terminal domain (NTD, residues 49–174) and the C-terminal domain (CTD, residues 247–364) are connected by a flexible linker (residues 175–246) (Figure 2a).

 The structure of N-NTD is folded into a right-handed shape and consists of six antiparallel β-sheets (β4-β2-β3-β1-β5-β6), thus forming the palm (Figure 2b). A protruding β-hairpin region locates out of the core subdomain which is formed by a four-stranded antiparallel β-sheet (Figure 2b).

 The N-terminal domain of nucleocapsid protein bound to viral RNA forms a ribonucleoprotein complex as shown in Figure 2c. The overall structure of N-NTD complexed with double strand RNA (dsRNA) which is shown in electrostatic surface potential illustrates the negatively charged RNA binding to the positively charged region in the nucleocapsid protein.

 The C-terminal domain of nucleocapsid protein forms a cuboid architecture, thus composing of homologous dimers. Each protomer consists of six α-helices and two β-strands (Figure 2d).

Figure 2 (a) Schematic diagram of the nucleocapsid protein (N); the N-terminal domain (NTD and the C-terminal domain (CTD). (b) The overall structure of N-NTD depicted in ribbon representation. (c) The overall structure of N-NTD complexed with dsRNA. (d) The overall structure of C-NTD shown in cartoon representation. Figures were obtained from Yan et al., 2022.

 The SARS-CoV-2 N protein is a highly immunogenic viral protein that plays essential roles in corona viral transcription and replication assembly. Moreover, the N protein provides several good advantages: it shares substantial sequence conservation, is less vulnerable to mutation in variants, and activates a stronger protective immune response in the host cells. Therefore, N protein is an excellent potential target for drug design and diagnosis of COVID-19.

Re-written by Chomphunuch Songsiriritthigul (Beamline Scientist, SLRI)

References

 Neuman, B.W., Buchmeier, M.J. (2016). Supramolecular Architecture of the Coronavirus Particle. Advances in Virus Research. 96, 1-27. DOI: 10.1016/bs.aivir.2016.08.005.
McBride, R., van Zyl, M., Fielding, B.C. (2014). The coronavirus nucleocapsid is a multifunctional protein. Viruses. 6(8), 2991-3018. DOI: 10.3390/v6082991.

 Schoeman, D., Fielding, B.C. (2019). Coronavirus envelope protein: current knowledge. Virology Journal. 16(1), 69. DOI: 10.1186/s12985-019-1182-0.
Walls, A.C., Park, Y.J., Tortorici, M.A, et al. (2020). Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell. 181(2), 281-292.e6. DOI: 10.1016/j.cell.2020.02.058.
Yan, W., Zheng, Y., Zeng, X., He, B., Cheng, W. (2022). Structural biology of SARS-CoV-2: open the door for novel therapies. Signal Transduction and Targeted Therapy. 7(26). DOI: 10.1038/s41392-022-00884-5.