Ian Andrew Wilson | |
---|---|
Born | |
Alma mater | University of Edinburgh, Oxford University |
Known for | Structural biology |
Scientific career | |
Institutions | Scripps Research Institute |
Doctoral advisor | David C. Phillips |
Other academic advisors | Don Craig Wiley |
Ian Andrew Wilson is the Hansen Professor of Structural Biology and chair of the Department of Integrative Structural and Computational Biology [1] [2] at the Scripps Research Institute in San Diego, California, United States.
He received his BSc in biochemistry from the University of Edinburgh in 1971, his PhD degree in molecular biophysics from Oxford University in 1976 under the guidance of David C. Phillips working on the structure of the triosephosphate isomerase. [3] He then did postdoctoral research at Harvard University with Don Craig Wiley from 1977 to 1982 during which he solved the first crystal structure of the influenza virus hemagglutinin. [4] [2]
After his postdoc positions, he joined the Scripps Research Institute in La Jolla, California, in 1982 as an assistant professor and is currently professor in the department of molecular biology and the Skaggs Institute for Chemical Biology. His laboratory focuses on the recognition of microbial pathogens by the immune system and has determined over 85 crystal structures of mouse, human, shark, and catalytic antibodies, with a variety of antigens, including steroids, peptides, carbohydrates and viral proteins, such as HIV-1 and Hepatitis C virus envelope glycoproteins. [5] His team was reported by the 6 February 2004 edition of Science magazine to have managed to synthesise the hemagglutinin protein responsible for the 1918 outbreak of Spanish flu. [6]
Since 2000, he has directed the Joint Center for Structural Genomics (JCSG) that has pioneered innovative new methods for high throughput structural studies, including x-ray and NMR. The JCSG has determined over 700 structures that focus on the expanding protein universe. [7]
He was elected as a Fellow of the Royal Society of London in 2000, a Member of the American Academy of Arts and Sciences in 2002, a Fellow of the Royal Society of Edinburgh in 2008, a foreign associate of the National Academy of Sciences in 2016. [8] He also served on the Life Sciences jury for the Infosys Prize in 2014.
Ian was born in Perth, Scotland. His father was a journalist. [2]
Influenza hemagglutinin (HA) or haemagglutinin[p] is a homotrimeric glycoprotein found on the surface of influenza viruses and is integral to its infectivity.
Don Craig Wiley was an American structural biologist.
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Hemagglutinin esterase (HEs) is a glycoprotein that certain enveloped viruses possess and use as an invading mechanism. HEs helps in the attachment and destruction of certain sialic acid receptors that are found on the host cell surface. Viruses that possess HEs include influenza C virus, toroviruses, and coronaviruses of the subgenus Embecovirus. HEs is a dimer transmembrane protein consisting of two monomers, each monomer is made of three domains. The three domains are: membrane fusion, esterase, and receptor binding domains.
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Donald L. D. Caspar was an American structural biologist known for his works on the structures of biological molecules, particularly of the tobacco mosaic virus. He was an emeritus professor of biological science at the Institute of Molecular Biophysics, Florida State University, and an emeritus professor of biology at the Rosenstiel Basic Medical Sciences Research Center, Brandeis University. He has made significant scientific contributions in virus biology, X-ray, neutron and electron diffraction, and protein plasticity.
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human influenza virus. The HA-tag is derived from the HA-molecule corresponding to amino acids 98-106. HA-tag has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA-tag, which does not generally appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation and purification of the protein of interest.
Viral neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Neuraminidase inhibitors are antiviral agents that inhibit influenza viral neuraminidase activity and are of major importance in the control of influenza.
In molecular biology, hemagglutinins are receptor-binding membrane fusion glycoproteins produced by viruses in the Paramyxoviridae family. Hemagglutinins are responsible for binding to receptors on red blood cells to initiate viral attachment and infection. The agglutination of red cells occurs when antibodies on one cell bind to those on others, causing amorphous aggregates of clumped cells.
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