JAMA  Published Online: March 25, 2026 
Sanjay Kishore, MD1; Margaret Hayden, MD, MPhil1; Micah Johnson, MD2

Since initially becoming available in 2013, direct-acting antivirals (DAAs) have transformed the treatment of hepatitis C virus (HCV) infection. Treatment is well tolerated and results in cure (sustained virologic response) in more than 95% of individuals. However, only about a third of people in the US with HCV infection receive treatment within a year of diagnosis, an estimated 2.5 million to 4 million remain chronically infected, and incident cases of HCV have increased during the last decade.1,2 To better understand how the use of DAAs has evolved in the US, this study measured changes in patient and prescriber characteristics for these medications from 2013 to 2025.

TO READ FULL ARTICLE:https://jamanetwork.com/journals/jama/fullarticle/2846850​

Scripps Research scientists reengineer critical proteins on the surface of HCV, paving the way for a new vaccine design.  March 03, 2026

LA JOLLA, CA--Hepatitis C virus (HCV) infects an estimated 50 million people worldwide, according to the World Health Organization, and remains a leading cause of cirrhosis and liver cancer. While antiviral drugs can cure most infections, global access remains limited and these drugs do not stop reinfection.
This is why a durable vaccine is critically needed. Developing one has proven exceptionally challenging, however, as HCV evades immune detection using two distinct proteins that coat its surface. These proteins, known collectively as the E1E2 glycoprotein complex, have been historically difficult to produce in the stable, native form needed for vaccination.
In a new Nature Communications study, scientists at Scripps Research have now engineered that native-like, stabilized version of HCV’s E1E2 complex and used it to build a nanoparticle-based vaccine candidate. The approach uses a technology called self-assembling protein nanoparticles, or SApNPs, which organizes many copies of the proteins into virus-like clusters that the immune system can more easily recognize. The study was published as an article-in-press on February 11, 2026.
“Our lab focuses on all the major virus families, including those with surface proteins that are too unstable to use in traditional vaccines,” says senior author Jiang Zhu, professor at Scripps Research. “For HCV, the central problem for decades has been that the two surface proteins, E1 and E2, fall apart or misassemble when removed from the virus. In this study, we were able to stabilize the native E1–E2 interface and generate a soluble complex that faithfully mimics the viral surface.”
On HCV’s viral surface, E1 and E2 form tightly linked pairs known as heterodimers. Together, they both shield the virus from immune attack and allow it to attach to and enter human cells. Because vaccines train the immune system to recognize viral proteins, scientists must first recreate accurate copies of them in the lab. However, the E1 and E2 glycoproteins are notoriously difficult and labor-intensive to manufacture: once removed from the virus, they often misfold or fall apart.
For more than two decades, scientists been attempting to produce this stable, soluble E1E2 complex that preserves the correct interface between the two proteins. Without it, vaccines cannot teach the body’s immune system to recognize HCV’s true viral structure. It’s remained a major unsolved challenge in the HCV field at large.

TO CONTINUE: https://www.scripps.edu/news-and-events/press-room/2026/20260303-zhu-nanoparticle-vaccine.html