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Related Experiment Video

Updated: Jun 13, 2026

Measurement of In Vitro Integration Activity of HIV-1 Preintegration Complexes

Measurement of In Vitro Integration Activity of HIV-1 Preintegration Complexes

Published on: February 22, 2017

Nucleoprotein intermediates in HIV-1 DNA integration visualized by atomic force microscopy.

Svetlana Kotova¹, Min Li, Emilios K Dimitriadis

¹Laboratory of Bioengineering and Physical Science, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892, USA.

Journal of Molecular Biology

|April 27, 2010

Summary

Human immunodeficiency virus type 1 (HIV-1) integrase forms stable complexes called intasomes with viral DNA. These intasomes are crucial for viral replication and integration into host DNA.

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Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Published on: July 18, 2011

Area of Science:

Molecular Biology
Virology
Structural Biology

Background:

HIV-1 DNA integration into host genomes is vital for viral replication.
This process is mediated by the HIV-1 integrase protein.

Purpose of the Study:

To investigate the structure and dynamics of HIV-1 integrase-DNA complexes.
To understand the role of integrase in viral DNA integration using atomic force microscopy.

Main Methods:

Atomic Force Microscopy (AFM) was employed to visualize stable complexes.
Time-course experiments were conducted to study intasome assembly intermediates.

Main Results:

A tetramer of HIV-1 integrase stably bridges viral DNA ends, forming a stable intasome.
Intasomes exhibit high stability in high ionic strength conditions.
Integrase tetramers associate tightly with viral DNA ends, suggesting specific binding interactions.
The integration product remains bound by the integrase tetramer, with target DNA ends free to rotate.

Conclusions:

The study elucidates the structural organization of HIV-1 intasomes.
Findings suggest distinct conformations of integrase tetramers in solution versus within intasomes.
The dynamics of target DNA interaction within the intasome complex are revealed.