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Comparative biochemical analysis of HIV-1 subtype B and C integrase enzymes

Author(s): Bar-Magen Tamara | Sloan Richard | Faltenbacher Verena | Donahue Daniel | Kuhl Björn | Oliveira Maureen | Xu Hongtao | Wainberg Mark

Journal: Retrovirology
ISSN 1742-4690

Volume: 6;
Issue: 1;
Start page: 103;
Date: 2009;
Original page

Abstract Background Integrase inhibitors are currently being incorporated into highly active antiretroviral therapy (HAART). Due to high HIV variability, integrase inhibitor efficacy must be evaluated against a range of integrase enzymes from different subtypes. Methods This study compares the enzymatic activities of HIV-1 integrase from subtypes B and C as well as susceptibility to various integrase inhibitors in vitro. The catalytic activities of both enzymes were analyzed in regard to each of 3' processing and strand transfer activities both in the presence and absence of the integrase inhibitors raltegravir (RAL), elvitegravir (EVG), and MK-2048. Results Our results show that integrase function is similar with enzymes of either subtype and that the various integrase strand transfer inhibitors (INSTIs) that were employed possessed similar inhibitory activity against both enzymes. Conclusion This suggests that the use of integrase inhibitors against HIV-1 subtype C will result in comparable outcomes to those obtained against subtype B infections.
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