New view into protein folding could lead to development of better flu vaccines


Cornell researchers have discovered a novel observation method that could send influenza to the outskirts of health concerns at some point in the near future.

Illustrated in the July 16 edition of the Proceedings of the National Academy of Sciences, the technique involved experts taking snapshots of ribosomes during different stages of protein production. Once the microcellular photo session concluded, scientists pieced the images together, panoramically reconstructing protein-folding processes that occur during synthesis. Researchers found that following the function of proteins from inception could eventually lead to more advanced flu vaccines, among other medical applications.

"Like a magnifier, we enrich a small pool from the bigger ocean and then paint a picture from early to late stages of the process," said Shu-Bing Qian, assistant professor of nutritional sciences and corresponding author of the paper, regarding the team's protein photographing practice.

Qian and Yan Han (the lead author of the study), along with other colleagues, said their method could lead to a better understanding of the protein hemagglutinin (HA), which is located at the surface level of the influenza A virus. Common scientific knowledge dictates that HA infects the cell due to something within its intricate folding structure; thus, tracing the pitiless protein back to its origins could cause the modus operandi of influenza A to unravel.

"Folding is a very fundamental issue in biology," Qian continued. "It's been a long-term mystery how the cell achieves this folding successfully, with such speed and with such a great success rate."

The foundation of flu vaccines is cemented by antibodies that recognize proteins like HA. Up to this point, the mutation rates of viruses — HA has the highest mutation degree of all the flu virus surface proteins — have allowed for sickness to evade most vaccination resistance, and surface proteins play a particularly predominant role in this antibody aversion. Knowing the enemy’s lineage could prove integral in winning the battle against one of health’s most familiar adversaries.

"If people know the folding picture of how a mutation changes, it will be helpful for designing a better vaccine," Qian said. 

Perhaps scratching the surface, in cases such as these, is all that’s required to eliminate a long-term itch.