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Structures and functions of the C-Terminal domain of HIV-1 integration

Abstract : HIV Integrase is a DNA recombinase that catalyzes two endonucleolytic reactions that allow the viral DNA integration into host DNA for replication and subsequent viral protein production. HIV Integrase consists of 3 structural and functional domains: The N-terminal zinc domain involved in 3’ processing and strand transfer, the catalytic core domain which contains the active site, and the C-terminal domain that binds DNA non- specifically. Recent research highlights the importance of the CTD in binding with other viral proteins such as Reverse Transcriptase. The aim of the thesis was to understand the roles and importance of the C-terminal domain of HIV-1 Integrase in two contexts: chromatin integration, and co-evolution, with the overall purpose of understanding the role of multimerization in IN function. Overall, results from my project indicate that the IN-CTD plays an important role, by contributing to the formation of higher order multimers that are important for IN functionality.
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Submitted on : Monday, July 2, 2018 - 11:30:06 AM
Last modification on : Friday, October 23, 2020 - 4:45:54 PM
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  • HAL Id : tel-01827378, version 1



Oyindamola Oladosu. Structures and functions of the C-Terminal domain of HIV-1 integration. Immunology. Université de Strasbourg, 2017. English. ⟨NNT : 2017STRAJ025⟩. ⟨tel-01827378⟩



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