Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

4.1K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
4.1K
Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

3.0K
Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a...
3.0K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

5.3K
The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
5.3K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

15.6K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
15.6K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.8K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.8K
Protein Complex Assembly02:41

Protein Complex Assembly

13.4K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
13.4K

You might also read

Related Articles

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

Sort by
Same author

A Viral Protein Antagonist for Both AID and APOBEC3.

Viruses·2026
Same author

Apobec-mediated retroviral hypermutation in vivo is dependent on mouse strain.

PLoS pathogens·2024
Same author

Apobec-Mediated Retroviral Hypermutation <i>In Vivo</i> is Dependent on Mouse Strain.

bioRxiv : the preprint server for biology·2023
Same author

APOBECs: Our fickle friends?

PLoS pathogens·2023
Same author

A Retrotranslocation Assay That Predicts Defective VCP/p97-Mediated Trafficking of a Retroviral Signal Peptide.

mBio·2022
Same author

Glossopharyngeal and Vagus Nerve Palsy in a Child With Scrub Typhus Meningitis.

Indian pediatrics·2021
Same journal

Correction: Bulatov et al. Camelpox Virus in Western Kazakhstan: Assessment of the Role of Local Fauna as Reservoirs of Infection. <i>Viruses</i> 2024, <i>16</i>, 1626.

Viruses·2026
Same journal

Correction: Franco et al. Whole Blood Volume-Based Absolute Quantification of HTLV-1 Proviral Load: A Comparative Method Evaluation Study. <i>Viruses</i> 2026, <i>18</i>, 580.

Viruses·2026
Same journal

Correction: Medkour et al. Adenovirus Infections in African Humans and Wild Non-Human Primates: Great Diversity and Cross-Species Transmission. <i>Viruses</i> 2020, <i>12</i>, 657.

Viruses·2026
Same journal

Burden of Malaria and Dengue Across Global, Asian, and Chinese Populations Based on GBD 2021 Data: A Quantitative Assessment of Importation Risks to China.

Viruses·2026
Same journal

First Report of <i>Orthonairovirus songlingense</i> in <i>Haemaphysalis concinna</i> Ticks from Russia.

Viruses·2026
Same journal

Epidemiological and Virological Characteristics of H9N2 Avian Influenza Virus in Jiangsu Province, China, 2024.

Viruses·2026
See all related articles

Related Experiment Video

Updated: Oct 18, 2025

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

18.4K

How Viruses Use the VCP/p97 ATPase Molecular Machine.

Poulami Das1, Jaquelin P Dudley1,2

  • 1Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.

Viruses
|September 28, 2021
PubMed
Summary
This summary is machine-generated.

The valosin-containing protein (VCP), also known as p97, is crucial for viral replication. Targeting this host factor could lead to broad-spectrum antiviral therapies.

Keywords:
ERADVCPantiviral immune responsecellular traffickingegressp97retrotranslocationuncoatingvirus replication

More Related Videos

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
07:24

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

Published on: March 27, 2016

9.2K
Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16
06:03

Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16

Published on: July 15, 2019

8.1K

Related Experiment Videos

Last Updated: Oct 18, 2025

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

18.4K
In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
07:24

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

Published on: March 27, 2016

9.2K
Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16
06:03

Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16

Published on: July 15, 2019

8.1K

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Viruses rely on host cell machinery for replication, making host factors essential targets for viral strategies.
  • The valosin-containing protein (VCP), also known as p97, is a highly conserved AAA ATPase involved in diverse cellular functions.

Purpose of the Study:

  • To investigate the role of the host protein VCP/p97 in the replication of various viruses.
  • To explore the potential of VCP/p97 as a target for developing novel antiviral therapeutics.

Main Methods:

  • Review of existing literature on VCP/p97 interactions with viral life cycles.
  • Analysis of VCP/p97's known cellular functions and their relevance to viral replication stages.

Main Results:

  • VCP/p97 facilitates the replication of diverse RNA- and DNA-containing viruses.
  • This host protein participates in multiple stages of the viral life cycle, including entry, uncoating, and egress.

Conclusions:

  • Understanding VCP/p97's interactions with viruses offers insights into host-pathogen dynamics and viral mechanisms.
  • The essential role of VCP/p97 in viral replication presents a promising target for broad-spectrum antiviral drug development.