About 300,000 individuals perish annually due to hepatitis C. A recent study has unveiled the protein complex that allows the virus to invade our cells, which may lead to the discovery of an effective vaccine.
Approximately 58 million people live with chronic inflammation triggered by the hepatitis C virus, and each year, 300,000 lives are lost to this condition.
To date, no treatment has succeeded in decreasing the global rates of hepatitis C, prompting researchers to explore the development of a vaccine. However, a lack of understanding regarding the protein complex that permits the virus to infect cells has hindered progress.
Fortunately, a new study from a multidisciplinary team at the University of Copenhagen aims to change this scenario.
“We are the first to identify the protein complex on the hepatitis C virus’s surface that allows it to attach to our cells,” explains Associate Professor Jannick Prentø.
“Understanding the structure of this protein complex will help us design potential vaccines that can stop the virus from invading the cells,” says Postdoc Elias Augestad.
This protein complex is essential for the virus’s attachment to cells. In contrast to the coronavirus’s well-known spike protein with its distinctive spikes, the hepatitis C virus has a different structure, but its protein complex performs the same function.
Advances vaccine research
This study acts as a foundational guide for developing a hepatitis C vaccine. Researchers are optimistic that they can leverage this newfound understanding to create a vaccine that prompts the immune system to generate antibodies capable of effectively binding to the hepatitis C virus’s surface, rendering it inactive.
“Producing and purifying the protein complex is incredibly challenging, which is why it has not been accomplished until now. The design of these proteins on the hepatitis C virus’s surface makes them exceptionally fragile. Scientists were unsure of their structure, leading to failures when trying to recreate them in a lab as they would disintegrate before detailed examination could take place,” remarks Associate Professor Jannick Prentø.
“However, we successfully described their structure, which allowed us to replicate these protein complexes outside of the cells and study them thoroughly,” states Associate Professor Pontus Gourdon.
