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According to the World Health Organization, an estimated 1 billion people get the flu each year, 3-5 million become seriously ill, and up to 650,000 flu-related respiratory deaths occur. Seasonal influenza vaccines must be readjusted each year, primarily for prevalent strains. Vaccines are highly effective when they match the dominant strain. But if they don’t match, you may get little protection.
The main targets of influenza vaccines are two surface glycoproteins, hemagglutinin (HA) and neuraminidase (NA). The HA protein helps the virus bind to the host cell, while the NA protein acts like a pair of scissors that cut HA from the cell membrane, allowing the virus to replicate.
Although the properties of both glycoproteins have been studied previously, a complete understanding of their movements does not exist.
Researchers at the University of California, San Diego have created the first atomic-level computer model of the H1N1 virus. This model reveals new vulnerabilities through glycoprotein ‘breathing’ and ’tilting’ movements. This work, published in ACS Central Sciencesuggesting possible strategies for the design of future vaccines and antiviral agents against influenza.
“When I first saw how dynamic these glycoproteins were, how much respiration and tilt they had, I really thought there was something wrong with the simulation,” said the project’s principal investigator. said Rommie Amaro, Distinguished Professor of Chemistry and Biochemistry. “Once we knew our model was correct, we realized the great potential of this discovery. can be used for
