AROUND THE COLUMNS
On Oct. 3, 2018, Professor Emeritus George Smith, second from right, was informed that he had won a Nobel Prize. On Dec. 10, he received the award in Stockholm, Sweden. Smith is shown here walking toward Jesse Hall with Chancellor Alexander Cartwright.
Just days before this magazine went to press, King Carl XVI Gustaf of Sweden, resplendent in white tie and tails, stood before the assembled members of the Royal Swedish Academy and handed George P. Smith, an avuncular molecular biologist who has spent the whole of his 43-year career at Mizzou, a hand-lettered diploma and a medal struck in gold. Pro pace et fraternitate gentium, that medal read: “For the peace and brotherhood of men.” The 2018 Nobel Prize for Chemistry was awarded to Smith, now a distinguished professor emeritus of biological sciences, along with two fellow researchers, Caltech’s Frances Arnold and Sir Gregory Winter of Britain’s MRC Laboratory of Molecular Biology, on Dec. 10. The prize was announced Oct. 3. Arnold, an engineer who is just the fifth woman to win the chemistry Nobel, was honored for her insights into how a “directed” form of natural selection could help engineer enzymes. Smith and Winter shared the second half of the prize for their use of bacteriophages, viruses that infect bacteria, in “evolving” antibodies and other proteins into promising therapeutic and research tools. The Swedish Academy called Smith’s contribution “ingenious” and “brilliant in its simplicity,” though in this case simplicity is a decidedly relative term. A bacteriophage (phage for short) consists of a small chromosome encapsulated in a shell of coat proteins. Working with a particularly malleable class of phages, the filamentous phages, Smith had a flash of insight. If he inserted a gene for an extra “guest” protein into the gene for one of the phage’s coat proteins, this guest protein would, because it resided on the surface, retain its ability to bind to a target
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receptor or antibody. It also, thanks in part to its naturally infectious tendencies, could be propagated into vast numbers simply by using it to infect fresh bacterial cells. Smith’s next step was crucial: connecting these phages to specific receptors or antibodies of interest to researchers. In his lab in MU’s Tucker Hall, Smith and his assistants poured one of these new libraries into a Petri dish, hoping a few of the guest proteins might bind to a receptor immobilized on the dish’s surface. When this, in fact, happened as planned, Smith’s team then washed out the dish leaving only the immobilized phages behind. Because those phages were far too few in number to analyze directly, his team propagated them using the technique described above. The genius of the scheme, which came to be called “phage display,” was that it combined two essential features of natural evolution: diversification, in this case the creation of immense artificial libraries of phage-borne proteins; and selection, scientists’ ability to artificially select useful phages by exploiting their binding affinity. “Evolution in a test tube,” Smith called it during a packed press conference at MU’s Memorial Union. “You very much simplify it. And also — and this is important — you don’t let nature’s natural selection create the pressure on survival. You, the experimenter, decide.” Phage display has since been deployed by thousands of researchers around the world. Smith’s co-Nobel recipient Greg Winter was among the first to recognize its value, using it to develop antibodies that eventually led to successful treatments for rheumatoid arthritis, psoriasis and inflammatory bowel diseases. Future phage-enabled discoveries, the Royal Academy said, are poised to “promote a greener chemicals industry, produce new materials, manufacture sustainable biofuels, mitigate disease and save lives.”— Charles E. Reineke
MICHAEL CALI
Mizzou’s First Nobel Prize
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