Structural characterization of a 2'F-RNA aptamer that binds a HIV-1 SU glycoprotein,gp120 |
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Authors: | Sayer N Ibrahim J Turner K Tahiri-Alaoui A James W |
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Institution: | Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK. |
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Abstract: | Here we describe the isolation of specific 2'F-substituted RNA ligands for the SU glycoprotein, gp120, of HIV-1 strain HXB2. These aptamers bind the target protein with an affinity of the order of 10(-7) M. Binding was specific to SU glycoprotein and directed to a non-neutralizing epitope that was not shared with the related strain, HIV-1(BaL). The structure of one aptamer was defined by a combination of deletion analysis and enzymatic probing studies, revealing a 42 nt minimal element comprising a three-helix junction that retained the binding affinity of the parental sequence. Interestingly, binding to SU glycoprotein was accompanied by structural changes in the aptamer that stabilized the weakest of the 3 helices. |
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Keywords: | HIV Aptamer Neutralization RNA structure Diagnostics |
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