Research

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

Tamara Bar-Magen¹ , Richard D Sloan¹ , Verena H Faltenbacher¹ , Daniel A Donahue^1,2 , Björn D Kuhl^1,3 , Maureen Oliveira¹ , Hongtao Xu¹ and Mark A Wainberg^1,2,3

¹  McGill University AIDS Centre, Lady Davis Institute-Jewish General Hospital, Montreal, Quebec, Canada

²  Department of Microbiology and Immunology, McGill University, Montreal, Quebec H3A 2T5, Canada

³  Division of Experimental Medicine, McGill University, Montreal, Quebec H3A 2T5, Canada

author email corresponding author email

Retrovirology 2009, 6:103doi:10.1186/1742-4690-6-103

Published:	11 November 2009

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.