A supramolecular assembly mediates lentiviral DNA integration

Author:

Ballandras-Colas Allison1,Maskell Daniel P.1,Serrao Erik23,Locke Julia4,Swuec Paolo4,Jónsson Stefán R.5,Kotecha Abhay6,Cook Nicola J.1,Pye Valerie E.1,Taylor Ian A.7,Andrésdóttir Valgerdur5,Engelman Alan N.23,Costa Alessandro4,Cherepanov Peter18

Affiliation:

1. Chromatin Structure and Mobile DNA, The Francis Crick Institute, London NW1 1AT, UK.

2. Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA 02215, USA.

3. Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.

4. Macromolecular Machines Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

5. Institute for Experimental Pathology, University of Iceland, Keldur, 112 Reykjavik, Iceland.

6. Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.

7. Macromolecular Structure Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

8. Division of Medicine, Imperial College London, London W2 1PG, UK.

Abstract

High-resolution insights into the intasome An essential step in the life cycle of lentiviruses such as HIV-1 is when viral DNA integrates into the host genome, establishing a permanent infection of the host cell. The viral integrase enzyme catalyzes this process and is a major drug target. During viral integration, integrase binds the ends of viral DNA, forming a higher-order structure called the intasome. Passos et al. and Ballandras-Colas et al. used cryo—electron microscopy to solve the structures of the intasomes from HIV-1 and maedi-visna virus (ovine lentivirus), respectively. These structures reveal how integrase self-associates to form a functional intasome and help resolve previous conflicting models of intasome assembly. Science , this issue p. 89 , p. 93

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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