Cryo-EM structure of the deltaretroviral intasome in complex with the PP2A regulatory subunit B56γ

Michał S. Barski, Jordan J. Minnell, Zuzana Hodakova, Valerie E. Pye, Andrea Nans, Peter Cherepanov and Goedele N. Maertens ()
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Michał S. Barski: Imperial College London, St Mary’s Hospital, Department of Infectious Disease, Section of Virology
Jordan J. Minnell: Imperial College London, St Mary’s Hospital, Department of Infectious Disease, Section of Virology
Zuzana Hodakova: Chromatin Structure and Mobile DNA Laboratory, The Francis Crick Institute
Valerie E. Pye: Chromatin Structure and Mobile DNA Laboratory, The Francis Crick Institute
Andrea Nans: Structural Biology Science Technology Platform, The Francis Crick Institute
Peter Cherepanov: Imperial College London, St Mary’s Hospital, Department of Infectious Disease, Section of Virology
Goedele N. Maertens: Imperial College London, St Mary’s Hospital, Department of Infectious Disease, Section of Virology

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Human T-cell lymphotropic virus type 1 (HTLV-1) is a deltaretrovirus and the most oncogenic pathogen. Many of the ~20 million HTLV-1 infected people will develop severe leukaemia or an ALS-like motor disease, unless a therapy becomes available. A key step in the establishment of infection is the integration of viral genetic material into the host genome, catalysed by the retroviral integrase (IN) enzyme. Here, we use X-ray crystallography and single-particle cryo-electron microscopy to determine the structure of the functional deltaretroviral IN assembled on viral DNA ends and bound to the B56γ subunit of its human host factor, protein phosphatase 2 A. The structure reveals a tetrameric IN assembly bound to two molecules of the phosphatase via a conserved short linear motif. Insight into the deltaretroviral intasome and its interaction with the host will be crucial for understanding the pattern of integration events in infected individuals and therefore bears important clinical implications.

Date: 2020
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DOI: 10.1038/s41467-020-18874-y

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