Inhibition of Vif-Cul5 Interaction Through Use of Zinc Chelator

The Vif ? A3G axis is one of the most promising new drug targets in HIV research. Previous studies have discovered that Vif is an HIV-derived protein that acts to derail antiviral efforts from the host cell. Vif tags Apobec3G (A3G), an antiviral host factor, with ubiquitin for destruction in the 26S proteasome in addition to partially inhibiting the expression of new A3G proteins. In the absence of Vif, A3G is incorporated into the HIV virus and severely decreases the infectivity of progeny virions. Scientists at JHU have identified a zinc-stabilized interface required for the interaction between Vif proteins and a critical part of the ubiquitin proteasome machinery, Cullin-5. Using a zinc chelator, JHU scientists disrupted the Vif-Cullin5 interaction and in doing so inhibited HIV Vif-mediated A3G degradation allowing the antiviral function of A3G to proceed. Description (Set) Proposed Use (Set) In the United States alone, currently one million people are living with either HIV or AIDS. Around the world, approximately 42 million people are estimated to be infected with HIV; 22 million have already died from AIDS. The market reach of an effective HIV drug would be vast. Current anti-viral drugs have focused on targeting viral protein functions such as reverse transcription and the proteasome but have failed due to high mutation rates of the HIV virus and patient non-compliance resulting from complicated treatment regimes. Disruption of the zinc-stabilized Vif-Cullin5 interaction represents a novel strategy for the development of anti-viral drugs for the treatment of HIV and the prevention of AIDS.

Inventor(s): Yu, Xiao-fang

Type of Offer: Licensing

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