Date: 22 July (Thursday)
Time: 10:40 – 12:10 (GMT+8)
Scripps Family Chair Professor of Chemistry
The Scripps Research Institute
Professor Wong received his B.S. (1970) and M.S. (1977) degrees (with KT Wang) from National Taiwan University, and Ph.D. (1982) in Chemistry (with George M. Whitesides) from Massachusetts Institute of Technology. He then worked at Harvard University as a postdoctoral fellow (with George M. Whitesides) for another year, and became a faculty member at Texas A&M University (1983) where he was promoted to full professor in 1987. He then moved to The Scripps Research Institute in 1989 as Professor and Ernest W. Hahn Chair in Chemistry. From 2006 to 2016, he served as President of Academia Sinica in Taiwan. He is currently the Scripps Family Chair Professor of Chemistry at The Scripps Research Institute and holds a joint appointment as Distinguished Professor at the Genomics Research Center, Academia Sinica.
Professor Wong received numerous honors for recognition of his accomplishments, including, for example, the Presidential Young Investigator Award in Chemistry USA (1986), the Roy Whistler Award of the International Carbohydrate Organization (1994), the ACS Claude S. Hudson Award in Carbohydrate Chemistry (1999), the International Enzyme Engineering Award (1999), the US Presidential Green Chemistry Challenge Award (2000), The ACS Award for Creative Work in Synthetic Organic Chemistry (2005), Humboldt Research Award for Senior Scientists (2006), the Nikkei Asia Prize for Science, Technology and Innovation (2012), the ACS Arthur C. Cope Medal (2012), the Wolf Prize in Chemistry (2014), and the Robert Robinson Award of the Royal Society of Chemistry, UK (2015).
He is a member of Academia Sinica (1994), the American Academy of Arts and Sciences (1996), the US National Academy of Sciences (2002) and the US National Academy of Inventors (2014). He served as Chairman of the Executive Board of Editors of the Tetrahedron Publications (2006-2008), Head of the Frontier Research Program on Glycotechnology at RIKEN in Japan (1991–1999), and a board member of the US National Research Council on Chemical Sciences and Technology (2000–2003). In addition, he has received many honorary doctor degrees, given numerous plenary and named lectures, and served as a science advisor to many organizations, including a scientific advisor to the Max-Planck Institute (2000-2008), a member of RIKEN Advisory Council (2010-16), and the Chief Science Advisor to the Taiwan Government (2006-2015).
His research interests are in the field of chemical biology and synthetic chemistry, with particular focus on the development of new methods and tools for the synthesis and study of complex carbohydrates and glycoproteins associated with aberrant glycosylation that causes diseases. He has published over 750 papers and received more than 120 patents, and is a highly cited scientist with an h-index of 148.
A major challenge to end the pandemic caused by SARS-CoV-2 and emerging variants is to develop broadly protective vaccines with long-term immunity. The viral surface spike (S) protein has been the major immunogen for vaccine development; however, it is frequently mutated and heavily glycosylated to evade host immune response, and the highly conserved epitopes are largely shielded by glycans. Here we show that S protein glycosylation is cell specific, with differential effect on viral infectivity, and the major glycoforms from lung epithelial cells, the primary cells for infection, are mainly complex-type and require sialylation for efficient infection. Immunization of S protein with all N-glycans trimmed to the monoglycosylated state (Smg) elicits stronger neutralizing antibody and balanced Th1/Th2 responses toward the wild type and the variants of concern, and is significantly more protective for hACE2 transgenic mice challenged with a lethal dose of virus as compared to the fully glycosylated S protein (Sfg). A monoclonal antibody identified from the single B cell clones of Smg immunized mice is also able to neutralize the wild type and the variants, demonstrating that removal of glycans from S protein to better expose the highly conserved sequences is an effective approach to universal vaccine development.