Researchers at the University of Minnesota have discovered how HIV binds to and destroys a specific human antiviral protein called APOBEC3F. The results suggest that a simple chemical change can convert APOBEC3F to a more effective antiviral agent and that shielding of a common feature shared by related proteins may yield a similar outcome.
This discovery highlights the potential for a novel approach to combating HIV/AIDS that would seek to stabilize and harness the innate antiviral activity of certain human proteins, according to lead author John Albin, a researcher in the laboratory of Reuben Harris, associate professor of biochemistry, molecular biology and biophysics in the College of Biological Sciences.
The finding was published in the Journal of Biological Chemistry. For a copy of the abstract and/or full article, contact Preston Smith or John Albin.
Human cells produce a family of antiviral proteins (called APOBECs) that have the unique and natural ability to destroy HIV. But HIV has evolved a way to overcome restriction using an accessory protein called Vif (virion infectivity factor) to degrade the APOBEC proteins and allow the virus to spread. Albin and colleagues learned where Vif interacts with one antiviral protein, APOBEC3F, and showed how the connection can be interrupted by a simple chemical change on the surface of APOBEC3F. They also noted that similar interaction sites are found on the same surface in other members of this antiviral protein family.
"This suggests that the interaction between Vif and these antiviral APOBEC proteins could be blocked with a drug that would shield the Vif interaction region," Albin says. "Such an intervention has the potential to allow as many as seven natural antiviral drugs to spring into action and prevent HIV from spreading."
The Harris lab is focuses on understanding every level of the vital interaction between these human cellular proteins and HIV Vif.
|Contact: John Albin|
University of Minnesota