We are exploring a novel approach against Aids by targeting the structure and function of non-coding RNA elements in the genome of HIV-1

The Ψ-packaging domain within the 5'UTR of HIV-1 is used to specify for and control the packaging of the genomic RNA into a budding immature viron. Interference, through mutations and deletions, to the structure of the Ψ-packaging domain severely diminish the ability of the virus to correctly package genomic RNA. The Gag polypeptide is heavily involved in the binding, coating, trafficking and packaging of genomic RNA. These processes are believed to be initiated by the structural rearrangement of the Ψ-packaging domain, upon binding of Gag. In collaboration with Professor Andrew Lever in the Department of Medicine (Cambridge) we are exploring these structural elements involved in HIV function and infectivity. Our major goal is the validation and exploitation of such structures as targets for molecular therapeutics.

 

References:

Comparative Structural Effects of HIV-1 Gag and Nucleocapsid Proteins in Binding to and Unwinding of the Viral RNA Packaging Signal
N M Bell; J C Kenyon; S Balasubramanian; A M L Lever
Biochemistry, 51 (15) 3162-9 (2012)
DOI: 10.1093/nar/gks068
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