Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Inhibitors of Virion Maturation and Assembly

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...

Intralumenal Vesicles and Multivesicular Bodies

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...

Pinching-off of Coated Vesicles

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

Retrovirus Life Cycles

Retrovirus Life Cycles

Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the retrovirus to...

ER Retrieval Pathway

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...

Retroviruses

Retroviruses

Retroviruses and retrotransposons both insert copies of their genetic elements into the genome of the host cell. Thus, the viral genes are passed on when the host genome is replicated or translated. A typical retroviral DNA sequence contains 3-4 genes that encode the different proteins required for its structural assembly and function as a molecular parasite. This DNA is transcribed into a single mRNA, which is very similar in structure to conventional mRNAs, i.e., it is capped at the 5’...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

VMA21 deficiency leads to autophagic dysregulation and altered vesicle trafficking in X-linked myopathy with excessive autophagy.

Acta neuropathologica·2026

Same author

Antibody-mediated targeting of SOSIP HIV-1 Env to skin Langerhans cells potentiates humoral responses.

EBioMedicine·2026

Same author

Beyond the Protocol: Revisiting the Critical Role of Donor Plants in Cryopreservation of Economically Important Clonal Crops.

Plants (Basel, Switzerland)·2026

Same author

Exposure to a high-fat diet compromises gut health, behavior, and HPA axis function, with partial reversal when limited to adolescence.

Brain research bulletin·2026

Same author

Lack of evidence for cargo release of CD63-EVs into recipient cells.

Scientific reports·2026

Same author

J-domain proteins: from molecular mechanisms to diseases.

Cell stress & chaperones·2025

Search research articles

Related Experiment Video

Updated: Jun 26, 2026

High Throughput In Vitro Assessment of Latency Reversing Agents on HIV Transcription and Splicing

High Throughput In Vitro Assessment of Latency Reversing Agents on HIV Transcription and Splicing

Published on: January 22, 2019

The ESCRT pathway and HIV-1 budding.

Yoshiko Usami¹, Sergei Popov, Elena Popova

¹Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.

Biochemical Society Transactions

|January 16, 2009

Summary

HIV-1 uses L domains to recruit ESCRT proteins for virus budding. Overexpressing Alix or Nedd4-2s can rescue budding defects, highlighting their roles in ESCRT regulation.

More Related Videos

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Published on: March 8, 2012

Related Experiment Videos

Last Updated: Jun 26, 2026

High Throughput In Vitro Assessment of Latency Reversing Agents on HIV Transcription and Splicing

High Throughput In Vitro Assessment of Latency Reversing Agents on HIV Transcription and Splicing

Published on: January 22, 2019

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Published on: March 8, 2012

Area of Science:

Virology
Cell Biology
Molecular Biology

Background:

HIV-1 Gag protein utilizes L domains to interact with the ESCRT pathway, facilitating virus budding.
The PTAP L domain recruits ESCRT-I via Tsg101, while the LYPX(n)L domain recruits Alix, an ESCRT-III binding partner.

Purpose of the Study:

To investigate the roles of Alix and Nedd4-2s in HIV-1 budding and ESCRT pathway regulation.
To understand how the overexpression of specific proteins can rescue HIV-1 budding defects.

Main Methods:

Analysis of HIV-1 Gag interactions with ESCRT components.
Investigating the effects of overexpressing Alix and Nedd4-2s on viral budding.
Studying the functional domains and interactions of ESCRT proteins (CHMPs) and ubiquitin ligases.

Main Results:

HIV-1 budding is impaired without the PTAP L domain but can be rescued by Alix overexpression, dependent on CHMP4 interaction.
Overexpression of Nedd4-2s, a ubiquitin ligase, also corrects budding defects, even in the absence of PPXY L domains.
Nedd4-2s appears to stimulate PTAP L domain activity, suggesting regulation of ESCRT-I.

Conclusions:

Alix and CHMP recruitment are critical for driving HIV-1 release.
Nedd4-2s may regulate ESCRT-I activity, offering a potential new target for antiviral strategies.
The ESCRT pathway's intricate regulation by viral proteins and host factors is crucial for viral replication.