Computer Model of Influenza Virus Shows Universal Vaccine Promise


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According to the World Health Organization, there are an estimated 1 billion cases of flu each year, between 3 and 5 million severe cases, and up to 650,000 flu-related respiratory deaths worldwide. Seasonal flu vaccines must be reformulated each year to match the predominately circulating strains. When the vaccine matches the predominant strain, it is highly effective; however, if it doesn’t match, it may offer little protection.

The main targets of the flu vaccine are two surface glycoproteins, hemagglutinin (HA) and neuraminidase (NA). While the HA protein helps the virus bind to the host cell, the NA protein acts like scissors to cut the HA away from the cell membrane, allowing the virus to replicate.

Although the properties of both glycoproteins have been studied before, a complete understanding of their movement does not exist.

For the first time, researchers at the University of California San Diego have created an atomic-level computer model of the H1N1 virus that reveals new vulnerabilities through glycoprotein “breathing” and “tilting” movements. This work, published in ACS Central Sciencesuggests possible strategies for the design of future flu vaccines and antivirals.

“When we first saw how dynamic these glycoproteins were, the great amount of breathing and tilting, we actually wondered if there was something wrong with our simulations,” says Distinguished Professor of Chemistry and Biochemistry Rommie Amaro, who is the principal investigator of the study. the project is. . “Once we knew our models were correct, we realized the enormous potential of this discovery. This research could be used to develop methods to keep the protein open so that it is constantly accessible to antibodies.

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