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Related Experiment Video

Updated: Apr 11, 2026

Amplification, Next-generation Sequencing, and Genomic DNA Mapping of Retroviral Integration Sites

Amplification, Next-generation Sequencing, and Genomic DNA Mapping of Retroviral Integration Sites

Published on: March 22, 2016

Structural basis for retroviral integration into nucleosomes.

Daniel P Maskell¹, Ludovic Renault², Erik Serrao³

¹Chromatin Structure and Mobile DNA, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK.

|June 11, 2015

Summary

This summary is machine-generated.

Prototype foamy virus intasome captures nucleosomes for retroviral DNA integration. This interaction involves specific DNA and histone contacts, enabling integration at preferred genomic locations.

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Assembly and Purification of Prototype Foamy Virus Intasomes

Assembly and Purification of Prototype Foamy Virus Intasomes

Published on: March 19, 2018

Area of Science:

Molecular Biology
Virology
Structural Biology

Background:

Retroviral DNA integration is mediated by the integrase (IN) enzyme, forming a stable intasome complex on viral DNA.
Chromosomal DNA is organized into nucleosomal arrays, and the mechanism by which intasomes interact with nucleosomes for integration is not understood.

Purpose of the Study:

To elucidate the molecular mechanism of how the prototype foamy virus (PFV) intasome interacts with and targets nucleosomal DNA for retroviral integration.

Main Methods:

Single-particle cryo-electron microscopy (cryo-EM) was used to determine the structure of the intasome-nucleosome complex.
Biochemical assays were performed to assess the impact of specific amino acid substitutions on intasome-nucleosome interactions and integration efficiency.

Main Results:

The PFV intasome stably captures nucleosomes through multivalent interactions involving both DNA gyres and the H2A-H2B heterodimer.
Integration occurs at preferred superhelix locations (±3.5) due to DNA lifting from the H2A-H2B surface, while the histone octamer remains intact.
Mutations disrupting these contacts impair nucleosome engagement and alter viral integration site distribution in the genome.

Conclusions:

The study reveals the molecular basis for nucleosome recognition and capture by the viral DNA recombination machinery.
Nucleosome plasticity, specifically the ability to lift DNA from histone surfaces, is crucial for enabling retroviral integration at specific genomic sites.