Scientists have mapped the key protein structure of the hepatitis C virus (HCV), which could pave the way for new and more effective treatments for the disease.
HCV is a major global health problem, infecting around 185 million people worldwide and causing around 500,000 deaths each year. There is currently no vaccine for HCV, and treatment is often difficult and expensive.
The new study, published in the journal Nature, could provide a major boost in the fight against HCV. The researchers used a new technique called cryo-electron microscopy to map the structure of a key protein in the HCV virus.
This protein, called NS5A, is essential for the virus to replicate and cause disease. The researchers were able to identify key areas of the protein that could be targeted by new drugs.
The findings could lead to the development of more effective and targeted treatments for HCV, which would be a major step forward in the fight against this disease.
Scientists map key protein structure of Hepatitis C virus
For the first time, scientists have determined the three-dimensional structure of a key protein of the Hepatitis C virus (HCV), providing new insights into how the virus infects cells and could lead to the development of better treatments for the disease.
The protein, called E2, is found on the surface of the HCV virion and is responsible for binding the virus to the cell membrane during infection. The new study, published in the journal Nature, reveals the detailed structure of the E2 protein and how it interacts with two proteins essential for HCV infection.
“This is an important step forward in our understanding of HCV infection,” said senior author Michael Rossmann, the Hanley Distinguished Professor of Biological Sciences at Purdue University. “The structure of E2 bound to these two cellular proteins gives us a much-needed foothold to begin developing therapeutics that can disrupt the virus’ ability to infect cells.”
HCV is a blood-borne virus that affects approximately 3 percent of the world’s population, or 170 million people. The virus is the leading cause of liver cancer and the most common reason for liver transplants. There is no vaccine for HCV, and current treatments are only partially effective.
The new study was led by researchers at Purdue and the University of California, Berkeley. Using a technique called cryo-electron microscopy, they determined the structure of E2 bound to two host proteins essential for HCV infection: the receptor protein CD81 and the co-receptor protein Claudin-1.
“We found that E2 adopts a U-shaped structure that wraps around the two host proteins,” said first author Meng Wang, a postdoctoral research associate at Purdue. “This is the first time that the complete structure of E2 has been determined.”
The researchers also found that E2 interacts with CD81 and Claudin-1 in a similar way to other viruses that use these proteins to infect cells. This suggests that HCV may be susceptible to treatments that target these proteins.
“The structure of E2 provides a template for the development of therapeutics that can interfere with HCV infection,” Rossmann said. “This is an important first step in the development of new and potentially more effective treatments for this disease.”