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Related Experiment Video

Updated: Jun 4, 2026

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

Published on: June 26, 2019

The nuclear pore complex: a new dynamic in HIV-1 replication.

Cora L Woodward¹, Samson A Chow

¹Department of Molecular and Medical Pharmacology, and UCLA AIDS Institute, UCLA School of Medicine, Los Angeles, CA, USA.

Nucleus (Austin, Tex.)

|February 18, 2011

Summary

Human immunodeficiency virus type 1 (HIV-1) enters the nucleus by binding its preintegration complex (PIC) to the nucleoporin NUP153. This interaction facilitates nuclear pore complex (NPC) passage for viral cDNA integration.

Keywords:

NUP153 human immunodeficiency virus type 1 integrase nuclear import nuclear pore complex nucleoporin preintegration complex

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Published on: January 19, 2015

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

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Related Experiment Videos

Last Updated: Jun 4, 2026

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

Published on: June 26, 2019

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

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

Area of Science:

Virology
Molecular Biology
Cell Biology

Background:

Human immunodeficiency virus type 1 (HIV-1) and other lentiviruses can infect non-dividing cells by entering the nucleus.
The specific viral factors and mechanisms governing HIV-1 nuclear entry remain largely undefined.
The nuclear envelope presents a barrier that HIV-1 must overcome to initiate infection.

Purpose of the Study:

To elucidate the mechanism of HIV-1 nuclear import.
To identify viral factors involved in traversing the nuclear envelope.
To understand how HIV-1 interacts with the nuclear pore complex (NPC).

Main Methods:

Investigated the role of nucleoporins in HIV-1 nuclear import.
Focused on the interaction between the HIV-1 preintegration complex (PIC) and NUP153.
Utilized findings on the binding of integrase (IN) to NUP153's C-terminal domain.

Main Results:

Identified a functional role for nucleoporin NUP153 in the nuclear import of the HIV-1 PIC.
Demonstrated that HIV-1 sub-viral particles interact directly with the NPC.
Showed that PIC-associated integrase (IN) binds to the C-terminal domain of NUP153.

Conclusions:

HIV-1 nuclear entry involves direct interaction with the NPC via IN-NUP153 binding.
NPC conformation and composition may influence PIC nuclear import and viral cDNA integration.
This mechanism is crucial for the integration of viral cDNA into actively transcribed genes.