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Researchers discover interaction site of HIV-1 and antiviral protein
Albin JS. J Biol Chem. 2010;285:40785-40792.
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University of Minnesota researchers have found where HIV-1 binds to and destroys a specific human antiviral protein, known as APOBEC3F, which restricts the infectivity of HIV-1 in the absence of the viral accessory protein virion infectivity factor.
Previous research demonstrated that human cells produce antiviral proteins — APOBEC3F and APOBEC3G — that have the ability to destroy HIV-1. However, HIV-1 has developed a way to overcome restriction using an accessory protein, virion infectivity factor (Vif), to degrade the APOBEC proteins and allow the virus to spread, according to background information in the study.
John Albin, MD-PhD student at the University of Minnesota, and colleagues assessed how HIV-1 interacts with APOBEC3F.
The researchers found that a simple chemical change may alter the APOBEC3F protein to make it a more effective antiviral agent. Shielding of a common attribute shared by associated proteins may yield similar outcomes, according to the researchers.
“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 said in a press release. “Such an intervention has the potential to allow as many as seven natural antiviral drugs to spring into action and prevent HIV from spreading.”
According to Albin, this research shows potential for a novel approach to combating HIV/AIDS that would seek to stabilize and harness the innate antiviral activity of certain human proteins.
“This should raise awareness among physicians and patients that it may be possible to fight infection not by inhibiting the virus itself, but rather by facilitating the body’s natural defenses. A great deal of additional research and development will be required,” Albin told Infectious Disease News. – by Ashley DeNyse
Disclosures: Dr. Albin reports no relevant disclosures.
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